|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
70-1524 |
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: 2982.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 70 DWNVTWNTSNPDFTKCFQNTVLVWVPCFYLWACFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCWADLFYSFWER 149
Cdd:TIGR00957 11 DWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCWADLFYSFWER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 150 SRGIFLAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTALKEDAQVDLFRDITFY 229
Cdd:TIGR00957 91 SHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAIVDPFRDTTFY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 230 VYFSLLLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKEDTSEQVVPV 309
Cdd:TIGR00957 171 IYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 310 LVKNWKKECAKTRKQPVKVVYSSKDPAQPKESSKVDANEEVEALIVKSPQKEWNPSLFKVLYKTFGPYFLMSFFFKAIHD 389
Cdd:TIGR00957 251 LVENWKKECKKTRKQPVSAVYGKKDPSKPKGSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYFLMSFCFKAIHD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 390 LMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARK 469
Cdd:TIGR00957 331 LMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 470 SSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMK 549
Cdd:TIGR00957 411 SSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMK 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 550 SKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIDENNI 629
Cdd:TIGR00957 491 SKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNI 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 630 LDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGtNSITVRNATFTWARS 709
Cdd:TIGR00957 571 LDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEG-NSITVHNATFTWARD 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 710 DPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG------------------------------ 759
Cdd:TIGR00957 650 LPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsvayvpqqawiqndslrenilfgkalneky 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 -----------------------------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGM 810
Cdd:TIGR00957 730 yqqvleacallpdleilpsgdrteigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGV 809
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 811 LKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGVSGPGKEAKQM 890
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLI 889
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 891 ENGMLVTDSAGKQLQRQLSSSSSYSGDISRHHNSTAELQKAEAKkEETWKLMEADKAQTGQVKLSVYWDYMKAIGLFISF 970
Cdd:TIGR00957 890 ENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAK-EETWKLMEADKAQTGQVELSVYWDYMKAIGLFITF 968
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 971 LSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSI 1050
Cdd:TIGR00957 969 LSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNK 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1051 LRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVAS 1130
Cdd:TIGR00957 1049 LRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVAS 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1131 SRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAAL 1210
Cdd:TIGR00957 1129 SRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAAL 1208
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1211 FAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFR 1290
Cdd:TIGR00957 1209 FAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFR 1288
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1291 NYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQD 1370
Cdd:TIGR00957 1289 NYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQD 1368
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 PVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1450
Cdd:TIGR00957 1369 PVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1451 TAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMAKDAGL 1524
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
82-1523 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 954.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 82 FTKCFQNTVLVWVPCFYLWAcFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCWADLFY------SFWERSRGIFL 155
Cdd:PLN03130 29 YTPCATDSLVINISHLVLLG-LCLYRIWLIKKDHKVQRFCLRSKWYNYFLALLAAYCTAEPLFrlvmgiSVLNLDGQTSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 156 APVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTaLKedaqvDLFRDITFYVYFSLL 235
Cdd:PLN03130 108 PPFEIVSLIVEALTWCSMLVMIGVETKIYIREFRWYVRFAVIYVLVGDAVMLNLVLS-VK-----EYYSSFVLYLYISEV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 236 LIQLVLSCF-----------SDRSPLFSETIHD---------PNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLW 295
Cdd:PLN03130 182 AAQVLFGILllvyfpnldpyPGYTPIGSESVDDyeyeelpggEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 296 SLNKEDTSEQVVPVLVKNWKKECAKTrkqpvkvvysskdpaqpkesskvdaneevealivkspqkewNPSLFKVLYKTFG 375
Cdd:PLN03130 262 KLDTWDQTETLYRSFQKCWDEELKKP-----------------------------------------KPWLLRALNNSLG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 376 PYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNdTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGA 455
Cdd:PLN03130 301 GRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQ-NGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 456 VYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAV 535
Cdd:PLN03130 380 VFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 536 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVAL 615
Cdd:PLN03130 460 IISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 616 CTFAVYVTIDENniLDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEE--LEPDSierrPVKDGgg 693
Cdd:PLN03130 540 VSFGVFTLLGGD--LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvLLPNP----PLEPG-- 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 694 TNSITVRNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE-GHVAIKG------------ 759
Cdd:PLN03130 612 LPAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGtvayvpqvswif 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 -----------------------------------------------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 792
Cdd:PLN03130 692 natvrdnilfgspfdperyeraidvtalqhdldllpggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 793 DAHVGKHIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQda 872
Cdd:PLN03130 772 DAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYV-- 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 873 EENGvtGVSGPGKEAKQMENGmlvtdsAGKQLQRqlsssssysgdisrhhNSTAELQKAEAKKeetwKLMEADKAQTGQV 952
Cdd:PLN03130 848 EENG--EEEDDQTSSKPVANG------NANNLKK----------------DSSSKKKSKEGKS----VLIKQEERETGVV 899
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 953 KLSVYWDYMKAIGLFisFLSIFLFMC---NHVSALASNYWLSLWTDDpivNGTQEHTKV-RLSVYGALGISQGIAVFGYS 1028
Cdd:PLN03130 900 SWKVLERYKNALGGA--WVVMILFLCyvlTEVFRVSSSTWLSEWTDQ---GTPKTHGPLfYNLIYALLSFGQVLVTLLNS 974
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1029 MAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPI 1108
Cdd:PLN03130 975 YWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTI 1054
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1109 AAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIV 1188
Cdd:PLN03130 1055 SLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMS 1134
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1189 ANRWLAVRLECVGNCIVLFAALFAVI-----SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSE 1263
Cdd:PLN03130 1135 SNRWLAIRLETLGGLMIWLTASFAVMqngraENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYID 1214
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1264 TEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEG 1343
Cdd:PLN03130 1215 LPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERG 1294
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1344 EIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGEN 1423
Cdd:PLN03130 1295 RILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGEN 1374
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1424 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYG 1503
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFD 1454
|
1530 1540
....*....|....*....|.
gi 2462549072 1504 APSDLLQ-QRGLFYSMAKDAG 1523
Cdd:PLN03130 1455 TPENLLSnEGSAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
155-1523 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 870.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 155 LAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMT---ALKEDAQVDLFRDITFYVY 231
Cdd:PLN03232 107 LPPFEVASLMVEAFAWFSMLVLIGLETKQYVKEFRWYVRFGVVYVLVADAVLLDLVLPlknSINRTALYLCISSRCCQAL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 232 FSLLLIQLV--LSCFSDRSPLFSETIHD---------PNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKE 300
Cdd:PLN03232 187 FGILLLVYIpeLDPYPGYHILNNESLDNveydalrggENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQW 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 301 DTSEQVVPVLVKNWKKECAKtrkqpvkvvysskdpaqPKesskvdaneevealivkspqkewnPSLFKVLYKTFGPYFLM 380
Cdd:PLN03232 267 DQTETLIKRFQRCWTEESRR-----------------PK------------------------PWLLRALNNSLGGRFWL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 381 SFFFKAIHDLMMFSGPQILKLLIKFVNDTKaPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKA 460
Cdd:PLN03232 306 GGIFKIGHDLSQFVGPVILSHLLQSMQEGD-PAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKS 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 461 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKT 540
Cdd:PLN03232 385 LRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKM 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 541 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAV 620
Cdd:PLN03232 465 RKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGV 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 621 YVTIDENniLDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLR-IFLSHEELEPDSIERRPvkdggGTNSITV 699
Cdd:PLN03232 545 FVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEeLLLSEERILAQNPPLQP-----GAPAISI 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 700 RNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE-------GHVAI-------------- 757
Cdd:PLN03232 618 KNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirGSVAYvpqvswifnatvre 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 ---------------------------------------KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 798
Cdd:PLN03232 698 nilfgsdfeserywraidvtalqhdldllpgrdlteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 799 HIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVT 878
Cdd:PLN03232 778 QVFDSCM--KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDEN 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 879 GVSGPGKEAKQMENGMLVTDSAGKQLQRQLSssssysgdisrhhnstaelqkaeaKKEETwklmeadkaQTGQVKLSVYW 958
Cdd:PLN03232 856 ILKLGPTVTIDVSERNLGSTKQGKRGRSVLV------------------------KQEER---------ETGIISWNVLM 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 959 DYMKAIG-LFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQehTKVRLSVYGALGISQGIAVFGYSMAVSIGGIL 1037
Cdd:PLN03232 903 RYNKAVGgLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYS--PGFYIVVYALLGFGQVAVTFTNSFWLISSSLH 980
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1038 ASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLG 1117
Cdd:PLN03232 981 AAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLL 1060
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1118 LIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRL 1197
Cdd:PLN03232 1061 ILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRL 1140
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1198 ECVGNCIVLFAALFAVI-----SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQI 1272
Cdd:PLN03232 1141 ETLGGVMIWLTATFAVLrngnaENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAII 1220
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1273 QETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI 1352
Cdd:PLN03232 1221 ENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV 1300
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1353 AKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLV 1432
Cdd:PLN03232 1301 AKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLL 1380
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1433 CLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQR 1512
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
1450
....*....|..
gi 2462549072 1513 G-LFYSMAKDAG 1523
Cdd:PLN03232 1461 TsAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
365-1523 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 680.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 365 SLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVS 444
Cdd:PTZ00243 233 SLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRC 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 445 GMRIKTAVIGAVYRKALVITNS--ARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAG 522
Cdd:PTZ00243 313 GLQYRSALNALIFEKCFTISSKslAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 523 VAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVG 602
Cdd:PTZ00243 393 VAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVAT 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 603 TFTWVCTPFLVALCTFAVYVTIdeNNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHE------ 676
Cdd:PTZ00243 473 SFVNNATPTLMIAVVFTVYYLL--GHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDnatcst 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 677 --ELEPDSIERR---------------------PVK-------------------------------------------- 689
Cdd:PTZ00243 551 vqDMEEYWREQRehstacqlaavlenvdvtafvPVKlprapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygs 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 690 --------DGGGTNSITVRNATFTWARSDPPT-------------LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM 748
Cdd:PTZ00243 631 pssasrhiVEGGTGGGHEATPTSERSAKTPKMktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 749 DKVEGHV-------------------------------------AI----------------------KGVNLSGGQKQR 769
Cdd:PTZ00243 711 EISEGRVwaersiayvpqqawimnatvrgnilffdeedaarladAVrvsqleadlaqlgggleteigeKGVNLSGGQKAR 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 770 VSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYqel 849
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSS--- 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 850 lardgafAEFLRTyaSTEQEQDAEENGVTGVSGPGKEAKQMENGML---VTDSAGKQLQRQlsssssysgdisrhhnSTA 926
Cdd:PTZ00243 866 -------ADFMRT--SLYATLAAELKENKDSKEGDADAEVAEVDAApggAVDHEPPVAKQE----------------GNA 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 927 ELQKAEAKKEETWKLMEADKAQTGQVKLSVYWDYMKAIG-LFISFLSIFLFMCNHVSALASNYWLSLWTddpiVNGTQEH 1005
Cdd:PTZ00243 921 EGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELVTVSSGVWLSMWS----TRSFKLS 996
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1006 TKVRLSVYgaLGIS-QGIAVFGYSMAVSIGGI-LASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPE 1083
Cdd:PTZ00243 997 AATYLYVY--LGIVlLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPM 1074
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1084 VIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE 1163
Cdd:PTZ00243 1075 SYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYG 1154
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1164 EQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI------SRHSLsaGLVGLSVSYSLQVTTY 1237
Cdd:PTZ00243 1155 KAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIgtmlraTSQEI--GLVSLSLTMAMQTTAT 1232
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1238 LNWLVRMSSEMETNIVAVERLKEYS-ETEKEAPWQ-----------------------IQETAPPSSWP---QVGRVEFR 1290
Cdd:PTZ00243 1233 LNWLVRQVATVEADMNSVERLLYYTdEVPHEDMPEldeevdalerrtgmaadvtgtvvIEPASPTSAAPhpvQAGSLVFE 1312
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1291 NYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQD 1370
Cdd:PTZ00243 1313 GVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQD 1392
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 PVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK-TKILVLDE 1449
Cdd:PTZ00243 1393 PVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDE 1472
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1450 ATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQR-GLFYSMAKDAG 1523
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRqSIFHSMVEALG 1547
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
969-1262 |
9.36e-168 |
|
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: 505.86 E-value: 9.36e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 969 SFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQ--EHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDL 1046
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQdtEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1047 LHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRF 1126
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1127 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVL 1206
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 1207 FAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1262
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
381-669 |
1.38e-162 |
|
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: 491.60 E-value: 1.38e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 381 SFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKA 460
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 461 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKT 540
Cdd:cd18595 82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 541 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAV 620
Cdd:cd18595 162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462549072 621 YVTIDENNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd18595 242 YVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
262-1515 |
2.00e-136 |
|
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: 458.99 E-value: 2.00e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 262 PESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKEDTSEQVVPVLVKNWKKECAKTRKqpvkvvysskdpaqpkes 341
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKK------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 342 skvdaneevealivkspqkewNPSLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDW-QGYFYT 420
Cdd:TIGR01271 67 ---------------------NPKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEReIAYYLA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 421 V---LLFVtacLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMI 497
Cdd:TIGR01271 126 LglcLLFI---VRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 498 WSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 577
Cdd:TIGR01271 203 WIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAM 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 578 KDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIdENNILdaQTAFVSLALFNILRFPLN-ILPMVI 656
Cdd:TIGR01271 283 EKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI-KGIIL--RRIFTTISYCIVLRMTVTrQFPGAI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 657 SSIVQASVSLKRLRIFLSHEElepdsieRRPVKDGGGTNSITVRNATFTW----------------ARSDP--------- 711
Cdd:TIGR01271 360 QTWYDSLGAITKIQDFLCKEE-------YKTLEYNLTTTEVEMVNVTASWdegigelfekikqnnkARKQPngddglffs 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 712 -------PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV------------------AIK-------- 758
Cdd:TIGR01271 433 nfslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswimpgTIKdniifgls 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 759 ---------------------------------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVI 805
Cdd:TIGR01271 513 ydeyrytsvikacqleedialfpekdktvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 806 GPkgMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGV-------- 877
Cdd:TIGR01271 593 CK--LMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAERRNSIltetlrrv 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 878 ------TGVSGP------------------------------------GKEAKQME-NGM-------------LVTDS-- 899
Cdd:TIGR01271 671 sidgdsTVFSGPetikqsfkqpppefaekrkqsiilnpiasarkfsfvQMGPQKAQaTTIedavrepserkfsLVPEDeq 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 900 ------------AGKQLQ---RQ--LSSSSSYSGDISRHHNSTAELQKAEAKKEETWKLMEAD-----KAQTGQVKLS-- 955
Cdd:TIGR01271 751 geeslprgnqyhHGLQHQaqrRQsvLQLMTHSNRGENRREQLQTSFRKKSSITQQNELASELDiysrrLSKDSVYEISee 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 956 --------VYWDYMKAIGLFIS---------------FLSIFLFMCNHVSALASNYWLSLWTDDPIVNG--TQEHTKVR- 1009
Cdd:TIGR01271 831 ineedlkeCFADERENVFETTTwntylryittnrnlvFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNyvDQQHANASs 910
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1010 -LSVYGAL--------------GISQGIAVFGYSMAVSIGGIL--ASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSK 1072
Cdd:TIGR01271 911 pDVQKPVIitptsayyifyiyvGTADSVLALGFFRGLPLVHTLltVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTK 990
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1073 ELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNET 1152
Cdd:TIGR01271 991 DMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITS 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1153 LLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSY 1230
Cdd:TIGR01271 1071 LKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQDGEGEVGIILTL 1147
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1231 SLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAP--PSS------------WPQVGRVEFRNYCLRY 1296
Cdd:TIGR01271 1148 AMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKyqLSTvlvienphaqkcWPSGGQMDVQGLTAKY 1227
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1297 REDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSG 1376
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 SLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1456
Cdd:TIGR01271 1307 TFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1457 ETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLF 1515
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1285-1505 |
2.32e-134 |
|
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: 413.43 E-value: 2.32e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1285 GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1364
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1444
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1445 LVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1505
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
380-669 |
1.05e-125 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 393.12 E-value: 1.05e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 380 MSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRK 459
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 460 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMK 539
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 540 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFA 619
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462549072 620 VYVTIDENNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd18559 241 AYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
942-1520 |
7.78e-122 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 393.76 E-value: 7.78e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 942 MEADKAQTGQVKLSVYWDYMKAIglfisFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQG 1021
Cdd:COG1132 1 MSKSPRKLLRRLLRYLRPYRGLL-----ILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1022 IAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIV 1101
Cdd:COG1132 76 LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1102 ILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQK 1181
Cdd:COG1132 156 LFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1182 AYYPSIVANRWLAVRLECVGNCIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLK 1259
Cdd:COG1132 236 ANLRAARLSALFFPLMELLGNLGLALVLLVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1260 EYSETEKEAPWQIQETAPPsswPQVGRVEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFR 1336
Cdd:COG1132 316 ELLDEPPEIPDPPGAVPLP---PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVnllLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1337 INEsaeGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKL 1413
Cdd:COG1132 392 PTS---GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1414 DHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIV 1493
Cdd:COG1132 467 DTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILV 546
|
570 580
....*....|....*....|....*..
gi 2462549072 1494 LDKGEIQEYGAPSDLLQQRGLFYSMAK 1520
Cdd:COG1132 547 LDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
969-1262 |
1.31e-119 |
|
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: 376.55 E-value: 1.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 969 SFLSIFLFMCNHVSALASNYWLSLWTDDPiVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLH 1048
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDP-VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1049 SILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIpPLGLIYFFVQRFYV 1128
Cdd:cd18559 80 KALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGI-PLGLLYVPVNRVYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1129 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFA 1208
Cdd:cd18559 159 ASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1209 ALFAVISRHSLsAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1262
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 ... |
969-1262 |
6.55e-113 |
|
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: 358.35 E-value: 6.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 969 SFLSIFLFMCNHVSALASNYWLSLWTDDpIVNGTQEHTKVRLSVYGALGI-SQGIAVFGYSMAVSIGGILASRCLHVDLL 1047
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD-WSSSPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1048 HSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFY 1127
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1128 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1207
Cdd:cd18580 160 LRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1208 AALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1262
Cdd:cd18580 240 VALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
381-669 |
2.22e-112 |
|
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: 356.41 E-value: 2.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 381 SFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPD-WQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRK 459
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 460 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMK 539
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 540 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFA 619
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462549072 620 VYVTIDenNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
964-1262 |
2.31e-105 |
|
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: 337.14 E-value: 2.31e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 964 IGLFISFLSIFLFmcnhvSALASNYWLSLWTDDpivngtqehtKVRLS------VYGALGISQGIAVFGYSMAVSIGGIL 1037
Cdd:cd18606 1 LPLLLLLLILSQF-----AQVFTNLWLSFWTED----------FFGLSqgfyigIYAGLGVLQAIFLFLFGLLLAYLGIR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1038 ASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLG 1117
Cdd:cd18606 66 ASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1118 LIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRL 1197
Cdd:cd18606 146 VLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1198 ECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1262
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 ... |
1281-1505 |
2.12e-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: 2.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1281 WPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL 1360
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1361 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELahlkdfvsalpdkldhecAEGGENLSVGQRQLVCLARALLR 1440
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1441 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1505
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1045-1520 |
1.41e-94 |
|
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: 322.17 E-value: 1.41e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1045 DLLHSILRSPMSFFERTPSGNLVNRFSkELDTVDSMIPEVIKMFMGSLFNVIGACIVILL----ATPIAAIIIPPLGLIY 1120
Cdd:COG2274 234 RFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFysppLALVVLLLIPLYVLLG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1121 FFVQRFYVASSRQlkrlESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSIVANRWLAVr 1196
Cdd:COG2274 313 LLFQPRLRRLSRE----ESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnaRFKLRRLSNLLSTLSGL- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1197 LECVGNCIVLFAALFAVISRHsLSAG-LVGlSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiqET 1275
Cdd:COG2274 388 LQQLATVALLWLGAYLVIDGQ-LTLGqLIA-FNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPERE----EG 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1276 APPSSWPQV-GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGIN 1351
Cdd:COG2274 462 RSKLSLPRLkGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLkllLGLYEPTS---GRILIDGID 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1352 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQ 1428
Cdd:COG2274 539 LRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQ 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1429 RQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL 1508
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
490
....*....|..
gi 2462549072 1509 LQQRGLFYSMAK 1520
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; ... |
970-1262 |
2.45e-90 |
|
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: 295.15 E-value: 2.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 970 FLSIFLFMCNHVSALASNYWLSLWT---DDPIVNGTQEHTKVR-LSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVD 1045
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWAsayETSSALPPSEVSVLYyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1046 LLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQR 1125
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1126 FYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIV 1205
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1206 LFAALFAViSRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1262
Cdd:cd18604 242 FATAALLV-YGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
967-1261 |
2.22e-86 |
|
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: 284.04 E-value: 2.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 967 FISFLsIFLFMCnHVSALASNYWLSLWTD---DPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLH 1043
Cdd:cd18605 1 LILIL-LSLILM-QASRNLIDFWLSYWVShsnNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1044 VDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFV 1123
Cdd:cd18605 79 NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1124 QRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNC 1203
Cdd:cd18605 159 QRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1204 IVLFAALFAVISRH---SLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEY 1261
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 ... |
970-1262 |
2.09e-85 |
|
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: 281.80 E-value: 2.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 970 FLSIFLFMCNHVSALASNYWLSLWTD-----------DPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILA 1038
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEanhdvasvvfnITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1039 SRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGL 1118
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1119 IYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLE 1198
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 1199 CVGNCIVLFAALFAVISRH--SLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1262
Cdd:cd18602 242 YLGAVIVFLAALSSLTAALagYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1285-1520 |
1.85e-83 |
|
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: 274.09 E-value: 1.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1285 GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1364
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1444
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1445 LVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLL-QQRGLFYSMAK 1520
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVR 254
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
382-669 |
1.64e-77 |
|
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: 259.35 E-value: 1.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 382 FFFKAIHDLMMFSGPQILKLLIKFV-NDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKA 460
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 461 LVITNSA-------------------RKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLA 521
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 522 GVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAV 601
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 602 GTFTWVCTPFLVALCTFAVYVTIdENNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
380-669 |
4.15e-76 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 254.69 E-value: 4.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 380 MSFFFKAIHDLMMFSGPQILKLLIKFVNDTKA-----PDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIG 454
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 455 AVYRKALVITNSARKSSTVGEIVNLMSVDAQRfMDLA-TYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVN 533
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSR-IDFAlGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 534 AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLV 613
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 614 ALCTFAVYVTIdeNNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd18597 240 SMLSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
383-669 |
1.20e-75 |
|
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: 253.24 E-value: 1.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 383 FFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQY-FHICFVsGMRIKTAVIGAVYRKAL 461
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYnFQMNKV-SLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 462 VITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTK 541
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 542 TYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVY 621
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462549072 622 VTIdeNNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd18598 243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1285-1513 |
3.53e-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: 246.37 E-value: 3.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1285 GRVEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1364
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWT-SLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1443
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1444 ILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRG 1513
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1025-1513 |
4.94e-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: 258.15 E-value: 4.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1025 FGYSMAVSIGGILASRclhvdLLHSILRSPMSFFERTPSGNLVNRFskeLDTVDSMIPEVIKmFMGSLFNVIGACIVILL 1104
Cdd:COG4988 81 AAFRAAARVKRRLRRR-----LLEKLLALGPAWLRGKSTGELATLL---TEGVEALDGYFAR-YLPQLFLAALVPLLILV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1105 AT----PIAAIII----PplgLIYFFV----QRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF----EEQERF 1168
Cdd:COG4988 152 AVfpldWLSGLILlvtaP---LIPLFMilvgKGAAKASRRQWRALARLS-----GHFLDRLRGLTTLKLFgrakAEAERI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1169 IHQSD---------LKVdenqkAYYPSIVanrwlavrLECVGnciVLFAALFAVISRHSLSAGLVGLSVSYSL------- 1232
Cdd:COG4988 224 AEASEdfrkrtmkvLRV-----AFLSSAV--------LEFFA---SLSIALVAVYIGFRLLGGSLTLFAALFVlllapef 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1233 -----QVTTYlnWLVRMSsemetNIVAVERLKEYSETEKEAPWQIQETAPpssWPQVGRVEFRNYCLRYrEDLDFVLRHI 1307
Cdd:COG4988 288 flplrDLGSF--YHARAN-----GIAAAEKIFALLDAPEPAAPAGTAPLP---AAGPPSIELEDVSFSY-PGGRPALDGL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1308 NVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DP 1384
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1385 fsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQS 1464
Cdd:COG4988 437 --DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462549072 1465 TIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRG 1513
Cdd:COG4988 515 ALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1016-1518 |
7.42e-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: 255.03 E-value: 7.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1016 LGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNV 1095
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1096 IGACIVILLA----TPIAAIIIPPLGLIyffvqrfyvaSSRQLKRLESVSRSPVYSH------FNETLLGVSVIRAF--- 1162
Cdd:TIGR02203 143 IGLFIVLLYYswqlTLIVVVMLPVLSIL----------MRRVSKRLRRISKEIQNSMgqvttvAEETLQGYRVVKLFggq 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1163 -EEQERFIHQSD------LKVDENQKAYYPSI--VANRWLAVrlecvgnciVLFAALFAVISRHSLSAGLVGLSVSySLQ 1233
Cdd:TIGR02203 213 aYETRRFDAVSNrnrrlaMKMTSAGSISSPITqlIASLALAV---------VLFIALFQAQAGSLTAGDFTAFITA-MIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1234 VTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiQETAPPsswPQV-GRVEFRNYCLRYREDLDFVLRHINVTIN 1312
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD---TGTRAI---ERArGDVEFRNVTFRYPGRDRPALDSISLVIE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1313 GGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfSQYS 1389
Cdd:TIGR02203 357 PGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQAD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1390 DEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQ 1469
Cdd:TIGR02203 436 RAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1470 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLF---YSM 1518
Cdd:TIGR02203 516 MQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYaqlHNM 567
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1036-1520 |
2.49e-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: 250.45 E-value: 2.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1036 ILASrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIkmfmgslFNVIGACIVILLATPIAAIIIPP 1115
Cdd:COG4987 86 LLAD--LRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVL-------LPLLVALLVILAAVAFLAFFSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1116 LGLIYF------------FVQRFYVASSRQLKRLesvsRSPVYSHFNETLLGVSVIRAFEEQERFIHQsdlkVDENQKAY 1183
Cdd:COG4987 157 LALVLAlglllaglllplLAARLGRRAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALAR----LDAAEARL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1184 ypsiVANRWLAVRLECVGNCIVLFAALFAVI----------SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIV 1253
Cdd:COG4987 229 ----AAAQRRLARLSALAQALLQLAAGLAVVavlwlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1254 AVERLKEYSETEKeapwQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLG 1333
Cdd:COG4987 305 AARRLNELLDAPP----AVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1334 LFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALP 1410
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1411 DKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTR 1490
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDR 538
|
490 500 510
....*....|....*....|....*....|
gi 2462549072 1491 VIVLDKGEIQEYGAPSDLLQQRGLFYSMAK 1520
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, ... |
965-1262 |
1.09e-70 |
|
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: 239.77 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 965 GLFISFLSIFLFMCNHVSALASNYWLSLW---TDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGIL---- 1037
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLirgf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1038 --------ASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIA 1109
Cdd:cd18599 81 vfvkvtlrASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1110 AIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVA 1189
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1190 NRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1262
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
383-669 |
5.21e-69 |
|
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: 234.82 E-value: 5.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 383 FFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQ------------------GYFYTVLLFVTACLQTLVLHQYFHICFVS 444
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 445 GMRIKTAVIGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAG 522
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 523 VAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVG 602
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 603 TFTWVCTPFLVALCTFAVYVTIDENNiLDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
697-839 |
1.68e-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: 226.20 E-value: 1.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSD---PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI---------------- 757
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVpgsiayvsqepwiqng 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 -------------------------------------------KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 794
Cdd:cd03250 81 tirenilfgkpfdeeryekvikacalepdleilpdgdlteigeKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462549072 795 HVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQVDVIIVMSGGK 839
Cdd:cd03250 161 HVGRHIFENCILGLLL-NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1287-1518 |
1.76e-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: 224.42 E-value: 1.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1441
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1442 TKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
965-1262 |
5.93e-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: 217.57 E-value: 5.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 965 GLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHT----------------KVRLSVYGALGISQGIAVFGYS 1028
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRvqgenstnvdiedldrDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1029 MAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPI 1108
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1109 AAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIV 1188
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1189 ANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1262
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1287-1518 |
2.29e-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: 212.86 E-value: 2.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1441
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1442 TKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1287-1498 |
2.50e-62 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 209.93 E-value: 2.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLFSGSLRMNLdpfsqysdeevwtslelahlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKILV 1446
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1447 LDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1498
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1042-1518 |
1.49e-61 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 222.29 E-value: 1.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1042 LHVDLLHSILRSPMSFFERTPSGNLVNRFSKelDTvdsmipEVIK----MFMGSLFN---VIGACIVILLATP-----IA 1109
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTN--DT------EVIRdlyvTVVATVLRsaaLIGAMLVAMFSLDwrmalVA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1110 AIIIPPLGLIYFFVQRFyvaSSRQLKRLESVsRSPVYSHFNETLLGVSVIRAFEEQERFihqsDLKVDENQKAYYPSiva 1189
Cdd:PRK10790 172 IMIFPAVLVVMVIYQRY---STPIVRRVRAY-LADINDGFNEVINGMSVIQQFRQQARF----GERMGEASRSHYMA--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1190 nRWLAVRLE--CVGNCIVLFAALF--AVISRHSLSA-GLVGLSVSYSlqvttYLNWLVRMS----------SEMETNIVA 1254
Cdd:PRK10790 241 -RMQTLRLDgfLLRPLLSLFSALIlcGLLMLFGFSAsGTIEVGVLYA-----FISYLGRLNeplielttqqSMLQQAVVA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1255 VERLKEYseteKEAPWQI--QETAPPSSwpqvGRVEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLTL 1332
Cdd:PRK10790 315 GERVFEL----MDGPRQQygNDDRPLQS----GRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLAS 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1333 GLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDK 1412
Cdd:PRK10790 386 LLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDG 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1413 LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVI 1492
Cdd:PRK10790 466 LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTIL 545
|
490 500
....*....|....*....|....*.
gi 2462549072 1493 VLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:PRK10790 546 VLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1287-1520 |
2.70e-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: 207.01 E-value: 2.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRY--REDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1364
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALL 1439
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1440 RKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMA 1519
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 2462549072 1520 K 1520
Cdd:cd03249 236 K 236
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
396-669 |
1.37e-59 |
|
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: 207.10 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 396 PQILKLLIK-FVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVG 474
Cdd:cd18594 17 PLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSKITTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 475 EIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNR 554
Cdd:cd18594 97 HIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 555 IKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIdeNNILDAQT 634
Cdd:cd18594 177 VKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLT--GNTLTARK 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462549072 635 AFVSLALFNILRFPLNI-LPMVISSIVQASVSLKRL 669
Cdd:cd18594 255 VFTVISLLNALRMTITRfFPESIQTLSESRVSLKRI 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
360-867 |
7.71e-59 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 213.87 E-value: 7.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 360 KEWNPSLFKVLYKTFGPY---FLMSFFFKAIHDLMMFSGPQILKLLIKFVndTKAPDWQG-YFYTVLLFVTACLQTLVLH 435
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDAL--LAGGDLSAlLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 436 QYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD-LATYINMIWSAPLQVILALYLLWLN 514
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 515 LGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYA---WELA-FKDKVLAIRQEELK 590
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGreeRELErFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 591 VLKKSAYLSAVGTFtwVCTPFLVALCTFAVYVTIdeNNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLR 670
Cdd:COG1132 240 AARLSALFFPLMEL--LGNLGLALVLLVGGLLVL--SGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 671 IFLSHEELEPDSIERRPVKDGGGtnSITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 750
Cdd:COG1132 316 ELLDEPPEIPDPPGAVPLPPVRG--EIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 751 VEGHVAI------------------------------------------------------------------------- 757
Cdd:COG1132 393 TSGRILIdgvdirdltleslrrqigvvpqdtflfsgtirenirygrpdatdeeveeaakaaqahefiealpdgydtvvge 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSG 837
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDD 549
|
570 580 590
....*....|....*....|....*....|
gi 2462549072 838 GKISEMGSYQELLARDGAFAEFLRTYASTE 867
Cdd:COG1132 550 GRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1214-1518 |
1.32e-58 |
|
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: 213.91 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1214 ISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEapwqIQET--APPSSwPQVGRVEFRN 1291
Cdd:COG5265 288 VVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE----VADApdAPPLV-VGGGEVRFEN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1292 YCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDP 1371
Cdd:COG5265 363 VSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1372 VLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1446
Cdd:COG5265 442 VLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1447 LDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1010-1518 |
2.08e-57 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 213.05 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1010 LSVYGALGISQGIAVFGYSMAvsiggiLASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFM 1089
Cdd:TIGR00958 210 LSIASSVSAGLRGGSFNYTMA------RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1090 GSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQLKrlESVSRSPVYSHfnETLLGVSVIRAF--E 1163
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPrltmVTLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1164 EQE--RFIHQSDLKVDENQK---AYYPSIVANRWLAVRLECvgncIVLFAALFAVISRHSLSAGLVGLsVSYSLQVTTYL 1238
Cdd:TIGR00958 360 EGEasRFKEALEETLQLNKRkalAYAGYLWTTSVLGMLIQV----LVLYYGGQLVLTGKVSSGNLVSF-LLYQEQLGEAV 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1239 NWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPsswPQVGRVEFRNYCLRY--REDLDfVLRHINVTINGGEK 1316
Cdd:TIGR00958 435 RVLSYVYSGMMQAVGASEKVFEYLDRKPNIP-LTGTLAPL---NLEGLIEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEV 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1317 VGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWT 1395
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1396 SLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTirTQFEDCTV 1475
Cdd:TIGR00958 590 AAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTV 667
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2462549072 1476 LTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:TIGR00958 668 LLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
407-669 |
3.38e-57 |
|
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: 200.14 E-value: 3.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 407 NDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQR 486
Cdd:cd18593 30 NGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 487 FMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAmktktYQVAHMKSK-----DNRIKLMNEI 561
Cdd:cd18593 110 FDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-----KLFSKLRRKtaartDKRIRIMNEI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 562 LNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIDenNILDAQTAFVSLAL 641
Cdd:cd18593 185 INGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLG--NILTAERVFVTMAL 262
|
250 260
....*....|....*....|....*....
gi 2462549072 642 FNILRFPLNI-LPMVISSIVQASVSLKRL 669
Cdd:cd18593 263 YNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1285-1515 |
5.60e-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: 196.23 E-value: 5.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1285 GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGINIAKIGLHDLRFKI 1364
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1444
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1445 LVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLF 1515
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1285-1499 |
2.64e-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: 188.95 E-value: 2.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1285 GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHDLR 1361
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLkllAGLYK---PTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1362 FKITIIPQDPVLFSGSLRMNLDPFSQY-SDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1440
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1441 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEI 1499
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1287-1518 |
2.16e-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: 2.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1443
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1444 ILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
970-1238 |
5.78e-53 |
|
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: 187.46 E-value: 5.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 970 FLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQE--HTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLL 1047
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1048 HSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFY 1127
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1128 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1207
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 2462549072 1208 AALFAV--ISRHSLSAGLVGLSVSYSLQVTTYL 1238
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1046-1515 |
2.34e-52 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 194.85 E-value: 2.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1046 LLHSILRSPMSFFERTPSGNLVNRFskeldTVDSmiPEVIKMFMGSLFNVI--GACIVILLAT--------PIAAIIIPP 1115
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRI-----TYDS--EQVASSSSGALITVVreGASIIGLFIMmfyyswqlSLILIVIAP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1116 L--GLIYFFVQRFyvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERF------IHQSDLKVDENQKAY 1183
Cdd:PRK11176 177 IvsIAIRVVSKRF-----RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFggqeVETKRFdkvsnrMRQQGMKMVSASSIS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1184 YPSI--VANRWLAVrlecvgnciVLFAALFAVIsRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEY 1261
Cdd:PRK11176 252 DPIIqlIASLALAF---------VLYAASFPSV-MDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1262 --SETEKEAPWQIQETAPpsswpqvGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE 1339
Cdd:PRK11176 322 ldLEQEKDEGKRVIERAK-------GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1340 SAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFS--QYSDEEVWTSLELAHLKDFVSALPDKLDHEC 1417
Cdd:PRK11176 395 IDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVI 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1418 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKG 1497
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
|
490
....*....|....*...
gi 2462549072 1498 EIQEYGAPSDLLQQRGLF 1515
Cdd:PRK11176 555 EIVERGTHAELLAQNGVY 572
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
380-669 |
9.37e-52 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 184.30 E-value: 9.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 380 MSFFFKAIHDLMMFSGPQIL-KLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYR 458
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 459 KALVITNSARKSstVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAM 538
Cdd:cd18592 81 KILRLRSLGDKS--VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 539 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTF 618
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 619 AVYVTIDENniLDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd18592 239 LAHVALGND--LTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1050-1525 |
1.75e-49 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 186.71 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1050 ILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEvikmFMGSLFNVIGAcIVILLATPIA-----AIIIPPLGLIYFFVQ 1124
Cdd:PRK13657 99 IIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLE----FMREHLATLVA-LVVLLPLALFmnwrlSLVLVVLGIVYTLIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1125 RFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF---EEQERFIHQSdlkVDENQKAYYPsiVANRW-LAVRLECV 1200
Cdd:PRK13657 174 TLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnriEAETQALRDI---ADNLLAAQMP--VLSWWaLASVLNRA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1201 GNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSS 1280
Cdd:PRK13657 249 ASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVP-DVRDPPGAID 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1281 WPQV-GRVEFRNYCLRYR------EDLDFvlrhinvTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA 1353
Cdd:PRK13657 328 LGRVkGAVEFDDVSFSYDnsrqgvEDVSF-------EAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1354 KIGLHDLRFKITIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQ 1428
Cdd:PRK13657 401 TVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1429 RQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL 1508
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
490
....*....|....*..
gi 2462549072 1509 LQQRGLFYSMAKDAGLV 1525
Cdd:PRK13657 557 VARGGRFAALLRAQGML 573
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1047-1518 |
2.44e-48 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 185.33 E-value: 2.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1047 LHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMG-SLFNVIGACIV---------ILLATPIAAIIIppl 1116
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDmWILVIVGLFLVrqnmllfllSLLSIPVYAVII--- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1117 gliYFFVQRFYVASSRQLKrlesvSRSPVYSHFNETLLGVSVIRAF-EEQERFIHQSDLKVDENQKA--YYPSIVANRWL 1193
Cdd:TIGR01193 313 ---ILFKRTFNKLNHDAMQ-----ANAVLNSSIIEDLNGIETIKSLtSEAERYSKIDSEFGDYLNKSfkYQKADQGQQAI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1194 AVRLECVGNCIVLFAALFAVIsRHSLSAGLVglsVSYSLQVTTYLNWL---VRMSSEMETNIVAVERLKE--YSETEKEA 1268
Cdd:TIGR01193 385 KAVTKLILNVVILWTGAYLVM-RGKLTLGQL---ITFNALLSYFLTPLeniINLQPKLQAARVANNRLNEvyLVDSEFIN 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1269 PWQIQETAPPSSWPQVGRVEFR-NYClryredlDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1347
Cdd:TIGR01193 461 KKKRTELNNLNGDIVINDVSYSyGYG-------SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1348 DGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ--YSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLS 1425
Cdd:TIGR01193 534 NGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSIS 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1426 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIrTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1505
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSH 692
|
490
....*....|...
gi 2462549072 1506 SDLLQQRGLFYSM 1518
Cdd:TIGR01193 693 DELLDRNGFYASL 705
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1015-1482 |
3.01e-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: 178.71 E-value: 3.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1015 ALGISQgiAVFGY-SMAVSIGGILASRC-LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIkmfmgsl 1092
Cdd:TIGR02868 61 AFGIGR--AVFRYlERLVGHDAALRSLGaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1093 FNVIGACIVILLATPIAAIIIPPLGLI--------YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEE 1164
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALIlaaglllaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1165 QERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQVTTYLNWLV 1242
Cdd:TIGR02868 212 LPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGpaVADGRLAPVTLAVLVLLPLAAFEAFAALP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1243 RMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSSwPQVGRVEFRNYCLRYrEDLDFVLRHINVTINGGEKVGIVGR 1322
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVG-LGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1323 TGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLEL 1399
Cdd:TIGR02868 370 SGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALER 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1400 AHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIA 1479
Cdd:TIGR02868 448 VGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLIT 527
|
...
gi 2462549072 1480 HRL 1482
Cdd:TIGR02868 528 HHL 530
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
420-861 |
1.22e-46 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 180.42 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 420 TVLLFVTACLQTL--VLHQYF--HIcfvsGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNlmsvdaqRFMDLATYIN 495
Cdd:COG2274 199 AIGLLLALLFEGLlrLLRSYLllRL----GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-------RFRDVESIRE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 496 MIWSAPLQVILAlyllwlnlGPSVLAGVAVM-----------VLMVPVNAVMA------MKTKTYQVAHMKSKDNRikLM 558
Cdd:COG2274 268 FLTGSLLTALLD--------LLFVLIFLIVLffyspplalvvLLLIPLYVLLGllfqprLRRLSREESEASAKRQS--LL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 559 NEILNGIKVLKLYA--------WELAFKDKVLAirqeELKVLKKSAYLSAVGTFtwvctpfLVALCTFAVYVT----IDE 626
Cdd:COG2274 338 VETLRGIETIKALGaesrfrrrWENLLAKYLNA----RFKLRRLSNLLSTLSGL-------LQQLATVALLWLgaylVID 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 627 NNI-LDAQTAFVSLalfnILRF--PLNILPMVISSIVQASVSLKRLRIFLSHEeLEPDSiERRPVKDGGGTNSITVRNAT 703
Cdd:COG2274 407 GQLtLGQLIAFNIL----SGRFlaPVAQLIGLLQRFQDAKIALERLDDILDLP-PEREE-GRSKLSLPRLKGDIELENVS 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 704 FTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----------------LAEMDKVE-----GHV------ 755
Cdd:COG2274 481 FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlglyeptsgrilidgidLRQIDPASlrrqiGVVlqdvfl 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 756 -----------------------AIK----------------------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 790
Cdd:COG2274 561 fsgtirenitlgdpdatdeeiieAARlaglhdfiealpmgydtvvgegGSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 791 AVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLR 861
Cdd:COG2274 641 ALDAETEAIILENL---RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1051-1520 |
1.38e-44 |
|
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: 173.60 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1051 LRSPMSFFERTPSGNLVNRFSKeLDTVDSMIPEV-IKMFMGSLFNVIG-----------ACIVILLATPIAAIIippLGL 1118
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGStLTTLLSGIFALLNlglmfyyswklALVAVALALVAIAVT---LVL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1119 IYFFVQRfyvasSRQLKRLESVSRSPVYSHFNetllGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLe 1198
Cdd:TIGR03797 296 GLLQVRK-----ERRLLELSGKISGLTVQLIN----GISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFN- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1199 cVGNCIVLFAALFAVISRHSLSAGL-VGLSVSYSLQVTTYLNWLVRMSSEMeTNIVAV----ERLKEYSETEKEAPwqiQ 1273
Cdd:TIGR03797 366 -AVLPVLTSAALFAAAISLLGGAGLsLGSFLAFNTAFGSFSGAVTQLSNTL-ISILAViplwERAKPILEALPEVD---E 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1274 ETAPPSswPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSL---TLGlFRINESaeGEIIIDGI 1350
Cdd:TIGR03797 441 AKTDPG--KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLlrlLLG-FETPES--GSVFYDGQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1351 NIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQ 1430
Cdd:TIGR03797 516 DLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1431 LVCLARALLRKTKILVLDEATAAVDLETDDLI-QSTIRTQfedCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLL 1509
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVsESLERLK---VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM 672
|
490
....*....|.
gi 2462549072 1510 QQRGLFYSMAK 1520
Cdd:TIGR03797 673 AREGLFAQLAR 683
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1285-1499 |
7.73e-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: 7.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1285 GRVEFRNYCLRYREDLD-FVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFK 1363
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1364 ITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKT 1442
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1443 KILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEI 1499
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1307-1518 |
9.97e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 169.26 E-value: 9.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1307 INVTINGGEKVGIVGRTGAGKSSLT---LGLFrineSAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL- 1382
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLnalLGFL----PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 --DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD 1460
Cdd:PRK11174 445 lgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1461 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1022-1494 |
3.10e-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: 163.61 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1022 IAVFGYSMAVSIGGILASRC-------LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDS----MIPEVIKMFMG 1090
Cdd:TIGR02857 52 LVLLLRALLGWLQERAAARAaaavksqLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGyfarYLPQLVLAVIV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1091 SLfnVIGAciVILLATPIAAIII---PPLgLIYFFVQRFYVASSRQLKRLESVSRspVYSHFNETLLGVSVIRAF----E 1163
Cdd:TIGR02857 132 PL--AILA--AVFPQDWISGLILlltAPL-IPIFMILIGWAAQAAARKQWAALSR--LSGHFLDRLRGLPTLKLFgrakA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1164 EQERFIHQSD---------LKVdenqkAYYPS------------IVAnRWLAVRLecVGNCIVLFAALFAVISRHSLSAG 1222
Cdd:TIGR02857 205 QAAAIRRSSEeyrertmrvLRI-----AFLSSavlelfatlsvaLVA-VYIGFRL--LAGDLDLATGLFVLLLAPEFYLP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1223 LVGLSVSY--SLQVTTylnwlvrmSSEMETNIVAVERLKEYSETEKEApwqiqetAPPSSwpqvgrVEFRNYCLRYrEDL 1300
Cdd:TIGR02857 277 LRQLGAQYhaRADGVA--------AAEALFAVLDAAPRPLAGKAPVTA-------APASS------LEFSGVSVAY-PGR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1301 DFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRM 1380
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NL---DPFSqySDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1457
Cdd:TIGR02857 415 NIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
490 500 510
....*....|....*....|....*....|....*..
gi 2462549072 1458 TDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVL 1494
Cdd:TIGR02857 493 TEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
378-649 |
6.71e-41 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 152.41 E-value: 6.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 378 FLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQ-GYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAV 456
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 457 YRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSV-LAGVAVMVLMVPVNAV 535
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 536 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKV-LKKSAYLSAVGTFTWVCTPFLVA 614
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 2462549072 615 LCTFAVYVTIDENNiLDAQTAFVSLALFNILRFPL 649
Cdd:pfam00664 241 LALWFGAYLVISGE-LSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1252-1518 |
4.48e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.06 E-value: 4.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1252 IVAVERLKEYSETEKEAPWQIQETAPPSSwpqvGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT 1331
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAADQ----VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1332 LGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSA 1408
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1409 lPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTI--M 1486
Cdd:PRK11160 462 -DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqF 540
|
250 260 270
....*....|....*....|....*....|..
gi 2462549072 1487 DytRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:PRK11160 541 D--RICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
697-839 |
2.73e-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: 144.06 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleslrkniay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSY 825
Cdd:cd03228 81 vpqdpflfsgtireniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLST 157
|
170
....*....|....
gi 2462549072 826 LPQVDVIIVMSGGK 839
Cdd:cd03228 158 IRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
519-861 |
3.10e-39 |
|
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: 155.31 E-value: 3.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 519 VLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSkDNRIKLMnEILNGIKVLKLY-AWElAFKDKVLAIRQEELKVLKKSAY 597
Cdd:COG4987 161 LALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYgALD-RALARLDAAEARLAAAQRRLAR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 598 LSAVGTF-TWVCTPFLVALCTFAVYVTIDENNILDAQTA---FVSLALFNILRfPLnilPMVISSIVQASVSLKRLRIFL 673
Cdd:COG4987 238 LSALAQAlLQLAAGLAVVAVLWLAAPLVAAGALSGPLLAllvLAALALFEALA-PL---PAAAQHLGRVRAAARRLNELL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 674 SHEELEPDSIERRPVKDGGgtnSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 753
Cdd:COG4987 314 DAPPAVTEPAEPAPAPGGP---SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 754 HVAIKGV------------------------------------------------------------------------- 760
Cdd:COG4987 391 SITLGGVdlrdldeddlrrriavvpqrphlfdttlrenlrlarpdatdeelwaalervglgdwlaalpdgldtwlgeggr 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPkgmLKNKTRILVTHSMSYLPQVDVIIVMSGGKI 840
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA---LAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
410 420
....*....|....*....|.
gi 2462549072 841 SEMGSYQELLARDGAFAEFLR 861
Cdd:COG4987 548 VEQGTHEELLAQNGRYRQLYQ 568
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1287-1512 |
5.42e-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: 5.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLTL---GLFRINEsaeGEIIIDGINIAKIGLHDLRFK 1363
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRllnGLLKPTS---GEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1364 ITIIPQDPV--LFSGSLR-------MNLdpfsQYSDEE----VWTSLELAHLKDFvsalpdkLDHECAEggenLSVGQRQ 1430
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEedvafgpENL----GLPREEirerVEEALELVGLEHL-------ADRPPHE----LSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1431 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1508
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREV 221
|
....
gi 2462549072 1509 LQQR 1512
Cdd:COG1122 222 FSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1288-1498 |
5.62e-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: 130.28 E-value: 5.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1288 EFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITII 1367
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1368 PQDP------------VLFsgSLRmNLdpfsQYSDEEVWTSLELAhLKDFvsALPDKLDHECAEggenLSVGQRQLVCLA 1435
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NL----GLPEEEIEERVEEA-LELV--GLEGLRDRSPFT----LSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1436 RALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGE 1498
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1287-1503 |
9.21e-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: 127.62 E-value: 9.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFV--LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRF-- 1362
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1363 -KITIIPQDPvlfSGSL--RMN-----LDPF------SQYSDEEVWTSLELAHLKDfVSALPDKLDHEcaeggenLSVGQ 1428
Cdd:cd03257 82 kEIQMVFQDP---MSSLnpRMTigeqiAEPLrihgklSKKEARKEAVLLLLVGVGL-PEEVLNRYPHE-------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1429 RQLVCLARALLRKTKILVLDEATAAVDLETDDLIQST---IRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYG 1503
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 ... |
1288-1499 |
1.10e-32 |
|
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: 125.41 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1288 EFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHDLRFKI 1364
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLArliLGLLR---PTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFSGSLRMNLdpfsqysdeevwtslelahlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKI 1444
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 1445 LVLDEATAAVDLETDDLIQSTI-RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEI 1499
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1288-1498 |
2.77e-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: 123.51 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1288 EFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITII 1367
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1368 PQdpvlfsgslrmnldpfsqysdeevwtslelahlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVL 1447
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1448 DEATAAVDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGE 1498
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1286-1509 |
4.63e-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: 126.31 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1286 RVEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKIT 1365
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1366 IIPQDPVL-FSGSLR----M----NLDPFSQYSDEE---VWTSLELAHLKDFVsalpdklDHECAEggenLSVGQRQLVC 1433
Cdd:COG1120 79 YVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1434 LARALLRKTKILVLDEATAAVDL----ETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDL 1508
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
.
gi 2462549072 1509 L 1509
Cdd:COG1120 226 L 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1287-1511 |
7.38e-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: 131.95 E-value: 7.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGINIAKIGLHDLRFK 1363
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1364 ITIIPQDP------------VLFsgSLRMNLDPFSQySDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQL 1431
Cdd:COG1123 85 IGMVFQDPmtqlnpvtvgdqIAE--ALENLGLSRAE-ARARVLELLEAVGLERRLDRYP----HQ-------LSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1432 VCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1508
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEI 230
|
...
gi 2462549072 1509 LQQ 1511
Cdd:COG1123 231 LAA 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1287-1503 |
7.39e-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: 123.19 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKIGlHDLRFKIT 1365
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTGDLKPqQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1366 IIPQDPVLFSGSLRMNLdpfsqysdeevwtslelahlkdfvsalpdkldhecaegGENLSVGQRQLVCLARALLRKTKIL 1445
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1446 VLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYG 1503
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
697-858 |
9.56e-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: 124.65 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWarsDP--PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI----------------- 757
Cdd:cd03253 1 IEFENVTFAY---DPgrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtldslrrai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 --------------------------------------------------------KGVNLSGGQKQRVSLARAVYSNAD 781
Cdd:cd03253 78 gvvpqdtvlfndtigynirygrpdatdeevieaakaaqihdkimrfpdgydtivgeRGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 782 IYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 858
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
672-854 |
1.41e-31 |
|
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: 131.80 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 672 FLSHEELEPDSIERRPVKDGGgtNSITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKV 751
Cdd:COG4988 314 LLDAPEPAAPAGTAPLPAAGP--PSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 752 EGHVAI-------------------------------------------------------------------------K 758
Cdd:COG4988 391 SGSILIngvdlsdldpaswrrqiawvpqnpylfagtirenlrlgrpdasdeeleaaleaagldefvaalpdgldtplgeG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 759 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGG 838
Cdd:COG4988 471 GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
250
....*....|....*.
gi 2462549072 839 KISEMGSYQELLARDG 854
Cdd:COG4988 548 RIVEQGTHEELLAKNG 563
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
998-1518 |
2.96e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 130.99 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 998 IVNGTQEHTKVRLSVYGALGISQGIAV-------------FG--YSMAVSiggilasrcLHVDLLHSILRSPMSFFERTP 1062
Cdd:PRK10789 21 IVDGVTEQHMTTGQILMWIGTMVLIAVvvyllryvwrvllFGasYQLAVE---------LREDFYRQLSRQHPEFYLRHR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1063 SGNLVNRFSKELDTVDSMIPEVIKMFMGSLfnVIGACIVILLAT--------------PIAAIIIPPLGLIYFfvQRFYV 1128
Cdd:PRK10789 92 TGDLMARATNDVDRVVFAAGEGVLTLVDSL--VMGCAVLIVMSTqiswqltllallpmPVMAIMIKRYGDQLH--ERFKL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1129 ASSrqlkrlesvSRSPVYSHFNETLLGVSVIRAFEEQErfiHQS----DLKVDENQKAYYPSIVANRWLAVRLECVGnci 1204
Cdd:PRK10789 168 AQA---------AFSSLNDRTQESLTSIRMIKAFGLED---RQSalfaADAEDTGKKNMRVARIDARFDPTIYIAIG--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1205 vlFAALFAV------ISRHSLSAGlvglsvsyslQVTTYLNWLVRMSSEMET-----NIV-----AVERLKEYSEtekEA 1268
Cdd:PRK10789 233 --MANLLAIgggswmVVNGSLTLG----------QLTSFVMYLGLMIWPMLAlawmfNIVergsaAYSRIRAMLA---EA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1269 PWQIQETAPPSSWPQVGRVEFRNYClrYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1348
Cdd:PRK10789 298 PVVKDGSEPVPEGRGELDVNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1349 GINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLS 1425
Cdd:PRK10789 376 DIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1426 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1505
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNH 533
|
570
....*....|...
gi 2462549072 1506 SDLLQQRGLFYSM 1518
Cdd:PRK10789 534 DQLAQQSGWYRDM 546
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1304-1452 |
9.11e-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: 118.90 E-value: 9.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSG-SLRMNL 1382
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1383 -------DPFSQYSDEEVWTSLELAhlkdfvsALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1452
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 ... |
697-838 |
1.11e-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: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------------- 755
Cdd:cd03290 1 VQVTNGYFSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsrnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 756 -------------------------------------------------------AIKGVNLSGGQKQRVSLARAVYSNA 780
Cdd:cd03290 80 svayaaqkpwllnatveenitfgspfnkqrykavtdacslqpdidllpfgdqteiGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 781 DIYLFDDPLSAVDAHVGKHIFEnvigpKGMLK-----NKTRILVTHSMSYLPQVDVIIVMSGG 838
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1287-1511 |
2.26e-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: 127.71 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRN----YCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHD 1359
Cdd:COG1123 261 LEVRNlskrYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1360 LRFKITIIPQDPvlfSGSL--RMN--------LDPFSQYSDEEVW----TSLELAHL-KDFVSALPdkldHEcaeggenL 1424
Cdd:COG1123 340 LRRRVQMVFQDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERRervaELLERVGLpPDLADRYP----HE-------L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1425 SVGQRQLVCLARALLRKTKILVLDEATAAVDLetddLIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKG 1497
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYIAdRVAVMYDG 481
|
250
....*....|....
gi 2462549072 1498 EIQEYGAPSDLLQQ 1511
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 ... |
1303-1511 |
3.99e-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: 127.46 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1382
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 DPFSQYSD-EEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD- 1460
Cdd:TIGR01842 413 ARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQa 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1461 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:TIGR01842 493 LANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
749-1522 |
8.16e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 129.38 E-value: 8.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 749 DKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDaHVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQ 828
Cdd:PTZ00265 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 829 VDVIIVMSGgkiSEMGSYQELlarDGAFAEFLRTYASTEQEQDAEENGVTGVS---------------GPGKEAKQMENG 893
Cdd:PTZ00265 646 ANTIFVLSN---RERGSTVDV---DIIGEDPTKDNKENNNKNNKDDNNNNNNNnnnkinnagsyiieqGTHDALMKNKNG 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 894 MLVT----------DSAGKQLQRQLSSSSSYSGDISRHH-------NSTAELQKAEAKKEETWKLMEADKAQTGQvKLS- 955
Cdd:PTZ00265 720 IYYTminnqkvsskKSSNNDNDKDSDMKSSAYKDSERGYdpdemngNSKHENESASNKKSCKMSDENASENNAGG-KLPf 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 956 -----------------VY---WDYMKAIGlfISFLSIFLF--MCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVY 1013
Cdd:PTZ00265 799 lrnlfkrkpkapnnlriVYreiFSYKKDVT--IIALSILVAggLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIA 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1014 GALGISQGIAVFgYSMAVsigGILASRCLHVDLLHSILRSPMSFFER---TPsGNLVNRFSKELDTVDSMIPEVIKMFMG 1090
Cdd:PTZ00265 877 IAMFISETLKNY-YNNVI---GEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTH 951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1091 SLFNVIGACIVILLATPIAAIIippLGLIYFFVQRFYVASSR-------QLKRLESVSRSPVYSH-----------FNET 1152
Cdd:PTZ00265 952 FIVLFLVSMVMSFYFCPIVAAV---LTGTYFIFMRVFAIRARltankdvEKKEINQPGTVFAYNSddeifkdpsflIQEA 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1153 LLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFA--VISRHSLSAGLVGLSVSY 1230
Cdd:PTZ00265 1029 FYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGsfLIRRGTILVDDFMKSLFT 1108
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1231 SLQVTTYLNWLVRMSSEMETNIVAVERL------KEYSETEKEAPWQIQETAPPSswpqvGRVEFRNYCLRY--REDLDf 1302
Cdd:PTZ00265 1109 FLFTGSYAGKLMSLKGDSENAKLSFEKYypliirKSNIDVRDNGGIRIKNKNDIK-----GKIEIMDVNFRYisRPNVP- 1182
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSL--------------------------------------TLGLFRINESA--- 1341
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVmsllmrfydlkndhhivfknehtndmtneqdyqgdeeqNVGMKNVNEFSltk 1262
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1342 -------------EGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQ--YSDEEVWTSLELAHLKDFV 1406
Cdd:PTZ00265 1263 eggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKRACKFAAIDEFI 1341
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1407 SALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNT 1484
Cdd:PTZ00265 1342 ESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIAS 1421
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 2462549072 1485 IMDYTRVIVLDKGE-----IQEYGAPSDLLQ-QRGLFYSMAKDA 1522
Cdd:PTZ00265 1422 IKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQDGVYKKYVKLA 1465
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1282-1498 |
5.26e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.07 E-value: 5.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1282 PQVGRVEFRNYCLRY--REDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGINIAKIGLH 1358
Cdd:PTZ00265 378 KDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1359 DLRFKITIIPQDPVLFSGSLRMN----------LDPFSQYSDEE---------------------------VWTSLELAH 1401
Cdd:PTZ00265 457 WWRSKIGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYYNEDgndsqenknkrnscrakcagdlndmsnTTDSNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1402 LK---------------------DFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD 1460
Cdd:PTZ00265 537 MRknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462549072 1461 LIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1498
Cdd:PTZ00265 617 LVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
698-839 |
1.33e-28 |
|
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: 113.11 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 698 TVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN---------------- 761
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDiaklpleelrrrigyv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 --LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENVIgpKGML-KNKTRILVTHSMSYLPQV-DVIIVMSG 837
Cdd:cd00267 79 pqLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELL--RELAeEGRTVIIVTHDPELAELAaDRVIVLKD 155
|
..
gi 2462549072 838 GK 839
Cdd:cd00267 156 GK 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1287-1498 |
1.92e-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: 114.10 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRY---REDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLfrINESA--EGEIIIDGiniakiglhdlr 1361
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEklSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1362 fKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1441
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 1442 TKILVLDEATAAVDLETDDLIqstirtqFEDC---------TVLTIAHRLNTIMDYTRVIVLDKGE 1498
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1288-1503 |
2.15e-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: 113.30 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1288 EFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITII 1367
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1368 PQdpVLfsgslrmnldpfsqysdeevwTSLELAHLKD-FVSalpdkldhecaeggeNLSVGQRQLVCLARALLRKTKILV 1446
Cdd:cd03214 79 PQ--AL---------------------ELLGLAHLADrPFN---------------ELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1447 LDEATAAVDL----ETDDLIQSTIRTqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYG 1503
Cdd:cd03214 121 LDEPTSHLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1287-1510 |
3.60e-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: 114.90 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLD--FVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1364
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPvlfSGSL--RMNLD-----PFS----QYSDEEVWTSLELAHLKDfvsALPDKLDHEcaeggenLSVGQRQLVC 1433
Cdd:COG1124 82 QMVFQDP---YASLhpRHTVDrilaePLRihglPDREERIAELLEQVGLPP---SFLDRYPHQ-------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1434 LARALLRKTKILVLDEATAAVDL----ETDDLIQStIRTQfEDCTVLTIAHRLNTImDY--TRVIVLDKGEIQEYGAPSD 1507
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVsvqaEILNLLKD-LREE-RGLTYLFVSHDLAVV-AHlcDRVAVMQNGRIVEELTVAD 225
|
...
gi 2462549072 1508 LLQ 1510
Cdd:COG1124 226 LLA 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1287-1514 |
4.21e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.42 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGINIAK----IG--- 1356
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLlkaILGLLPP---TSGTVRLFGKPPRRarrrIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1357 ---LHDLRFKITIipQDPVLfsgslrMNLDP----FSQYSDEE---VWTSLELAHLKDF----VSALpdkldhecaegge 1422
Cdd:COG1121 82 qraEVDWDFPITV--RDVVL------MGRYGrrglFRRPSRADreaVDEALERVGLEDLadrpIGEL------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1423 nlSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIq 1500
Cdd:COG1121 141 --SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRGLV- 217
|
250
....*....|....
gi 2462549072 1501 EYGAPSDLLQQRGL 1514
Cdd:COG1121 218 AHGPPEEVLTPENL 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
697-840 |
4.50e-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: 111.92 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpnelgdhvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKgmLKNKTRILVTHSMSY 825
Cdd:cd03246 81 lpqddelfsgsiaeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK--AAGATRIVIAHRPET 158
|
170
....*....|....*
gi 2462549072 826 LPQVDVIIVMSGGKI 840
Cdd:cd03246 159 LASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1287-1508 |
2.87e-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: 111.50 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINES-----AEGEIIIDGINIAKIGLHD-- 1359
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1360 LRFKITIIPQDPVLFSGSLRMNLDpfsqYS------------DEEVWTSLELAHLKDFVSalpDKLDhecaegGENLSVG 1427
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA----YGlrlhgiklkeelDERVEEALRKAALWDEVK---DRLH------ALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1428 QRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNT---IMDYTrvIVLDKGEIQEYGA 1504
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADRT--AFLLNGRLVEFGP 223
|
....
gi 2462549072 1505 PSDL 1508
Cdd:cd03260 224 TEQI 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1303-1511 |
3.95e-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: 118.31 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRineSAEGEIIIDGINIA-----KIGLHdlrfkITIIPQDPVLF 1374
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLarlLVGVWP---PTAGSVRLDGADLSqwdreELGRH-----IGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1375 SGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1454
Cdd:COG4618 419 DGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1455 DLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:COG4618 499 DDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1233-1497 |
4.42e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.37 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1233 QVTTYLNWLVRMSSEMeTNIVA-VERLKEYSETEKEAPwQIQETAPPSSWPQVGRVEFRNYCLRyREDLDFVLRHINVTI 1311
Cdd:COG4178 310 QVQGALSWFVDNYQSL-AEWRAtVDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1312 NGGEKVGIVGRTGAGKSSLtlglFR----INESAEGEIIidginiakigLHDLRfKITIIPQDPVLFSGSLRMNL---DP 1384
Cdd:COG4178 387 KPGERLLITGPSGSGKSTL----LRaiagLWPYGSGRIA----------RPAGA-RVLFLPQRPYLPLGTLREALlypAT 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1385 FSQYSDEEVWTSLELAHLKDFVsalpDKLDHEcAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQS 1464
Cdd:COG4178 452 AEAFSDAELREALEAVGLGHLA----ERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
250 260 270
....*....|....*....|....*....|....
gi 2462549072 1465 TIRTQFEDCTVLTIAHRlNTIMDY-TRVIVLDKG 1497
Cdd:COG4178 527 LLREELPGTTVISVGHR-STLAAFhDRVLELTGD 559
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
697-861 |
1.35e-26 |
|
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: 109.94 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------- 761
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsqig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------------------------------------LSGGQKQRVSLARAVYSNADI 782
Cdd:cd03249 81 lvsqepvlfdgtiaenirygkpdatdeeveeaakkanihdfimslpdgydtlvgergsqLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 783 YLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLR 861
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1302-1513 |
1.37e-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: 109.95 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1302 FVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRfKITIIPQDPVLFSG-SLRM 1380
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGVLPDERGLYDRlTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NLD---PFSQYSDEEVWTSLE-LAHLKDfvsaLPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1456
Cdd:COG4555 94 NIRyfaELYGLFDEELKKRIEeLIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1457 ETDDLIQSTIRTQF-EDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQRG 1513
Cdd:COG4555 166 MARRLLREILRALKkEGKTVLFSSHIMQEVEALCdRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1036-1258 |
1.46e-26 |
|
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: 112.20 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1036 ILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPP 1115
Cdd:cd18600 99 ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1116 LGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERF---IHQSdlkVDENQKAYYPSIVANRW 1192
Cdd:cd18600 179 VIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFetlFHKA---LNLHTANWFLYLSTLRW 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1193 LAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1258
Cdd:cd18600 256 FQMRIEMI---FVIFftAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
697-858 |
3.36e-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: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI------------------- 757
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytlaslrrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 ------------------------------------------------------KGVNLSGGQKQRVSLARAVYSNADIY 783
Cdd:cd03251 81 vsqdvflfndtvaeniaygrpgatreeveeaaraanahefimelpegydtvigeRGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 784 LFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 858
Cdd:cd03251 161 ILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1288-1497 |
2.21e-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: 105.69 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1288 EFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIglhdlRFKI 1364
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLkaiLGLLK---PTSGSIRVFGKPLEKE-----RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQD-------PVLFSGSLRMNLDP----FSQYSDEE---VWTSLELAHLKDFVSAlpdKLDHecaeggenLSVGQRQ 1430
Cdd:cd03235 71 GYVPQRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSELADR---QIGE--------LSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1431 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1497
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFdRVLLLNRT 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1303-1509 |
2.58e-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: 106.13 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFKITIIPQDPVLFSG--- 1376
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLSSrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 ----SLRMNLDPFSQ-YSDEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1451
Cdd:cd03258 100 fenvALPLEIAGVPKaEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1452 AAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1509
Cdd:cd03258 169 SALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1287-1499 |
2.74e-25 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 105.65 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLD--FVLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLfrINESAEGEIIIDGINIAKIGLHDL-- 1360
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVRVDGTDISKLSEKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1361 --RFKITIIPQD---------------PVLFSGSLRMnldpfsqySDEEVWTSLeLAHLKdfvsaLPDKLDHECAEggen 1423
Cdd:cd03255 79 frRRHIGFVFQSfnllpdltalenvelPLLLAGVPKK--------ERRERAEEL-LERVG-----LGDRLNHYPSE---- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1424 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEI 1499
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1287-1499 |
1.03e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 102.48 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGINIAKIGlHDLRFK 1363
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIkiiLGLLKPDS---GEIKVLGKDIKKEP-EEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1364 ITIIPQDPVLfsgslrmnldpfsqYSDEEVWTSLELahlkdfvsalpdkldhecaeggenlSVGQRQLVCLARALLRKTK 1443
Cdd:cd03230 75 IGYLPEEPSL--------------YENLTVRENLKL-------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1444 ILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEI 1499
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1287-1509 |
1.87e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 104.69 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDP-VLFSGSLRMNLDPFS----QYSDEEVWTS-LELAHlkdfVSALPDKLDHEcaegGENLSVGQRQLVCLARALLR 1440
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGlenkKVPPKKMKDIiDDLAK----KVGMEDYLDKE----PQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1441 KTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1288-1512 |
2.22e-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: 103.80 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1288 EFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHDLRFKI 1364
Cdd:cd03256 2 EVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDP-----------VLfSGSL-RMNLDP--FSQYSDEEVWTSLELahLKDFvsALPDKLDHECAEggenLSVGQRQ 1430
Cdd:cd03256 81 GMIFQQFnlierlsvlenVL-SGRLgRRSTWRslFGLFPKEEKQRALAA--LERV--GLLDKAYQRADQ----LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1431 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSD 1507
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYAdRIVGLKDGRIVFDGPPAE 231
|
....*
gi 2462549072 1508 LLQQR 1512
Cdd:cd03256 232 LTDEV 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
696-861 |
2.54e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.53 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------- 761
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseaalrqais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 783
Cdd:PRK11160 418 vvsqrvhlfsatlrdnlllaapnasdealievlqqvgleklleddkglnawlgeggrqLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 784 LFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLR 861
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELL---AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1287-1510 |
3.01e-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: 102.97 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAK---IGLHDL 1360
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLrliVGLLR---PDSGEVLIDGEDISGlseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1361 RFKITIIPQDPVLFSG-SLRMN----LDPFSQYSDEE----VWTSLELAHLKDFVSALPDkldhecaeggeNLSVGQRQL 1431
Cdd:cd03261 76 RRRMGMLFQSGALFDSlTVFENvafpLREHTRLSEEEireiVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1432 VCLARALLRKTKILVLDEATAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIM---DytRVIVLDKGEIQEYGA 1504
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHDLDTAFaiaD--RIAVLYDGKIVAEGT 220
|
....*.
gi 2462549072 1505 PSDLLQ 1510
Cdd:cd03261 221 PEELRA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1287-1498 |
1.48e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 99.18 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLH--DLRFKI 1364
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFSgslRMNldpfsqysdeeVWTSLELAhlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKI 1444
Cdd:cd03229 79 GMVFQDFALFP---HLT-----------VLENIALG-----------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1445 LVLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGE 1498
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1287-1504 |
1.82e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFK 1363
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1364 ITIIPQDP-----------VLFsgSLR-MNLDPfsQYSDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQL 1431
Cdd:COG2884 81 IGVVFQDFrllpdrtvyenVAL--PLRvTGKSR--KEIRRRVREVLDLVGLSDKAKALP----HE-------LSGGEQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1432 VCLARALLRKTKILVLDEATAAVDLET-DDLIQstirtQFED-----CTVLtIA-HRLNTIMDY-TRVIVLDKGEIQEYG 1503
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETsWEIME-----LLEEinrrgTTVL-IAtHDLELVDRMpKRVLELEDGRLVRDE 219
|
.
gi 2462549072 1504 A 1504
Cdd:COG2884 220 A 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
712-868 |
3.75e-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: 101.09 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 712 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV------------------AIK--------------- 758
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisfssqfswimpgTIKeniifgvsydeyryk 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 759 --------------------------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPkgMLK 812
Cdd:cd03291 131 svvkacqleeditkfpekdntvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 813 NKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQ 868
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQ 264
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1286-1511 |
1.07e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.70 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1286 RVEFRNYclRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHDLRF 1362
Cdd:PRK13635 7 RVEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL---PEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1363 KITIIPQDP------------VLFSgsLRMNLDPFSQYSdEEVWTSLELAHLKDFvsalpdkLDHECAeggeNLSVGQRQ 1430
Cdd:PRK13635 82 QVGMVFQNPdnqfvgatvqddVAFG--LENIGVPREEMV-ERVDQALRQVGMEDF-------LNREPH----RLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1431 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL 1508
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
...
gi 2462549072 1509 LQQ 1511
Cdd:PRK13635 228 FKS 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
697-844 |
1.09e-22 |
|
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: 96.61 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsdlekalsslisvl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIgpkGMLKNKTRILVTHSM 823
Cdd:cd03247 81 nqrpylfdttlrnnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHL 157
|
170 180
....*....|....*....|.
gi 2462549072 824 SYLPQVDVIIVMSGGKISEMG 844
Cdd:cd03247 158 TGIEHMDKILFLENGKIIMQG 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1294-1512 |
3.30e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.13 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1294 LRYREDlDFVLRhINVTINGGEKVGIVGRTGAGKSSLtLGL---FRinESAEGEIIIDGINIAKIGLHDlRfKITIIPQD 1370
Cdd:COG3840 7 LTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTL-LNLiagFL--PPDSGRILWNGQDLTALPPAE-R-PVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 PVLFSG-SLRMN----LDPFSQYSDEE---VWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKT 1442
Cdd:COG3840 80 NNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1443 KILVLDEATAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQR 1512
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 ... |
1287-1503 |
3.40e-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: 96.43 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDGINIAKIGLHdlRF 1362
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTL-LrliaGLERP---DSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1363 KITIIPQDPVLF----------SGsLRMNLDPFSQySDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLV 1432
Cdd:cd03259 73 NIGMVFQDYALFphltvaeniaFG-LKLRGVPKAE-IRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1433 CLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYG 1503
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1304-1514 |
4.80e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.20 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA--KIGLHDLRFKITIIPQDP--VLFS---- 1375
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1376 -----GSLRMNLdpfsqySDEE----VWTSLELAHLKdfVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILV 1446
Cdd:PRK13637 103 kdiafGPINLGL------SEEEienrVKRAMNIVGLD--YEDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1447 LDEATAAVDLETDDLIQSTIRTQFE--DCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPS------DLLQQRGL 1514
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRevfkevETLESIGL 244
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
696-840 |
5.75e-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: 5.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI------------------ 757
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpadlrrnig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 -------------------------------------------------------KGVNLSGGQKQRVSLARAVYSNADI 782
Cdd:cd03245 82 yvpqdvtlfygtlrdnitlgapladderilraaelagvtdfvnkhpngldlqigeRGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 783 YLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKI 840
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 ... |
699-839 |
8.12e-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: 95.23 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 699 VRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN----------------- 761
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrkvglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDP 788
Cdd:cd03225 82 qnpddqffgptveeevafglenlglpeeeieerveealelvgleglrdrspftLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 789 LSAVDAHVGKHIFEnvigpkgMLK-----NKTRILVTHSMSYLPQV-DVIIVMSGGK 839
Cdd:cd03225 162 TAGLDPAGRRELLE-------LLKklkaeGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
649-881 |
1.89e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 100.56 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 649 LNILPMV----ISSIVQ-ASVSLKRLRIFLSHEELEPDSIErrPVKDGGGTNSITVRnaTFTWARSDPPTLNGITFSIPE 723
Cdd:PRK10789 265 LMIWPMLalawMFNIVErGSAAYSRIRAMLAEAPVVKDGSE--PVPEGRGELDVNIR--QFTYPQTDHPALENVNFTLKP 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 724 GALVAVVGQVGCGKSSLLSALLAEMDKVEG-------------------------------------------------- 753
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDVSEGdirfhdipltklqldswrsrlavvsqtpflfsdtvannialgrpdatqqe 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 754 -----------------------HVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGM 810
Cdd:PRK10789 421 iehvarlasvhddilrlpqgydtEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL---RQW 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 811 LKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRtYASTEQEQDAEENGVTGVS 881
Cdd:PRK10789 498 GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR-YQQLEAALDDAPEIREEAV 567
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
697-854 |
2.31e-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: 94.60 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALL------------------------------- 745
Cdd:cd03254 3 IEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMrfydpqkgqilidgidirdisrkslrsmigv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 746 ----------------------AEMDKV--------------------EGHVAIKGVNLSGGQKQRVSLARAVYSNADIY 783
Cdd:cd03254 82 vlqdtflfsgtimenirlgrpnATDEEVieaakeagahdfimklpngyDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 784 LFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDG 854
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 ... |
697-857 |
2.46e-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: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL---------------------------------LSA 743
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLtkliqrfyvpengrvlvdghdlaladpawlrrqVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 744 LLAE--------------------MDKV-----------------EGH---VAIKGVNLSGGQKQRVSLARAVYSNADIY 783
Cdd:cd03252 81 VLQEnvlfnrsirdnialadpgmsMERVieaaklagahdfiselpEGYdtiVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 784 LFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFA 857
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
378-669 |
2.46e-21 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 96.08 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 378 FLMSFFFKAIHDLMMFSGPQILKLLIKFVndTKAPDWQGYFYTVLLFVTAC-LQTLVLHQYFHICFVSGMRIKTAVIGAV 456
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLAlLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 457 YRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATY-INMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAV 535
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 536 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWE----LAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPF 611
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRAARLSALFSPLIGLLTALGTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 612 LVALctFAVYVTIDENniLDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 669
Cdd:cd07346 239 LVLL--YGGYLVLQGS--LTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
697-840 |
3.94e-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: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGVN------------ 761
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGTDisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -------------------------------------------------------------LSGGQKQRVSLARAVYSNA 780
Cdd:cd03255 80 rrrhigfvfqsfnllpdltalenvelplllagvpkkerreraeellervglgdrlnhypseLSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 781 DIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQVDVIIVMSGGKI 840
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVME-------LLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
714-840 |
9.44e-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: 90.92 E-value: 9.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------------------------- 761
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDikkepeevkrrigylpeepslyenltvrenlk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVIgpKGMLK-NKTRILVTHSMSYLPQV-DVIIVMSGGK 839
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELKKeGKTILLSSHILEEAERLcDRVAILNNGR 172
|
.
gi 2462549072 840 I 840
Cdd:cd03230 173 I 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1287-1511 |
1.25e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.14 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFV--LRHINVTINGGEKVGIVGRTGAGKSSLtlglFR-IN--ESA-EGEIIIDGINIAKI---GL 1357
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTL----IRcINllERPtSGSVLVDGVDLTALserEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1358 HDLRFKITIIPQDPVLFSgslrmnldpfsqysdeevwtS----------LELAHLK------------DFVSaLPDKLDH 1415
Cdd:COG1135 78 RAARRKIGMIFQHFNLLS--------------------SrtvaenvalpLEIAGVPkaeirkrvaellELVG-LSDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1416 ECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD----DLIQStIRTQFeDCTVLTIAHRLN---TIMDy 1488
Cdd:COG1135 137 YPSQ----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDvvrRICD- 209
|
250 260
....*....|....*....|...
gi 2462549072 1489 tRVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:COG1135 210 -RVAVLENGRIVEQGPVLDVFAN 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
672-861 |
1.26e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 672 FLSHEELEPDSIERRPVKDGGgtNSITVRNATFTwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMdKV 751
Cdd:PRK11174 327 FLETPLAHPQQGEKELASNDP--VTIEAEDLEIL-SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 752 EGHVAIKGVNL--------------------------------------------------------------------- 762
Cdd:PRK11174 403 QGSLKINGIELreldpeswrkhlswvgqnpqlphgtlrdnvllgnpdasdeqlqqalenawvseflpllpqgldtpigdq 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 763 ----SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGG 838
Cdd:PRK11174 483 aaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL---NAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|...
gi 2462549072 839 KISEMGSYQELLARDGAFAEFLR 861
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLA 582
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1287-1512 |
2.80e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.99 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHDLRFKI 1364
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDP--VLFSGSLR-------MNLdpfsQYSDEEVWTSLELAHLKDFVSALPDKLDHEcaeggenLSVGQRQLVCLA 1435
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNL----KLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1436 RALLRKTKILVLDEATAAVD-LETDDLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQR 1512
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCdNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1287-1508 |
2.94e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPV-LFSGS---------LRMNLDPFSQYSdEEVWTSLELAHLKdfvsalpDKLDHEcaegGENLSVGQRQLVCLAR 1436
Cdd:PRK13648 88 VFQNPDnQFVGSivkydvafgLENHAVPYDEMH-RRVSEALKQVDML-------ERADYE----PNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1437 ALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL 1508
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1303-1499 |
3.41e-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: 89.02 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQdpvlfsgslrmn 1381
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1382 ldpfsqysdeevwtslelahlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL-ETDD 1460
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462549072 1461 LIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEI 1499
Cdd:cd03216 121 LFKVIRRLRAQGVAVIFISHRLDEVFEIAdRVTVLRDGRV 160
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1286-1467 |
4.93e-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: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1286 RVEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGINIAKIGlHDLRF 1362
Cdd:COG4133 2 MLEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLlrILaGLLPP---SAGEVLWNGEPIRDAR-EDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1363 KITIIPQDPVLFSG-SLRMNLDpFSQ------YSDEEVWTSLELAHLKDFvsalpdkLDHECAeggeNLSVGQRQLVCLA 1435
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR-FWAalyglrADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|..
gi 2462549072 1436 RALLRKTKILVLDEATAAVDLETDDLIQSTIR 1467
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
697-863 |
6.31e-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: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:COG1121 7 IELENLTV--SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrrigyvpqra 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -------------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFD 786
Cdd:COG1121 85 evdwdfpitvrdvvlmgrygrrglfrrpsradreavdealervgledladrpigeLSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 787 DPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRILVTHSMSYLPQ-VDVIIVMSGGKISEmGSYQELLARDgafaEFL 860
Cdd:COG1121 165 EPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTPE----NLS 232
|
...
gi 2462549072 861 RTY 863
Cdd:COG1121 233 RAY 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
697-861 |
6.56e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 95.86 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDlrdytlaslrnqval 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------------------------------------LSGGQKQRVSLARAVYSNADI 782
Cdd:PRK11176 422 vsqnvhlfndtianniayarteqysreqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 783 YLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLR 861
Cdd:PRK11176 502 LILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHK 577
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
658-852 |
8.31e-20 |
|
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: 95.20 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 658 SIVQASVSLKRLRIFLSHEELEPDSIER-RPvkdgggTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCG 736
Cdd:COG4618 297 QFVSARQAYRRLNELLAAVPAEPERMPLpRP------KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 737 KSSLLSALL----------------------------------------------------AEMDKV------------- 751
Cdd:COG4618 371 KSTLARLLVgvwpptagsvrldgadlsqwdreelgrhigylpqdvelfdgtiaeniarfgdADPEKVvaaaklagvhemi 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 752 ----EG---HVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVIgpkGMLK--NKTRILVTHS 822
Cdd:COG4618 451 lrlpDGydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAALAAAI---RALKarGATVVVITHR 526
|
250 260 270
....*....|....*....|....*....|
gi 2462549072 823 MSYLPQVDVIIVMSGGKISEMGSYQELLAR 852
Cdd:COG4618 527 PSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1303-1510 |
9.31e-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: 9.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQDPVLFSG-SLRM 1380
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NLD--PFSQYSDEEVWTsleLAHLKDFVSALPDKLDHEcaegGENLSVGQRQLVCLARALLRKTKILVLDEATAA----- 1453
Cdd:cd03224 95 NLLlgAYARRRAKRKAR---LERVYELFPRLKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGlapki 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1454 VDlETDDLIQsTIRTqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQ 1510
Cdd:cd03224 168 VE-EIFEAIR-ELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
635-862 |
1.29e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.03 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 635 AFVSLALFNILRfplniLPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGG-TNSITVRNATFTWARSdPPT 713
Cdd:PRK13657 277 AFVGFATLLIGR-----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRvKGAVEFDDVSFSYDNS-RQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------------------------- 761
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtvtraslrrniavvfqdaglfnrsiednir 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG--- 797
Cdd:PRK13657 431 vgrpdatdeemraaaeraqahdfierkpdgydtvvgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEakv 510
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 798 KHIFENVigpkgmLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRT 862
Cdd:PRK13657 511 KAALDEL------MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
698-840 |
1.46e-19 |
|
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: 87.88 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 698 TVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN---------------- 761
Cdd:cd03214 1 EVENLSV--GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkelarkiayv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHS 822
Cdd:cd03214 79 pqalellglahladrpfneLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARE-RGKTVVMVLHD 157
|
170
....*....|....*....
gi 2462549072 823 MSYLPQV-DVIIVMSGGKI 840
Cdd:cd03214 158 LNLAARYaDRVILLKDGRI 176
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1303-1518 |
1.65e-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: 91.27 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDGINIAKIG---LHDLRFK-ITIIPQDPvlfs 1375
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLAraiLGLLPPPGITSGEILFDGEDLLKLSekeLRKIRGReIQMIFQDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1376 gslrMN-LDP--------------FSQYSDEEVWT----SLELAHL---KDFVSALPdkldHEcaeggenLSVGQRQLVC 1433
Cdd:COG0444 96 ----MTsLNPvmtvgdqiaeplriHGGLSKAEAREraieLLERVGLpdpERRLDRYP----HE-------LSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1434 LARALLRKTKILVLDEATAAVDLetddLIQSTI-------RTQFeDCTVLTIAHRLNT---IMDytRVIVLDKGEIQEYG 1503
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDLGVvaeIAD--RVAVMYAGRIVEEG 233
|
250 260
....*....|....*....|.
gi 2462549072 1504 APSDLLQQ------RGLFYSM 1518
Cdd:COG0444 234 PVEELFENprhpytRALLSSI 254
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
648-858 |
2.43e-19 |
|
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: 94.12 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 648 PLNILPMVISSIVQASVSLKRLriF-LSHEELEP-DSIERRPVKDGGGTnsITVRNATFTWarsDP--PTLNGITFSIPE 723
Cdd:COG5265 311 PLNFLGFVYREIRQALADMERM--FdLLDQPPEVaDAPDAPPLVVGGGE--VRFENVSFGY---DPerPILKGVSFEVPA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 724 GALVAVVGQVGCGKSSLlSALL------------------------------------------------------AEMD 749
Cdd:COG5265 384 GKTVAIVGPSGAGKSTL-ARLLfrfydvtsgrilidgqdirdvtqaslraaigivpqdtvlfndtiayniaygrpdASEE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 750 KVEGhvAIK----------------------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigp 807
Cdd:COG5265 463 EVEA--AARaaqihdfieslpdgydtrvgerGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL--- 537
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 808 KGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 858
Cdd:COG5265 538 REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1287-1509 |
3.15e-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: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYReDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLFSG-SLRMN--LDP-FSQYSDEEVWT-SLELAHLKDFVSA-LPDKLDHEcaeggenLSVGQRQLVCLARALLR 1440
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIRErADELLALVGLDPAeFADRYPHE-------LSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1441 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDC--TVLTIAHRLN-TIMDYTRVIVLDKGEIQEYGAPSDLL 1509
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
697-839 |
3.43e-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: 86.86 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTwaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:cd03229 1 LELKNVSKR--YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplrrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKnKTRILV 819
Cdd:cd03229 79 gmvfqdfalfphltvlenialgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLG-ITVVLV 157
|
170 180
....*....|....*....|.
gi 2462549072 820 THSMSYLPQV-DVIIVMSGGK 839
Cdd:cd03229 158 THDLDEAARLaDRVVVLRDGK 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1304-1511 |
3.55e-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: 93.21 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGINIAKIG---LHDLRFKITIIPQDPvlFsGSL-- 1378
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1379 RMN-----------LDPfsQYSDEE----VWTSLELAHLKdfvsalPDKLD---HEcaeggenLSVGQRQLVCLARALLR 1440
Cdd:COG4172 378 RMTvgqiiaeglrvHGP--GLSAAErrarVAEALEEVGLD------PAARHrypHE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1441 KTKILVLDEATAAVDLetddliqsTIRTQfedctVLT---------------IAHRLN---TIMDytRVIVLDKGEIQEY 1502
Cdd:COG4172 443 EPKLLVLDEPTSALDV--------SVQAQ-----ILDllrdlqrehglaylfISHDLAvvrALAH--RVMVMKDGKVVEQ 507
|
....*....
gi 2462549072 1503 GAPSDLLQQ 1511
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 ... |
1287-1480 |
4.15e-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: 87.53 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDF--VLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGINIAKIGLHdlr 1361
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLlriIAGLERP---TSGEVLVDGEPVTGPGPD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1362 fkITIIPQDPVLF---------SGSLRMNLDPFSQySDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQLV 1432
Cdd:cd03293 75 --RGYVFQQDALLpwltvldnvALGLELQGVPKAE-ARERAEELLELVGLSGFENAYP----HQ-------LSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1433 CLARALLRKTKILVLDEATAAVDLETDDLIQSTI-----RTQFedcTVLTIAH 1480
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTH 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
697-839 |
4.69e-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: 85.19 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------LSGGQKQR 769
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVkigyfeqLSGGEKMR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 770 VSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENvigpkgMLKN--KTRILVTHSMSYLPQV-DVIIVMSGGK 839
Cdd:cd03221 79 LALAKLLLENPNLLLLDEPTNHLDLE-SIEALEE------ALKEypGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
697-842 |
9.52e-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: 9.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGVN------------ 761
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGQDisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -------------------------------------------------------------LSGGQKQRVSLARAVYSNA 780
Cdd:COG1136 84 rrrhigfvfqffnllpeltalenvalplllagvsrkerrerarellervglgdrldhrpsqLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 781 DIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQVDVIIVMSGGKISE 842
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
697-876 |
1.14e-18 |
|
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: 91.50 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVAIKGVN------------ 761
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAlmgLLPHGGRISGEVLLDGRDllelsealrgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 783
Cdd:COG1123 85 igmvfqdpmtqlnpvtvgdqiaealenlglsraeararvlelleavglerrldryphqLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 784 LFDDPLSAVDAHVGKHIFEnVIGPKGMLKNKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARDGAFAEFLRT 862
Cdd:COG1123 165 IADEPTTALDVTTQAEILD-LLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAPQALAAVPRL 243
|
250
....*....|....
gi 2462549072 863 YASTEQEQDAEENG 876
Cdd:COG1123 244 GAARGRAAPAAAAA 257
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1287-1509 |
1.14e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 87.06 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLtLGLF--RINESAEGEIIIDGINIAKIGLHDLRFKI 1364
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTL-LSLItgDLPPTYGNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 ---------TIIPQDPVL------FSGSLrmnlDPFSQYSDEEV-----W-TSLELAHLKD--FVSalpdkldhecaegg 1421
Cdd:COG1119 81 glvspalqlRFPRDETVLdvvlsgFFDSI----GLYREPTDEQRerareLlELLGLAHLADrpFGT-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1422 enLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMD-YTRVIVLDKGE 1498
Cdd:COG1119 143 --LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDGR 220
|
250
....*....|.
gi 2462549072 1499 IQEYGAPSDLL 1509
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1287-1524 |
1.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.93 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSS---LTLGLFRINESAEGEIIIDGINIAKIGLHDLRFK 1363
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1364 ITIIPQDP-VLFSGSLRMNLDPFS----QYSDEE----VWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCL 1434
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGlenrAVPRPEmikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1435 ARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQR 1512
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
250
....*....|..
gi 2462549072 1513 glfySMAKDAGL 1524
Cdd:PRK13640 235 ----EMLKEIGL 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1287-1501 |
1.45e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.25 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLD--FVLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFrinESA-EGEIIIDGINIAKIG---LH 1358
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILGGL---DRPtSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1359 DLRF-KITIIPQDPvlfsgslrmNLDPFsqYSDEE-VWTSLELAHLKDFVSA-----------LPDKLDHECAEggenLS 1425
Cdd:COG1136 82 RLRRrHIGFVFQFF---------NLLPE--LTALEnVALPLLLAGVSRKERRerarellervgLGDRLDHRPSQ----LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1426 VGQRQLVCLARALLRKTKILVLDEATAAVDLETD----DLIQSTIRTQfeDCTVLTIAH--RLNTIMDytRVIVLDKGEI 1499
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHdpELAARAD--RVIRLRDGRI 222
|
..
gi 2462549072 1500 QE 1501
Cdd:COG1136 223 VS 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1287-1499 |
1.47e-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: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLdFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAkiGLHD-----LR 1361
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1362 FKITIIPQDPVLFSG---------SLRMNLDPfSQYSDEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLV 1432
Cdd:cd03292 78 RKIGVVFQDFRLLPDrnvyenvafALEVTGVP-PREIRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1433 CLARALLRKTKILVLDEATAAVDLETDDLIqSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEI 1499
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKagTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1298-1508 |
2.04e-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: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1298 EDLDF------VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLHDLRFKI 1364
Cdd:COG1117 15 RNLNVyygdkqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPDVDVVELRRRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFSGS--------LRMNLDPFSQYSDEEVWTSLELAHLKDFVSalpDKLDhecaEGGENLSVGQRQLVCLAR 1436
Cdd:COG1117 95 GMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALWDEVK---DRLK----KSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1437 ALLRKTKILVLDEATAAVD-LETD---DLIQStIRtqfEDCTVLTIAHRLNT---IMDYTrvIVLDKGEIQEYGAPSDL 1508
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDpISTAkieELILE-LK---KDYTIVIVTHNMQQaarVSDYT--AFFYLGELVEFGPTEQI 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1304-1507 |
2.06e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.70 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFKITIIPQDPVLFSgslrm 1380
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKARRQIGMIFQHFNLLS----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 nldpfSQYSDEEVWTSLELAHL-KDFVSA----------LPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDE 1449
Cdd:PRK11153 96 -----SRTVFDNVALPLELAGTpKAEIKArvtellelvgLSDKADRYPA----QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1450 ATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRlntiMDYT-----RVIVLDKGEIQEYGAPSD 1507
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRElgLTIVLITHE----MDVVkricdRVAVIDAGRLVEQGTVSE 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1287-1514 |
2.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.09 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLD-FVLRHINVTINGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGINIAKIGLHDLRF 1362
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL---EAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1363 KITIIPQDP-VLFSGSLRMNLDPFS--------QYSDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVC 1433
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGlenkgiphEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1434 LARALLRKTKILVLDEATAAVDLETD-DLIQS--TIRTQFeDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL-- 1508
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELfs 229
|
250
....*....|
gi 2462549072 1509 ----LQQRGL 1514
Cdd:PRK13650 230 rgndLLQLGL 239
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
970-1258 |
2.14e-18 |
|
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: 87.61 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 970 FLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHS 1049
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1050 ILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQR 1125
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWkltlVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1126 FYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVG 1201
Cdd:cd07346 162 RIRKASREVR--ESLAE--LSAFLQESLSGIRVVKAFaaeeREIERFREANRDLRDANLRAARLSALFSPLIGL-LTALG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1202 NCIVLFAALFAVIsRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1258
Cdd:cd07346 237 TALVLLYGGYLVL-QGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1310-1509 |
2.61e-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: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1310 TINGGEKVGIVGRTGAGKSslTLG--LFRINESAEGEIIIDGINIAKIG---LHDLRFKITIIPQDPvlfSGSL--RMNL 1382
Cdd:COG4608 40 DIRRGETLGLVGESGCGKS--TLGrlLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 -----DPFsqysdeEVWTSLELAHLKDFVSAL-------PDKLD---HEcaeggenLSVGQRQLVCLARALLRKTKILVL 1447
Cdd:COG4608 115 gdiiaEPL------RIHGLASKAERRERVAELlelvglrPEHADrypHE-------FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1448 DEATAAVDLEtddlIQSTIRTQFED------CTVLTIAHRLNT---IMDytRVIVLDKGEIQEYGaPSDLL 1509
Cdd:COG4608 182 DEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLSVvrhISD--RVAVMYLGKIVEIA-PRDEL 245
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
714-840 |
2.89e-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: 83.63 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--VN-----------------LSGGQKQRVSLAR 774
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSfasprdarragiamvyqLSVGERQMVEIAR 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 775 AVYSNADIYLFDDPLSAVDAHVGKHIFEnVIgpkGMLKN--KTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFK-VI---RRLRAqgVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1304-1497 |
2.98e-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: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL----RFKITIIPQDPVLFSGSLR 1379
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1380 MNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-T 1458
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462549072 1459 DDLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKG 1497
Cdd:cd03290 177 DHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
518-835 |
4.03e-18 |
|
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: 89.65 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 518 SVLAGVAVMV--LMVPV-NAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAI----RQEELK 590
Cdd:TIGR02857 143 DWISGLILLLtaPLIPIfMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSseeyRERTMR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 591 VLKkSAYLSAVgtftwvCTPFLVALCTFAVYVTIDENNI---LDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLK 667
Cdd:TIGR02857 223 VLR-IAFLSSA------VLELFATLSVALVAVYIGFRLLagdLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 668 RLRIFLSHEELEpdSIERRPVkDGGGTNSITVRNATFTWARSDPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE 747
Cdd:TIGR02857 296 ALFAVLDAAPRP--LAGKAPV-TAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 748 MDKVEGHVAIKGVN------------------------------------------------------------------ 761
Cdd:TIGR02857 372 VDPTEGSIAVNGVPladadadswrdqiawvpqhpflfagtiaenirlarpdasdaeirealeragldefvaalpqgldtp 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIV 834
Cdd:TIGR02857 452 igeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVV 528
|
.
gi 2462549072 835 M 835
Cdd:TIGR02857 529 L 529
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1303-1499 |
4.33e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.91 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAKIGLHDlRFK-ITIIPQDPVL---- 1373
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTL-LnaiaGSLPPDS---GSILIDGKDVTKLPEYK-RAKyIGRVFQDPMMgtap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1374 ---------------FSGSLRMNLdpfsqysdeevwTSLELAHLKDFVSA----LPDKLDHECaeggENLSVGQRQLVCL 1434
Cdd:COG1101 96 smtieenlalayrrgKRRGLRRGL------------TKKRRELFRELLATlglgLENRLDTKV----GLLSGGQRQALSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1435 ARALLRKTKILVLDEATAAVD-------LE-TDDLIQStirtqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEI 1499
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
697-858 |
4.77e-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: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMdkvEGHVAIKGVN------------ 761
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLlrlLNGLLKPT---SGEVLVDGKDitkknlrelrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 783
Cdd:COG1122 77 vglvfqnpddqlfaptveedvafgpenlglpreeirerveealelvglehladrppheLSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 784 LFDDPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARDGAFA 857
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLE-------LLKrlnkeGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDYELLE 229
|
.
gi 2462549072 858 E 858
Cdd:COG1122 230 E 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
704-844 |
5.41e-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: 84.11 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 704 FTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGVN--------------------- 761
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLR-LIAGLERPdSGEILIDGRDvtgvpperrnigmvfqdyalf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 795
Cdd:cd03259 85 phltvaeniafglklrgvpkaeirarvrellelvglegllnrypheLSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 796 VGKHIFENVigpKGMLKN--KTRILVTHSMS-YLPQVDVIIVMSGGKISEMG 844
Cdd:cd03259 165 LREELREEL---KELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
696-852 |
7.64e-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: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG--VN----------- 761
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-MIAGLEDPtSGEILIGGrdVTdlppkdrniam 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ------------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDD 787
Cdd:COG3839 80 vfqsyalyphmtvyeniafplklrkvpkaeidrrvreaaellgledlldrkpkqLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 788 PLSAVDAHvgkhifenvigpkgmLKNKTR--------------ILVTH------SMSylpqvDVIIVMSGGKISEMGSYQ 847
Cdd:COG3839 160 PLSNLDAK---------------LRVEMRaeikrlhrrlgtttIYVTHdqveamTLA-----DRIAVMNDGRIQQVGTPE 219
|
....*
gi 2462549072 848 ELLAR 852
Cdd:COG3839 220 ELYDR 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1286-1516 |
8.53e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1286 RVEFRNYCLryrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHDLRFKI 1364
Cdd:PRK13644 3 RLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDP-VLFSGslRMNLDPFSQYSDEEVWTSLELAHLKDfvSALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKT 1442
Cdd:PRK13644 80 GIVFQNPeTQFVG--RTVEEDLAFGPENLCLPPIEIRKRVD--RALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1443 KILVLDEATAAVDLETDDLIQSTIRTQFEDC-TVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFY 1516
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
696-852 |
1.12e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.35 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS--------------------------------- 742
Cdd:COG1118 2 SIEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRiiagletpdsgrivlngrdlftnlpprerrvgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 743 -----ALLAEMDkVEGHVA------------IKGV-------------------NLSGGQKQRVSLARAVYSNADIYLFD 786
Cdd:COG1118 80 vfqhyALFPHMT-VAENIAfglrvrppskaeIRARveellelvqlegladrypsQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 787 DPLSAVDAHVGK-------HIFENVigpkgmlkNKTRILVTHSmsylpQVDV------IIVMSGGKISEMGSYQELLAR 852
Cdd:COG1118 159 EPFGALDAKVRKelrrwlrRLHDEL--------GGTTVFVTHD-----QEEAleladrVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1287-1509 |
1.17e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 83.92 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREdldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAkiGLHDLRFKITI 1366
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLF---------SGSLRMNLDPFSQYSDE--EVWTSLELAHLkdfvsalpdkLDHEcaegGENLSVGQRQLVCLA 1435
Cdd:cd03299 76 VPQNYALFphmtvykniAYGLKKRKVDKKEIERKvlEIAEMLGIDHL----------LNRK----PETLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1436 RALLRKTKILVLDEATAAVDLETDDLIQS---TIRTQFeDCTVLTIAHRLNTI-MDYTRVIVLDKGEIQEYGAPSDLL 1509
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREelkKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
696-845 |
1.40e-17 |
|
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: 83.31 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV--------------- 760
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiglhdlrsris 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 ---------------------------------------------------------NLSGGQKQRVSLARAVYSNADIY 783
Cdd:cd03244 82 iipqdpvlfsgtirsnldpfgeysdeelwqalervglkefveslpggldtvveeggeNLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 784 LFDDPLSAVDAHVGKHIFEnVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGS 845
Cdd:cd03244 162 VLDEATASVDPETDALIQK-TI--REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
755-858 |
1.69e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 88.64 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 755 VAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGpkgmLKNKTRILVTHSMSYLPQVDVIIV 834
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIV 680
|
90 100
....*....|....*....|....
gi 2462549072 835 MSGGKISEMGSYQELLARDGAFAE 858
Cdd:TIGR01193 681 LDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
697-842 |
1.86e-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: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGV------------- 760
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLR-LIAGLEKPtSGEVLVDGKpvtgpgpdrgvvf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 -------------N--------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 789
Cdd:COG1116 87 qepallpwltvldNvalglelrgvpkaerrerarellelvglagfedayphqLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 790 SAVDAHVgkhifenvigpKGML----------KNKTRILVTHSMS---YLpqVDVIIVMSG--GKISE 842
Cdd:COG1116 167 GALDALT-----------RERLqdellrlwqeTGKTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1286-1501 |
1.92e-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: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1286 RVEFRNYCLRYREDLD--FVLRHINVTINGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGINIAKIGLhd 1359
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLiaglEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1360 lrfKITIIPQDPVLF----------SGsLRMNLDPFSQYsDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQR 1429
Cdd:COG1116 81 ---DRGVVFQEPALLpwltvldnvaLG-LELRGVPKAER-RERARELLELVGLAGFEDAYP----HQ-------LSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1430 QLVCLARALLRKTKILVLDEATAAVDLET-----DDLIQstIRTQfEDCTVLTIAH------RLNtimdyTRVIVLDK-- 1496
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR--LWQE-TGKTVLFVTHdvdeavFLA-----DRVVVLSArp 216
|
....*
gi 2462549072 1497 GEIQE 1501
Cdd:COG1116 217 GRIVE 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
429-822 |
2.32e-17 |
|
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: 87.42 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 429 LQTLVLHqyfHICFvsgmRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMS--VDAQRFMDLATYINMIWSAPLQVIL 506
Cdd:TIGR02868 72 LERLVGH---DAAL----RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVGAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 507 ALYLLWLN--LGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRiKLMnEILNGIKVLKLYAWELAFKDKVLAI 584
Cdd:TIGR02868 145 VAAIAVLSvpAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAA-QLT-DALDGAAELVASGALPAALAQVEEA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 585 RQEELKVLKKSAYLSAVGT--FTWVCTpfLVALCTFAVYVTIDENNILDAQT----AFVSLALFNilrfPLNILPMVISS 658
Cdd:TIGR02868 223 DRELTRAERRAAAATALGAalTLLAAG--LAVLGALWAGGPAVADGRLAPVTlavlVLLPLAAFE----AFAALPAAAQQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 659 IVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGTNSITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKS 738
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 739 SLLSALLAEMDKVEGHVAIKGVN--------------------------------------------------------- 761
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPvssldqdevrrrvsvcaqdahlfdttvrenlrlarpdatdeelwaalervgladwlr 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 762 ----------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPkgmLKNKTRILVTHS 822
Cdd:TIGR02868 456 alpdgldtvlgeggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLITHH 529
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1287-1481 |
3.65e-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: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLtlglFRInesaegeiiIDGI------NIAKIGLHDL 1360
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRA---------LAGLwpwgsgRIGMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1361 RFkitiIPQDPVLFSGSLRmnldpfsqysdEEV---WtslelahlkdfvsalpdkldhecaegGENLSVGQRQLVCLARA 1437
Cdd:cd03223 67 LF----LPQRPYLPLGTLR-----------EQLiypW--------------------------DDVLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549072 1438 LLRKTKILVLDEATAAVDLETDDLIQSTIRTQFedCTVLTIAHR 1481
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1287-1510 |
4.10e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.45 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI--AKIGLHDLRFKI 1364
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDPVLFS----------GSLRMNldpfsQYSDEEvwtSLELAH-LKDFVsALPDKLDHECAEggenLSVGQRQLVC 1433
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR-----GASKEE---AEKQAReLLAKV-GLAERAHHYPSE----LSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1434 LARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQ 1510
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
694-852 |
4.94e-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: 84.38 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 694 TNSITVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLL---------------------SALLAE----- 747
Cdd:COG3842 3 MPALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLrmiagfetpdsgrilldgrdvTGLPPEkrnvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 748 -----------MDkVEGHVA----IKGVN---------------------------LSGGQKQRVSLARAVYSNADIYLF 785
Cdd:COG3842 81 mvfqdyalfphLT-VAENVAfglrMRGVPkaeirarvaellelvglegladryphqLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 786 DDPLSAVDAHVGKHIFENVigpKGMLK--NKTRILVTH------SMSylpqvDVIIVMSGGKISEMGSYQELLAR 852
Cdd:COG3842 160 DEPLSALDAKLREEMREEL---RRLQRelGITFIYVTHdqeealALA-----DRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1303-1499 |
5.16e-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: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI--AKIGLHDLRFKITIIPQDPVLFSgslRM 1380
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 N------LDP---FSQYSDEEVWTSLELahLKDFvsALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEAT 1451
Cdd:cd03262 92 TvlenitLAPikvKGMSKAEAEERALEL--LEKV--GLADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1452 AAVDLETDDLIQSTIRTQFED-CTVLTIAHRlntiMDY-----TRVIVLDKGEI 1499
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEgMTMVVVTHE----MGFarevaDRVIFMDDGRI 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
697-854 |
5.17e-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: 82.21 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkeprearrqigvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDP 788
Cdd:COG4555 80 pderglydrltvreniryfaelyglfdeelkkrieeliellgleefldrrvgeLSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 789 LSAVDAhVGKHIFENVIgpKGMLK-NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARDG 854
Cdd:COG4555 160 TNGLDV-MARRLLREIL--RALKKeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
697-861 |
6.71e-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: 82.48 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALL---------AEMDK-------------- 750
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLlptsgkvtvDGLDTldeenlweirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 751 --------------VEGHVAI----KGV---------------------------NLSGGQKQRVSLARAVYSNADIYLF 785
Cdd:TIGR04520 81 mvfqnpdnqfvgatVEDDVAFglenLGVpreemrkrvdealklvgmedfrdrephLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 786 DDPLSAVDahvgkhifenvigPKG-------MLK-----NKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARd 853
Cdd:TIGR04520 161 DEATSMLD-------------PKGrkevletIRKlnkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQ- 226
|
....*...
gi 2462549072 854 gafAEFLR 861
Cdd:TIGR04520 227 ---VELLK 231
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
970-1190 |
7.65e-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: 82.82 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 970 FLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRL--SVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLL 1047
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLlaLLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1048 HSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVIL-----LATpIAAIIIPPLGLIYFF 1122
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFllnwrLAL-ISLLVLPLLLLATYL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1123 VQRFYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVAN 1190
Cdd:cd18544 161 FRKKSRKAYREVR--EKLSR--LNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLF 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
699-840 |
9.38e-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: 80.66 E-value: 9.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 699 VRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN----------------- 761
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkrigyvpqrrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDP 788
Cdd:cd03235 80 drdfpisvrdvvlmglyghkglfrrlskadkakvdealervglseladrqigeLSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 789 LSAVDAHVGKHIFENVIGPKGmlKNKTRILVTHSM-SYLPQVDVIIVMSGGKI 840
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRR--EGMTILVVTHDLgLVLEYFDRVLLLNRTVV 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1303-1499 |
1.06e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 81.62 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSL----TlGLFRINEsaeGEIIIDGINIAKIGLHDL------R-FKIT-IIPQD 1370
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLfnliT-GFYRPTS---GRILFDGRDITGLPPHRIarlgiaRtFQNPrLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 PVL----------FSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSaLPDKLDHECAeggeNLSVGQRQLVCLARALLR 1440
Cdd:COG0411 95 TVLenvlvaaharLGRGLLAALLRLPRARREEREARERAEELLERVG-LADRADEPAG----NLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1441 KTKILVLDEATAAVDL-ETDDLIQsTIRT--QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEI 1499
Cdd:COG0411 170 EPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLAdRIVVLDFGRV 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
697-840 |
1.10e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.59 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK------------------------ 750
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLR-IIAGLERptsgevlvdgepvtgpgpdrgyvf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 751 ----------VEGHVA----IKGVN---------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 789
Cdd:cd03293 80 qqdallpwltVLDNVAlgleLQGVPkaeareraeellelvglsgfenayphqLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 790 SAVDAHVGKHIFENVIgpkGMLK--NKTRILVTHSMS---YLPqvDVIIVMSG--GKI 840
Cdd:cd03293 160 SALDALTREQLQEELL---DIWRetGKTVLLVTHDIDeavFLA--DRVVVLSArpGRI 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
697-861 |
1.45e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.58 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALL---------------------------- 745
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqsgeikidgitiskenlkeirkkigi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 746 -----------------------------AEMDKVEGHVAIK-GV---------NLSGGQKQRVSLARAVYSNADIYLFD 786
Cdd:PRK13632 88 ifqnpdnqfigatveddiafglenkkvppKKMKDIIDDLAKKvGMedyldkepqNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 787 DPLSAVDAHvGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDgafaEFLR 861
Cdd:PRK13632 168 ESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK----EILE 237
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
697-852 |
2.58e-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: 80.23 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRN--ATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------------- 759
Cdd:COG1124 2 LEVRNlsVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 ----------VN---------------------------------------------LSGGQKQRVSLARAVYSNADIYL 784
Cdd:COG1124 82 qmvfqdpyasLHprhtvdrilaeplrihglpdreeriaelleqvglppsfldryphqLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 785 FDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSM---SYLpqVDVIIVMSGGKISEMGSYQELLAR 852
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 ... |
1303-1507 |
3.15e-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: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGINIAKIGLHDLR-------FKITIIPQD 1370
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKT--TLfnlisGFLRPTS---GSVLFDGEDITGLPPHEIArlgigrtFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 ---------PVLFSGSLRMNLDPFSQYSDEEVWTSLELAhlkDFVsALPDKLDHECAeggeNLSVGQRQLVCLARALLRK 1441
Cdd:cd03219 90 ltvlenvmvAAQARTGSGLLLARARREEREARERAEELL---ERV-GLADLADRPAG----ELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1442 TKILVLDEATAAVDL-ETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSD 1507
Cdd:cd03219 162 PKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
520-852 |
5.24e-16 |
|
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: 83.31 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 520 LAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKL-YAWELAFKDKVLAIRQEELKVLKKSAYL 598
Cdd:COG4615 151 LLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLnRRRRRAFFDEDLQPTAERYRDLRIRADT 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 599 SAVGTFTWVCTPF--LVALCTFAV--YVTIDENNIldaqTAFVSLALFniLRFPLNILPMVISSIVQASVSLKRL-RIFL 673
Cdd:COG4615 231 IFALANNWGNLLFfaLIGLILFLLpaLGWADPAVL----SGFVLVLLF--LRGPLSQLVGALPTLSRANVALRKIeELEL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 674 SHEELEPDSIERRPVKDGGGTNSITVRNATFTWARSDPP---TLNGITFSIPEGALVAVVGQVGCGKSSLL--------- 741
Cdd:COG4615 305 ALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAklltglyrp 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 742 ------------------------SA-------------------------LLAEMdKVEGHVAIKG-----VNLSGGQK 767
Cdd:COG4615 385 esgeilldgqpvtadnreayrqlfSAvfsdfhlfdrllgldgeadparareLLERL-ELDHKVSVEDgrfstTDLSQGQR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 768 QRVSLARAVYSNADIYLFD------DPlsavdahVGKHIFENVIGPkgMLK--NKTRILVTHSMSYLPQVDVIIVMSGGK 839
Cdd:COG4615 464 KRLALLVALLEDRPILVFDewaadqDP-------EFRRVFYTELLP--ELKarGKTVIAISHDDRYFDLADRVLKMDYGK 534
|
410
....*....|...
gi 2462549072 840 ISEMGSYQELLAR 852
Cdd:COG4615 535 LVELTGPAALAAS 547
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
697-853 |
8.60e-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: 78.31 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:cd03261 1 IELRGLTK--SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 783
Cdd:cd03261 79 mgmlfqsgalfdsltvfenvafplrehtrlseeeireivlekleavglrgaedlypaeLSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 784 LFDDPLSAVDAhVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARD 853
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 ... |
696-845 |
1.04e-15 |
|
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: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV--------------- 760
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistipledlrsslt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 ---------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 801
Cdd:cd03369 86 iipqdptlfsgtirsnldpfdeysdeeiygalrvsegglNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549072 802 ENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGS 845
Cdd:cd03369 166 KTI---REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1289-1517 |
1.13e-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: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1289 FRNYCLRYREdldfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglhdlrfKITIIP 1368
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1369 QDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1448
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1449 EATAAVDLETDDLIqstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYS 1517
Cdd:cd03291 185 SPFGYLDVFTEKEI-------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSS 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1304-1503 |
1.46e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLHDLRFKITIIPQDPVLFSG 1376
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 S--------LRMNLDPFSQYSDEEVWTSLELAHLKDFVSalpDKLdHECAEGgenLSVGQRQLVCLARALLRKTKILVLD 1448
Cdd:PRK14239 101 SiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVK---DRL-HDSALG---LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1449 EATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRL---NTIMDYTrVIVLDkGEIQEYG 1503
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRISDRT-GFFLD-GDLIEYN 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
671-852 |
1.60e-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: 81.49 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 671 IFLSHEELE--PDSIERRPVKDGGGTNS---ITVRNATFTWARSDPPT---LNGITFSIPEGALVAVVGQVGCGKSSLLS 742
Cdd:COG1123 230 ILAAPQALAavPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 743 ALLAEMDKVEGHVAIKGVN------------------------------------------------------------- 761
Cdd:COG1123 310 LLLGLLRPTSGSILFDGKDltklsrrslrelrrrvqmvfqdpysslnprmtvgdiiaeplrlhgllsraerrervaelle 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ---------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVT 820
Cdd:COG1123 390 rvglppdladrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILN-------LLRdlqrelGLTYLFIS 462
|
250 260 270
....*....|....*....|....*....|...
gi 2462549072 821 HSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 852
Cdd:COG1123 463 HDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1303-1508 |
1.69e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGINIAKIGLHD-LRFKITIIPQDPVL--- 1373
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKS--TLmkilsGVYQPDS---GEILLDGEPVRFRSPRDaQAAGIAIIHQELNLvpn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1374 -------FSGSLRMN---LDPFSQYSD-EEVwtsleLAHLKdfVSALPDKLdhecaegGENLSVGQRQLVCLARALLRKT 1442
Cdd:COG1129 94 lsvaeniFLGREPRRgglIDWRAMRRRaREL-----LARLG--LDIDPDTP-------VGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1443 KILVLDEATAAVDL-ETDDLIQsTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1508
Cdd:COG1129 160 RVLILDEPTASLTErEVERLFR-IIRRlKAQGVAIIYISHRLDEVFEIAdRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
697-844 |
2.16e-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: 77.16 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRN--ATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN------------- 761
Cdd:cd03257 2 LEVKNlsVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------------------------LSGGQKQRVSLARAVY 777
Cdd:cd03257 82 keiqmvfqdpmsslnprmtigeqiaeplrihgklskkearkeavllllvgvglpeevlnrypheLSGGQRQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 778 SNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMG 844
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1303-1512 |
2.52e-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: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSltlgLFRI----NESAEGEIIIDGiniakiglhdlRFKITIIPQDPVLFSG-S 1377
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKIlageLEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1378 LRMNLdpfsQYSDEEVWTSL----ELAHLKDFVSALPDKLD---HECAEGGE--------------------------NL 1424
Cdd:COG0488 78 VLDTV----LDGDAELRALEaeleELEAKLAEPDEDLERLAelqEEFEALGGweaearaeeilsglgfpeedldrpvsEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1425 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTqfEDCTVLTIAH-R--LNTIMdyTRVIVLDKGEIQE 1501
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRVA--TRILELDRGKLTL 229
|
250
....*....|..
gi 2462549072 1502 Y-GAPSDLLQQR 1512
Cdd:COG0488 230 YpGNYSAYLEQR 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1304-1498 |
2.56e-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: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDG--INIAkiGLHD-LRFKITIIPQDPVLFs 1375
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKS--TLmkilyGLYQPDS---GEILIDGkpVRIR--SPRDaIALGIGMVHQHFMLV- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1376 gslrmnlDPFSQYsdEEVWTSLE--------LAHLKDFVSAL---------PDKLDHEcaeggenLSVGQRQLVCLARAL 1438
Cdd:COG3845 93 -------PNLTVA--ENIVLGLEptkggrldRKAARARIRELserygldvdPDAKVED-------LSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1439 LRKTKILVLDEATaAV--DLETDDLIQsTIRtQF--EDCTVLTIAHRLNTIMDYT-RVIVLDKGE 1498
Cdd:COG3845 157 YRGARILILDEPT-AVltPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIAdRVTVLRRGK 218
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
996-1258 |
3.19e-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: 77.99 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 996 DPIVNGTQEHTKVRLSVY-GALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKEL 1074
Cdd:cd18557 24 DTIIKGGDLDVLNELALIlLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1075 DTVDSMIPEVIKMFMGSLFNVIGaCIVILLA-----TPIAAIIIPPLGLIYFFVQRFYVASSRQLkrLESVSRSPvySHF 1149
Cdd:cd18557 104 SVLQSAVTDNLSQLLRNILQVIG-GLIILFIlswklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1150 NETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVAN---RWLAVRLECVGNCIVLFAALFAVISRHsLSAGLVGL 1226
Cdd:cd18557 179 EESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANalfQGITSLLIYLSLLLVLWYGGYLVLSGQ-LTVGELTS 257
|
250 260 270
....*....|....*....|....*....|..
gi 2462549072 1227 SVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1258
Cdd:cd18557 258 FILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1287-1514 |
3.58e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.47 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDP--VLFS---------GSLRMNLDPfsQYSDEEVWTSLELAHLKDFvsalPDKLDHecaeggeNLSVGQRQLVCLA 1435
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMWDF----RDKPPY-------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1436 RALLRKTKILVLDEATAAVDLETDDLIQSTI-RTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPS-----DL 1508
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWAdQVIVLKEGRVLAEGDKSlltdeDI 230
|
....*.
gi 2462549072 1509 LQQRGL 1514
Cdd:PRK13647 231 VEQAGL 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1303-1511 |
4.02e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.12 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFrineSAE-----GEIIIDGINIAKIGLHDLRFKITIIPQDPVL-FSG 1376
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTL-LRAL----SGElspdsGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 S----LRMNLDPFSQYSDE------EVWTSLELAHLKD-FVSALpdkldhecaEGGEnlsvgqRQLVCLARALLR----- 1440
Cdd:PRK13548 92 TveevVAMGRAPHGLSRAEddalvaAALAQVDLAHLAGrDYPQL---------SGGE------QQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1441 -KTKILVLDEATAAVDL----ETDDLIQStiRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVIVVLHDLNLAARYAdRIVLLHQGRLVADGTPAEVLTP 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1303-1509 |
4.31e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.88 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINIAKIGLHDLRFKITIIPQDP------ 1371
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1372 -VLFSGSLRMNLDPFSQYSDE---EVWTSLELAHLKDFVSalpDKLDhecAEGGEnLSVGQRQLVCLARALLRKTKILVL 1447
Cdd:PRK14247 98 sIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVK---DRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1448 DEATAAVDLETDDLIQSTIRTQFEDCTVLTIAH---RLNTIMDYtrVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVEWGPTREVF 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1300-1509 |
4.52e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.31 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1300 LDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHDLRFK--------ITIIP 1368
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1369 QDPVLFSGSLRMNLDPF-SQYSDEEVWTSLELAHLKDFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVL 1447
Cdd:PRK10070 120 HMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1448 DEATAAVD--LET---DDLIQSTIRTQFedcTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK10070 189 DEAFSALDplIRTemqDELVKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1303-1508 |
8.81e-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: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESAE---GEII--------------------------------- 1346
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1347 IDGINIAKIGLHDLRFKITIIPQDPVLFSGSLR-----MNLDPFSQYS-DEEVWTSLELAHLKdfvsalpdKLDHECAEG 1420
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIEMV--------QLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1421 GENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1497
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDLSdKAIWLENG 245
|
250
....*....|.
gi 2462549072 1498 EIQEYGAPSDL 1508
Cdd:TIGR03269 246 EIKEEGTPDEV 256
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1294-1467 |
1.18e-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: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1294 LRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGINIAKIglhdlrfkiTIIPQD 1370
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLlrILaGLLR---PDSGEVRWNGTPLAEQ---------RDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 PVLFSG---------SLRMNLD---PFSQYSDEEVWTSLELAHLKDFvSALPdkldheCAEggenLSVGQRQLVCLARAL 1438
Cdd:TIGR01189 74 NILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLP------AAQ----LSAGQQRRLALARLW 142
|
170 180
....*....|....*....|....*....
gi 2462549072 1439 LRKTKILVLDEATAAVDLETDDLIQSTIR 1467
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
714-849 |
1.24e-14 |
|
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: 74.91 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGVN--------------------------- 761
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDiydldvdvlelrrrvgmvfqkpnpfpg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAh 795
Cdd:cd03260 96 siydnvayglrlhgiklkeelderveealrkaalwdevkdrlhalgLSGGQQQRLCLARALANEPEVLLLDEPTSALDP- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 796 VGKHIFENVIgpKGMLKNKTRILVTHSMsylPQV----DVIIVMSGGKISEMGSYQEL 849
Cdd:cd03260 175 ISTAKIEELI--AELKKEYTIVIVTHNM---QQAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1287-1511 |
1.30e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.88 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHDLRFKI 1364
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1365 TIIPQDP--VLFS---------GSLRMNLdpfsqySDEEVWTSLELAHLKDFVSALPDKLDHecaeggeNLSVGQRQLVC 1433
Cdd:PRK13639 81 GIVFQNPddQLFAptveedvafGPLNLGL------SKEEVEKRVKEALKAVGMEGFENKPPH-------HLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1434 LARALLRKTKILVLDEATAAVD-LETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1287-1509 |
1.35e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDF-VLRHINVTINGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGINIAKIGLHDLRF 1362
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLF---EEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1363 KITIIPQDP-VLFSGSLRMNLDPFSQYSD----EEVWTSLELAHLKdfvsalPDKLDHECAEGGEnLSVGQRQLVCLARA 1437
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLA------VNMLDFKTREPAR-LSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1438 LLRKTKILVLDEATAAVDLETDDLIQSTIRtQFED---CTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
697-849 |
1.94e-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: 74.08 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL------------------LAEMDKVEGHVAI- 757
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtgelrptsgtayingysiRTDRKAARQSLGYc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 ----------------------KGV---------------------------NLSGGQKQRVSLARAVYSNADIYLFDDP 788
Cdd:cd03263 81 pqfdalfdeltvrehlrfyarlKGLpkseikeevelllrvlgltdkankrarTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 789 LSAVDaHVGKHIFENVIgpKGMLKNKTRILVTHSM---SYLpqVDVIIVMSGGKISEMGSYQEL 849
Cdd:cd03263 161 TSGLD-PASRRAIWDLI--LEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1042-1449 |
1.97e-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: 78.30 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1042 LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVD---SMIPEVIKMFMgslfnVIGACIVIL--LATPIAAIIIPPL 1116
Cdd:COG4615 83 LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISqafVRLPELLQSVA-----LVLGCLAYLawLSPPLFLLTLVLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1117 GLIyFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllgvSVIRAFEE----QER--FIHQSDLKV------DENQKAYY 1184
Cdd:COG4615 158 GLG-VAGYRLLVRRARRHLRRAREAEDRLFKHFR------ALLEGFKElklnRRRrrAFFDEDLQPtaeryrDLRIRADT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1185 PSIVANRWlavrlecvGNCIvLFAALFAVIsrhslsAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNI----------VA 1254
Cdd:COG4615 231 IFALANNW--------GNLL-FFALIGLIL------FLLPALGWADPAVLSGFVLVLLFLRGPLSQLVgalptlsranVA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1255 VERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLD---FVLRHINVTINGGEKVGIVGRTGAGKSSLT 1331
Cdd:COG4615 296 LRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1332 ---LGLFRineSAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGslrmNLDPFSQYSDEEVwtsleLAHLKDFvsa 1408
Cdd:COG4615 376 kllTGLYR---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR----LLGLDGEADPARA-----RELLERL--- 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2462549072 1409 lpdKLDHECA-EGGE----NLSVGQRQLVCLARALLRKTKILVLDE 1449
Cdd:COG4615 441 ---ELDHKVSvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
697-857 |
2.34e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.23 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALL------------------------------ 745
Cdd:TIGR00958 479 IEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptggqvlldgvplvqydhhylhrqva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 746 -----------------------AEMDKVEG--------------------HVAIKGVNLSGGQKQRVSLARAVYSNADI 782
Cdd:TIGR00958 559 lvgqepvlfsgsvreniaygltdTPDEEIMAaakaanahdfimefpngydtEVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 783 YLFDDPLSAVDAHVgkhifENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFA 857
Cdd:TIGR00958 639 LILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1303-1509 |
2.44e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.80 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtlgLFRINES---AEGEIIIDGINIAKIGLHDLRFKITIIPQDPVL---FSG 1376
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTL---LRAINGTltpTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 S--LRMNLDP----FSQYSDEEVwTSLELAHLKDFVSALPDKldhecaeGGENLSVGQRQLVCLARALLRKTKILVLDEA 1450
Cdd:PRK09536 95 RqvVEMGRTPhrsrFDTWTETDR-AAVERAMERTGVAQFADR-------PVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1451 TAAVDL----ETDDLIQSTIRtqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK09536 167 TASLDInhqvRTLELVRRLVD---DGKTAVAAIHDLDLAARYCdELVLLADGRVRAAGPPADVL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1303-1509 |
2.58e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.72 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFKITIIPQDPV------- 1372
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1373 ----LFSGSLR--MNLDPfsqySDEEVWTSlELAHLKDFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILV 1446
Cdd:PRK10419 107 tvreIIREPLRhlLSLDK----AERLARAS-EMLRAVDLDDSVLDKRPPQ-------LSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1447 LDEATAAVDLetddLIQSTI-------RTQFeDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK10419 175 LDEAVSNLDL----VLQAGVirllkklQQQF-GTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKL 240
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
703-852 |
2.71e-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: 74.15 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 703 TFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKGV--------------------- 760
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGTdltllsgkelrkarrrigmif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 ---------------------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPL 789
Cdd:cd03258 89 qhfnllssrtvfenvalpleiagvpkaeieervlellelvgledkadaypaQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 790 SAVDAHVGKHIFEnvigpkgMLK--NK----TRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 852
Cdd:cd03258 169 SALDPETTQSILA-------LLRdiNRelglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
697-852 |
3.36e-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: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGVN------------- 761
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrLIEPT--SGEIFIDGEDireqdpvelrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 783
Cdd:cd03295 78 gyviqqiglfphmtveenialvpkllkwpkekireradellalvgldpaefadrypheLSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 784 LFDDPLSAVDAHVGKHIFENVIGPKGMLkNKTRILVTHSM-SYLPQVDVIIVMSGGKISEMGSYQELLAR 852
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1285-1508 |
3.41e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.88 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1285 GRVEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAKIGLHDl 1360
Cdd:COG3839 2 ASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTL-LrmiaGLEDPTS---GEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1361 RfKITIIPQDPVLF----------SGsLRM-NLDPfsqysDE------EVWTSLELAHLKDfvsALPDkldhecaeggeN 1423
Cdd:COG3839 75 R-NIAMVFQSYALYphmtvyeniaFP-LKLrKVPK-----AEidrrvrEAAELLGLEDLLD---RKPK-----------Q 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1424 LSVGQRQLVCLARALLRKTKILVLDEATAAVD----LETddliqstiRTQfedctvltIA---HRLNTIMDY-------- 1488
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEM--------RAE--------IKrlhRRLGTTTIYvthdqvea 197
|
250 260
....*....|....*....|....
gi 2462549072 1489 ----TRVIVLDKGEIQEYGAPSDL 1508
Cdd:COG3839 198 mtlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1287-1508 |
3.82e-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: 73.43 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYreDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHdlRFKITI 1366
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLF---------SGSLRMNLDPfSQYSDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARA 1437
Cdd:cd03300 77 VFQNYALFphltvfeniAFGLRLKKLP-KAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1438 LLRKTKILVLDEATAAVD--------LETDDLIQSTirtqfeDCTVLTIAHRLN---TIMDytRVIVLDKGEIQEYGAPS 1506
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDlklrkdmqLELKRLQKEL------GITFVFVTHDQEealTMSD--RIAVMNKGKIQQIGTPE 216
|
..
gi 2462549072 1507 DL 1508
Cdd:cd03300 217 EI 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1306-1499 |
4.09e-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: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1306 HINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGINIAKIGLHDLrfKITIIPQDPVLFSG-------- 1376
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL-LNLIAGFETPQsGRVLINGVDVTAAPPADR--PVSMLFQENNLFAHltveqnvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 ---SLRMNLDPFSQysdEEVWTSLELAHLKDFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1453
Cdd:cd03298 93 lglSPGLKLTAEDR---QAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1454 VD----LETDDLIqSTIRTQfEDCTVLTIAHRLNTIMD-YTRVIVLDKGEI 1499
Cdd:cd03298 159 LDpalrAEMLDLV-LDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1303-1503 |
7.26e-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: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRF---------KITIIPQdpVL 1373
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYlpeerglypKMKVIDQ--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1374 FSGSLR-MNLDPFSQYSDEevW-TSLELAHLKDfvsalpDKLdhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1451
Cdd:cd03269 93 YLAQLKgLKKEEARRRIDE--WlERLELSEYAN------KRV--------EELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1452 AAVDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYG 1503
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
963-1258 |
7.64e-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: 74.00 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 963 AIGLFISFLSIFLFMcnhvsalaSNYWLSLWT-DDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRC 1041
Cdd:cd18542 2 LLAILALLLATALNL--------LIPLLIRRIiDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1042 LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGAcIVILLA-----TPIAAIIIPPL 1116
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGA-LIIMFSinwklTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1117 GLI-YFF---VQRFYVASSRQLKRLESVsrspvyshFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKA------ 1182
Cdd:cd18542 153 ALFsYVFfkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFaredYEIEKFDKENEEYRDLNIKLakllak 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1183 YYPSIVAnrwlavrLECVGNCIVLFAALFAVIsRHSLSAG-LVGLSvSYslqvTTYLNWLVRMS----SEMETNIVAVER 1257
Cdd:cd18542 225 YWPLMDF-------LSGLQIVLVLWVGGYLVI-NGEITLGeLVAFI-SY----LWMLIWPVRQLgrliNDMSRASASAER 291
|
.
gi 2462549072 1258 L 1258
Cdd:cd18542 292 I 292
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1287-1511 |
8.53e-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: 74.75 E-value: 8.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAKIGLHDlRf 1362
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTL-LrmiaGFETPDS---GRILLDGRDVTGLPPEK-R- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1363 KITIIPQDPVLFS----------GsLRM-NLDPfsQYSDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQL 1431
Cdd:COG3842 78 NVGMVFQDYALFPhltvaenvafG-LRMrGVPK--AEIRARVAELLELVGLEGLADRYP----HQ-------LSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1432 VCLARALLRKTKILVLDEATAAVDLETddliqsTIRTQFEdctVLTIAHRLN--TIM------------DytRVIVLDKG 1497
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKL------REEMREE---LRRLQRELGitFIYvthdqeealalaD--RIAVMNDG 212
|
250
....*....|....
gi 2462549072 1498 EIQEYGAPSDLLQQ 1511
Cdd:COG3842 213 RIEQVGTPEEIYER 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1303-1518 |
9.90e-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: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglhdlrfKITIIPQDPVLFSGSLRMNL 1382
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 dPFSQYSDEEVWTSLELA-HLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-D 1460
Cdd:TIGR01271 508 -IFGLSYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1461 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1518
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
714-852 |
1.85e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 71.63 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------------------------- 761
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaevrrrigyvpqepalypdltvrenlr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVI 805
Cdd:COG1131 96 ffarlyglprkeareridellelfgltdaadrkvgtLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-EARRELWELL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462549072 806 gpKGMLK-NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 852
Cdd:COG1131 175 --RELAAeGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
696-849 |
1.89e-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: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWARSdpPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG--------------- 759
Cdd:cd03296 2 SIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLR-LIAGLERPdSGTILFGGedatdvpvqernvgf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 --------------------------------------VN------------------LSGGQKQRVSLARAVYSNADIY 783
Cdd:cd03296 79 vfqhyalfrhmtvfdnvafglrvkprserppeaeirakVHellklvqldwladrypaqLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 784 LFDDPLSAVDAHVGKHIfenvigpKGMLK------NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQEL 849
Cdd:cd03296 159 LLDEPFGALDAKVRKEL-------RRWLRrlhdelHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1287-1524 |
2.26e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLD----FVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHDLR 1361
Cdd:PRK13633 5 IKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1362 FKITIIPQDP------------VLFsGSLRMNLDPfsqysdEEVWTSLELAHLKDFVSALPDKLDHEcaeggenLSVGQR 1429
Cdd:PRK13633 85 NKAGMVFQNPdnqivativeedVAF-GPENLGIPP------EEIRERVDESLKKVGMYEYRRHAPHL-------LSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1430 QLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSD 1507
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
250
....*....|....*..
gi 2462549072 1508 LLQQrglfYSMAKDAGL 1524
Cdd:PRK13633 231 IFKE----VEMMKKIGL 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
714-840 |
2.96e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLL-----------------SALLAE--------------------MDKV----- 751
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLrllagletpsagellagTAPLAEaredtrlmfqdarllpwkkvIDNVglglk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 752 -----EGHVAIKGVNL-----------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG---KHIFENVIGPKGMlk 812
Cdd:PRK11247 108 gqwrdAALQALAAVGLadranewpaalSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRiemQDLIESLWQQHGF-- 185
|
170 180
....*....|....*....|....*....
gi 2462549072 813 nkTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:PRK11247 186 --TVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1298-1511 |
3.11e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1298 EDLDFVLRHI----NVTINGGEKVGIVGRTGAGKSSLtLGL---FRINESaeGEIIIDGINIAKiglhdlrfkiTIIPQD 1370
Cdd:PRK10771 5 TDITWLYHHLpmrfDLTVERGERVAILGPSGAGKSTL-LNLiagFLTPAS--GSLTLNGQDHTT----------TPPSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 PV--------LFSG-SLRMN----LDPFSQYSDEEVWTSLELAH---LKDFVSALPDKLdhecaeggenlSVGQRQLVCL 1434
Cdd:PRK10771 72 PVsmlfqennLFSHlTVAQNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1435 ARALLRKTKILVLDEATAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELL 218
|
..
gi 2462549072 1510 QQ 1511
Cdd:PRK10771 219 SG 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1287-1517 |
3.56e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.95 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYreDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHdlRFKITI 1366
Cdd:PRK11607 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLF---------SGSLRMNLDPFSQYSDEeVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQLVCLARA 1437
Cdd:PRK11607 96 MFQSYALFphmtveqniAFGLKQDKLPKAEIASR-VNEMLGLVHMQEFAKRKP----HQ-------LSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1438 LLRKTKILVLDEATAAVDLETDDLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQRGL 1514
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
...
gi 2462549072 1515 FYS 1517
Cdd:PRK11607 244 RYS 246
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1303-1508 |
3.58e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHDLRFKITIIPQDPVLFSG-SLRM 1380
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NLD---PFSQYSDEEvwtslelahLKDFVSALPDKLDHECAEGgeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD-L 1456
Cdd:PRK15439 106 NILfglPKRQASMQK---------MKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1457 ETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1508
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLAdRISVMRDGTIALSGKTADL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1303-1503 |
3.64e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 70.64 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiNIAKIglhdLRFKITIIPQ----DPVLFSGSL 1378
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL----LGLGGGFNPEltgrENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1379 rMNLDPfsQYSDEEVWTSLELAHLKDFVSaLPDKldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1458
Cdd:cd03220 112 -LGLSR--KEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462549072 1459 DDLIQSTIRTQFEDC-TVLTIAHRLNTIMDY-TRVIVLDKGEIQEYG 1503
Cdd:cd03220 178 QEKCQRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1304-1511 |
3.73e-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: 71.52 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLR----------F-KITIIPQDPV 1372
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRelrrkkismvFqSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1373 LFSGSLRMNLDPFSQYSDEEVWT-SLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1451
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAeALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1452 AAVDletddliqSTIRTQFEDC----------TVLTIAHRLNTIM---DytRVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:cd03294 189 SALD--------PLIRREMQDEllrlqaelqkTIVFITHDLDEALrlgD--RIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1303-1510 |
3.99e-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: 70.65 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGINIAKIGLHD-LRFKITIIPQDPVLFSG-S 1377
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVKPDS---GKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1378 LRMNLDPF--SQYSDEEVWTSLELAHLKDFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1455
Cdd:cd03218 92 VEENILAVleIRGLSKKEREEKLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1456 LETDDLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQ 1510
Cdd:cd03218 166 PIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITdRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1287-1514 |
4.01e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.37 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1366
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDP--VLFS---------GSLRMNLDPFS-QYSDEEVWTSLELAHLKDFVSalpdkldhecaeggENLSVGQRQLVCL 1434
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEETvAHRVSSALHMLGLEELRDRVP--------------HHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1435 ARALLRKTKILVLDEATAAVDLE-TDDLIQSTIRTQFE-DCTVLTIAHRLNTI---MDYtrVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQgVKELIDFLNDLPETyGMTVIFSTHQLDLVpemADY--IYVMDKGRIVAYGTVEEIF 226
|
....*
gi 2462549072 1510 QQRGL 1514
Cdd:PRK13652 227 LQPDL 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1253-1455 |
4.64e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1253 VAVERLKEYSETEKEAPWQIqeTAPPSSWPqvgRVEFRNYCLRYrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTL 1332
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPR--PQAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1333 GLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSgslRMnLDPFSQYSDEEV---WtsleLAHLKdfvsaL 1409
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekW----LERLK-----M 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1410 PDKLDHecaEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1455
Cdd:PRK10522 435 AHKLEL---EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
714-790 |
4.70e-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: 68.06 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV--------------------------------- 760
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeigyvfqdpqlfprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 ----------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLS 790
Cdd:pfam00005 81 rlglllkglskrekdaraeealeklglgdladrpvgerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1303-1510 |
4.86e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQDPVLFSG-SLRM 1380
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NLDPFSQYSD-----------EEVWTSLELAHLKDFVsalpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLDE 1449
Cdd:PRK10895 98 NLMAVLQIRDdlsaeqredraNELMEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1450 ATAAVD-LETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQ 1510
Cdd:PRK10895 164 PFAGVDpISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
696-844 |
5.20e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 69.12 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFT----WARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHVAIKGVN-------- 761
Cdd:cd03213 3 TLSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPldkrsfrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK 812
Cdd:cd03213 83 iigyvpqddilhptltvretlmfaaklrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS-------LLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462549072 813 -----NKTRILVTHSMSYL--PQVDVIIVMSGGKISEMG 844
Cdd:cd03213 156 rladtGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1287-1489 |
5.22e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYreDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINEsAEGEIIIDG--------INIAKIGLH 1358
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1359 DLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEV-W-TSLEL-----AHLKDfvSALPDKLDHECAEGGENLSVGQRQL 1431
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWrPKLEIddiveSALKD--ADLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1432 VCLARALLRKTKILVLDEATAAVD----LETDDLIQS-TIRTQFEDCTVLTIAHRLNTIMDYT 1489
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSELTMVIVSHNLHQVSRLSDFT 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
697-850 |
6.06e-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: 70.46 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:COG1120 2 LEAENLSV--GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarriay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 783
Cdd:COG1120 80 vpqeppapfgltvrelvalgryphlglfgrpsaedreaveealertglehladrpvdeLSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 784 LFDDPLSAVDAHvgkHIFEnvigpkgML---------KNKTRILVTHsmsYLPQV----DVIIVMSGGKISEMGSYQELL 850
Cdd:COG1120 160 LLDEPTSHLDLA---HQLE-------VLellrrlareRGRTVVMVLH---DLNLAaryaDRLVLLKDGRIVAQGPPEEVL 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
714-852 |
6.49e-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: 70.02 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGVN------------------------------ 761
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGEDltdskkdinklrrkvgmvfqqfnlfphltv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD----AH 795
Cdd:COG1126 95 lenvtlapikvkkmskaeaeeramellervgladkadaypaqLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvGE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 796 VgkhifENVIgpK-----GMlknkTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 852
Cdd:COG1126 175 V-----LDVM--RdlakeGM----TMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
697-842 |
7.42e-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: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGVN------------ 761
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLG-LLAGLDRPtSGTVRLAGQDlfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------------------------------------LSGGQKQRVSLARAVYSNADI 782
Cdd:COG4181 88 rarhvgfvfqsfqllptltalenvmlplelagrrdarararallervglghrldhypaqLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 783 YLFDDPLSAVDAHVGKHI----FEnvigpkgmlKNKTR----ILVTHSMSYLPQVDVIIVMSGGKISE 842
Cdd:COG4181 168 LFADEPTGNLDAATGEQIidllFE---------LNRERgttlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
966-1173 |
7.53e-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: 70.91 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 966 LFISFLSIFLfmcnhVSALASnywLSLWTDDPIVNGTQEHTKVRLSVYGALGI-----SQGIAVFG--YSMAVSIGGILA 1038
Cdd:cd18552 1 LALAILGMIL-----VAATTA---ALAWLLKPLLDDIFVEKDLEALLLVPLAIiglflLRGLASYLqtYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1039 SrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLA----TPIAAIIIP 1114
Cdd:cd18552 73 D--LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdwklTLIALVVLP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1115 PLGL-IYFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF----EEQERFIHQSD 1173
Cdd:cd18552 151 LAALpIRRIGKRLRKISRRSQESMGDLT-----SVLQETLSGIRVVKAFgaedYEIKRFRKANE 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1303-1514 |
8.05e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.04 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSG-SLR-- 1379
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1380 --------MNL-DPFSQYSDEEVWTSLELAHlkdfVSALPDKLdhecaegGENLSVGQRQLVCLARALLRKTKILVLDEA 1450
Cdd:PRK11231 97 vaygrspwLSLwGRLSAEDNARVNQAMEQTR----INHLADRR-------LTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1451 TAAVDL----ETDDLIQstiRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQRGL 1514
Cdd:PRK11231 166 TTYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYCdHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
714-840 |
8.98e-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: 8.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGVN------------------------------ 761
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKltddkkninelrqkvgmvfqqfnlfphltv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 799
Cdd:cd03262 94 lenitlapikvkgmskaeaeeralellekvgladkadaypaqLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549072 800 IFENV--IGPKGMlknkTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:cd03262 174 VLDVMkdLAEEGM----TMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1303-1503 |
1.23e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 68.76 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIaKIGLHDLRFKITIIPQDpvlFSGSLRMNL 1382
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQE---FGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 DPFSQY-----------SDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1451
Cdd:cd03264 90 REFLDYiawlkgipskeVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1452 AAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMD-YTRVIVLDKGEIQEYG 1503
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1287-1508 |
1.35e-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: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYRedlDFV-LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAK-------IGL- 1357
Cdd:cd03296 3 IEVRNVSKRFG---DFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpvqernVGFv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1358 --HDLRFK-ITIIpqDPVLFSgsLRM---NLDPFSQYSDEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQL 1431
Cdd:cd03296 80 fqHYALFRhMTVF--DNVAFG--LRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1432 VCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTI--AHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1508
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEVAdRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1303-1499 |
1.69e-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: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLhDLRFKITIIPQDPVLFSG-SLRMN 1381
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1382 LDPFSQYSdeevwtSLELAHLKDFVSALPDKLD--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1459
Cdd:cd03266 99 LEYFAGLY------GLKGDELTARLEELADRLGmeELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549072 1460 DLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEI 1499
Cdd:cd03266 173 RALREFIRQLRALgKCILFSTHIMQEVERLCdRVVVLHRGRV 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1303-1509 |
1.78e-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: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL-RFKITIIPQDPVLFSG-SLRM 1380
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NLD--PFSQYSDEEVWTSLELAH-----LKDFVSALpdkldhecaeGGeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1453
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLKERRRQR----------AG-TLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1454 -----VDlETDDLIQsTIRTqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1509
Cdd:COG0410 167 lapliVE-EIFEIIR-RLNR--EGVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
697-852 |
1.90e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLL---SAL--------------LAEMDK------- 750
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLerptsgsvlvdgvdLTALSErelraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 751 -----------------VEGHVA----IKGV---------------------------NLSGGQKQRVSLARAVYSNADI 782
Cdd:COG1135 82 rkigmifqhfnllssrtVAENVAlpleIAGVpkaeirkrvaellelvglsdkadaypsQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 783 YLFDDPLSAVDAHVGKHIFEnvigpkgMLK--NK----TRILVTHSMsylpqvDVI--I-----VMSGGKISEMGSYQEL 849
Cdd:COG1135 162 LLCDEATSALDPETTRSILD-------LLKdiNRelglTIVLITHEM------DVVrrIcdrvaVLENGRIVEQGPVLDV 228
|
...
gi 2462549072 850 LAR 852
Cdd:COG1135 229 FAN 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
747-849 |
2.02e-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: 68.42 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 747 EMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKN--KTRILVTH--- 821
Cdd:cd03300 116 DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL---KRLQKElgITFVFVTHdqe 192
|
90 100 110
....*....|....*....|....*....|.
gi 2462549072 822 ---SMSylpqvDVIIVMSGGKISEMGSYQEL 849
Cdd:cd03300 193 ealTMS-----DRIAVMNKGKIQQIGTPEEI 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1287-1511 |
2.57e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSS---LTLGLfriNESAEGEIIIDGINIAK--IGLHDlr 1361
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTvlrLVAGL---EKPTEGQIFIDGEDVTHrsIQQRD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1362 fkITIIPQDPVLFSG---------SLRMNLDPFSQYSdEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLV 1432
Cdd:PRK11432 80 --ICMVFQSYALFPHmslgenvgyGLKMLGVPKEERK-QRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1433 CLARALLRKTKILVLDEATAAVDLETDDLIQSTIR---TQFeDCTVLTIAHrlntimDYTR-------VIVLDKGEIQEY 1502
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTH------DQSEafavsdtVIVMNKGKIMQI 218
|
....*....
gi 2462549072 1503 GAPSDLLQQ 1511
Cdd:PRK11432 219 GSPQELYRQ 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
762-851 |
2.65e-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: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH-VGKHIfeNVIgpKGMLKNK-TRILVTHSMSYLPQV-DVIIVMSGG 838
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPElVGEVL--NTI--RQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQG 220
|
90
....*....|...
gi 2462549072 839 KISEMGSYQELLA 851
Cdd:PRK11264 221 RIVEQGPAKALFA 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1303-1509 |
3.75e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1382
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 DPFSQYSDEEVWTSLELAHLKDFVSAL-PDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-- 1459
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQid 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1460 --DLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK10253 182 llELLSELNREK--GYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1269-1503 |
5.19e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1269 PWQIQETAPPSSWPQVGRVEF--RNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEII 1346
Cdd:PRK15134 265 PVPLPEPASPLLDVEQLQVAFpiRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1347 IDGINIAKIG---LHDLRFKITIIPQDPvlfSGSL--RMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDK--LDHEC-- 1417
Cdd:PRK15134 344 FDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLnpRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvgLDPETrh 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1418 ---AEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDYT-RV 1491
Cdd:PRK15134 421 rypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHDLHVVRALChQV 496
|
250
....*....|..
gi 2462549072 1492 IVLDKGEIQEYG 1503
Cdd:PRK15134 497 IVLRQGEVVEQG 508
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
697-858 |
5.39e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.12 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMD---KVEG----------------- 753
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLPEAgtiTVGGmvlseetvwdvrrqvgm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 754 ------------------------------------HVAIKGVN-----------LSGGQKQRVSLARAVYSNADIYLFD 786
Cdd:PRK13635 86 vfqnpdnqfvgatvqddvafglenigvpreemvervDQALRQVGmedflnrephrLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 787 DPLSAVDAhVGKhifENVIGPKGMLKNKTRILV---THSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 858
Cdd:PRK13635 166 EATSMLDP-RGR---REVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1304-1455 |
6.17e-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: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRINESAEGEIIIDGINIAKIGLHDLRfkITIIPQDPVLFS----- 1375
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLlaaIAGTLSPAFSASGEVLLNGRRLTALPAEQRR--IGILFQDDLLFPhlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1376 GSLRMNLDPFSQYSD--EEVWTSLELAHLKDFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1453
Cdd:COG4136 95 ENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 2462549072 1454 VD 1455
Cdd:COG4136 164 LD 165
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
697-840 |
7.32e-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: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNatFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:COG4619 1 LELEG--LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrqvay 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 789
Cdd:COG4619 79 vpqepalwggtvrdnlpfpfqlrerkfdreralellerlglppdildkpverLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 790 SAVDAHvGKHIFENVIgpKGMLKNKTR--ILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:COG4619 159 SALDPE-NTRRVEELL--REYLAEEGRavLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
714-849 |
7.49e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.59 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKG--------------------------------- 759
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLEKpTEGQIFIDGedvthrsiqqrdicmvfqsyalfphmslgenvg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 -----------------------VNL-----------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVI 805
Cdd:PRK11432 101 yglkmlgvpkeerkqrvkealelVDLagfedryvdqiSGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462549072 806 GPKGMLkNKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQEL 849
Cdd:PRK11432 181 ELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1303-1511 |
8.90e-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: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGINIAKIGLHDlRFK--ITIIPQDPVLFSGsl 1378
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1379 rmnldpfsqysdeevwtslelAHLKDFVSALpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1458
Cdd:cd03217 92 ---------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1459 DDLIQSTIRT-QFEDCTVLTIAHRLNtIMDY---TRVIVLDKGEIQEYGaPSDLLQQ 1511
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1296-1501 |
9.69e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1296 YREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFS 1375
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1376 GSLRMNLD-PF---SQYSDEEVWtsleLAHLKDFvsALPDK-LDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1450
Cdd:PRK10247 95 DTVYDNLIfPWqirNQQPDPAIF----LDDLERF--ALPDTiLTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1451 TAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDK--GEIQE 1501
Cdd:PRK10247 165 TSALDesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITLQPhaGEMQE 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1303-1503 |
1.56e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFRINESAEgeiiidgINIAkiglhDLRFKITIIPQDPVLFSgsLRM 1380
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEMPRSGT-------LNIA-----GNHFDFSKTPSDKAIRE--LRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NLD-PFSQY----------------------SDEEVWTS----LELAHLKDFVSALPdkldhecaeggENLSVGQRQLVC 1433
Cdd:PRK11124 83 NVGmVFQQYnlwphltvqqnlieapcrvlglSKDQALARaeklLERLRLKPYADRFP-----------LHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1434 LARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYG 1503
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQG 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
700-840 |
1.87e-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: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 700 RNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALL--------------------------------- 745
Cdd:cd03248 15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqggqvlldgkpisqyehkylhskvslvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 746 --------------------AEMDKV-------EGHVAI-------------KGVNLSGGQKQRVSLARAVYSNADIYLF 785
Cdd:cd03248 95 qepvlfarslqdniayglqsCSFECVkeaaqkaHAHSFIselasgydtevgeKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 786 DDPLSAVDAHvGKHIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKI 840
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 ... |
1303-1499 |
2.30e-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: 63.99 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQDPvlfsgsLRMN 1381
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDR------KREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1382 LdpFSQYSdeeVWTSLELAHLkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1461
Cdd:cd03215 89 L--VLDLS---VAENIALSSL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549072 1462 IQSTIRTQFED-CTVLTIAHRLNTIM---DytRVIVLDKGEI 1499
Cdd:cd03215 143 IYRLIRELADAgKAVLLISSELDELLglcD--RILVMYEGRI 182
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1301-1525 |
2.45e-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: 67.05 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1301 DFVLRhINVTINGGEKVGIVGRTGAGKSSLtL----GLFRineSAEGEIIIDG---------INIA----KIGLhdlrfk 1363
Cdd:COG4148 13 GFTLD-VDFTLPGRGVTALFGPSGSGKTTL-LraiaGLER---PDSGRIRLGGevlqdsargIFLPphrrRIGY------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1364 itiIPQDPVLFSG-SLRMNLD--------PFSQYSDEEVWTSLELAHLkdfvsalpdkLDHecaeGGENLSVGQRQLVCL 1434
Cdd:COG4148 82 ---VFQEARLFPHlSVRGNLLygrkraprAERRISFDEVVELLGIGHL----------LDR----RPATLSGGERQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1435 ARALLRKTKILVLDEATAAVDLETDDLIQ---STIRTQFeDCTVLTIAHRLNTIM---DytRVIVLDKGEIQEYGAPSDL 1508
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVArlaD--HVVLLEQGRVVASGPLAEV 221
|
250
....*....|....*...
gi 2462549072 1509 LQQRGLF-YSMAKDAGLV 1525
Cdd:COG4148 222 LSRPDLLpLAGGEEAGSV 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
760-851 |
2.45e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvIGPKGMLKNKTRILVTHSMSYLPQVDV-IIVMSGG 838
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQG 228
|
90
....*....|...
gi 2462549072 839 KISEMGSYQELLA 851
Cdd:PRK10619 229 KIEEEGAPEQLFG 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
746-844 |
2.53e-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: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 746 AEMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhiFENVIGPKGMLKN--KTRILVTHSm 823
Cdd:cd03301 115 AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR---VQMRAELKRLQQRlgTTTIYVTHD- 190
|
90 100
....*....|....*....|....*..
gi 2462549072 824 sylpQV------DVIIVMSGGKISEMG 844
Cdd:cd03301 191 ----QVeamtmaDRIAVMNDGQIQQIG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
713-840 |
3.19e-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: 64.20 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 713 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN------------------------------- 761
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrksigyvmqdvdyqlftdsvreell 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 --------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIFEnvI 805
Cdd:cd03226 95 lglkeldagneqaetvlkdldlyalkerhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerVGELIRE--L 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462549072 806 GPKGmlknKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:cd03226 173 AAQG----KAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1303-1494 |
3.23e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGINIAKIGLH---DLRFKITIIpqDPV---LFS 1375
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQRsevPDSLPLTVR--DLVamgRWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1376 --GSLRmnldPFSQYSDEEVWTSLELAHLKDFVSAlpdKLDhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1453
Cdd:NF040873 85 rrGLWR----RLTRDDRAAVDDALERVGLADLAGR---QLG--------ELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549072 1454 VDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVL 1494
Cdd:NF040873 150 LDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
692-849 |
3.29e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 692 GGTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---------------- 755
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 756 -------------------------------------------AIKGVN-----------LSGGQKQRVSLARAVYSNAD 781
Cdd:PRK13648 83 khigivfqnpdnqfvgsivkydvafglenhavpydemhrrvseALKQVDmleradyepnaLSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 782 IYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQEL 849
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSE-HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1287-1509 |
3.59e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.58 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNY--CLRYREDLdFVLRHINV------TINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglH 1358
Cdd:PRK15112 5 LEVRNLskTFRYRTGW-FRRQTVEAvkplsfTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD--------H 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1359 DLRF--------KITIIPQDPV-----------LFSGSLRMNLDPFSQYSDEEVWTSL-ELAHLKDFVSALPdkldheca 1418
Cdd:PRK15112 76 PLHFgdysyrsqRIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYP-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1419 eggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetddliqsTIRTQFEDCTV-LTIAHRLNTI--------MDYT 1489
Cdd:PRK15112 148 ---HMLAPGQKQRLGLARALILRPKVIIADEALASLDM--------SMRSQLINLMLeLQEKQGISYIyvtqhlgmMKHI 216
|
250 260
....*....|....*....|..
gi 2462549072 1490 --RVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK15112 217 sdQVLVMHQGEVVERGSTADVL 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1266-1503 |
4.21e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1266 KEAPWQiqetaPPSSWPQVGRVEFRNYclryredldfvlrhinvtinGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1345
Cdd:PRK15079 24 KQWFWQ-----PPKTLKAVDGVTLRLY--------------------EGETLGVVGESGCGKSTFARAIIGLVKATDGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1346 IIDGINIAKIG---LHDLRFKITIIPQDPvLFSGSLRMNL-----DPFSQY----SDEEVWTSLELAHLKdfVSALPDKL 1413
Cdd:PRK15079 79 AWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPRMTIgeiiaEPLRTYhpklSRQEVKDRVKAMMLK--VGLLPNLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1414 D---HEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLEtddlIQSTI-----RTQFE-DCTVLTIAHRLNT 1484
Cdd:PRK15079 156 NrypHE-------FSGGQCQRIGIARALILEPKLIICDEPVSALDVS----IQAQVvnllqQLQREmGLSLIFIAHDLAV 224
|
250 260
....*....|....*....|..
gi 2462549072 1485 ---IMDytRVIVLDKGEIQEYG 1503
Cdd:PRK15079 225 vkhISD--RVLVMYLGHAVELG 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
697-794 |
5.02e-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: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRN--ATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS-------------------------------- 742
Cdd:COG4525 4 LTVRHvsVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNliagflapssgeitldgvpvtgpgadrgvvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 743 --ALLAEMDKVEgHVA----IKGVN---------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 789
Cdd:COG4525 84 kdALLPWLNVLD-NVAfglrLRGVPkaerraraeellalvgladfarrriwqLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
....*
gi 2462549072 790 SAVDA 794
Cdd:COG4525 163 GALDA 167
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1303-1511 |
5.66e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSgSLRMNL 1382
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRT-RLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 DPFSQYSDEEVWTS----------LELAHLKDFVSALPDKLDHECAEGGE---NLSVGQRQLVCLARALLRKTKILVLDE 1449
Cdd:PRK10619 99 QHFNLWSHMTVLENvmeapiqvlgLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1450 ATAAVDLE-TDDLIQSTIRTQFEDCTVLTIAHRlntiMDYTR-----VIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:PRK10619 179 PTSALDPElVGEVLRIMQQLAEEGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFGN 242
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1304-1511 |
5.80e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI-AKIG---LHDLRFKITIIPQDP--VLFSGS 1377
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1378 L-----------RMNLDPFSQYSDEEVwtsLELAHLKDFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILV 1446
Cdd:PRK13646 103 VereiifgpknfKMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQ-----------MSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1447 LDEATAAVDLETDDLIQSTIRT-QFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSlQTDENkTIILVSHDMNEVARYAdEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1304-1503 |
5.96e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLrfkITIIPQD-------PVLFSG 1376
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 SLRMnldpfSQYSDEEvWTSLELAHLKDFVS---ALPDKLDHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 1453
Cdd:PRK15056 100 VVMM-----GRYGHMG-WLRRAKKRDRQIVTaalARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1454 VDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYG 1503
Cdd:PRK15056 173 VDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
762-861 |
6.40e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.34 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFENV---IGPKGMlknkTRILVTHSMSYLPQVDV-IIVMSG 837
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL-RHEVLKVmqdLAEEGM----TMVIVTHEIGFAEKVASrLIFIDK 211
|
90 100
....*....|....*....|....*.
gi 2462549072 838 GKISEMGSYQELLAR--DGAFAEFLR 861
Cdd:PRK09493 212 GRIAEDGDPQVLIKNppSQRLQEFLQ 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
697-805 |
8.52e-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: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:COG4133 3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrrlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ---------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLS 790
Cdd:COG4133 81 ghadglkpeltvrenlrfwaalyglradreaidealeavglagladlpvrqLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170
....*....|....*
gi 2462549072 791 AVDAHvGKHIFENVI 805
Cdd:COG4133 161 ALDAA-GVALLAELI 174
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1303-1499 |
9.49e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.93 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdginiAKIGLHDLRFKITIIPQDPVLF-------- 1374
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLMFQDARLLpwkkvidn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1375 -----SGSLRmnldpfsqysdEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDE 1449
Cdd:PRK11247 102 vglglKGQWR-----------DAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1450 ATAAVD----LETDDLIQSTIRTQ-FedcTVLTIAHRLN---TIMDytRVIVLDKGEI 1499
Cdd:PRK11247 160 PLGALDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGKI 212
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1302-1499 |
1.01e-10 |
|
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: 62.57 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1302 FVLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGINiakIGLHDLRFKITIIPQDPVLFsGSL- 1378
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILH-PTLt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1379 -RMNLDpFSqysdeevwtslelAHLKdfvsalpdkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1457
Cdd:cd03213 99 vRETLM-FA-------------AKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462549072 1458 TDDLIQSTIRtQFED--CTVLTIAHRLNTIMDYT--RVIVLDKGEI 1499
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFELfdKLLLLSQGRV 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
748-848 |
1.03e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.35 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 748 MDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHifenvigpkgM---LK------NKTRIL 818
Cdd:PRK09452 131 MVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ----------MqneLKalqrklGITFVF 200
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462549072 819 VTH------SMSylpqvDVIIVMSGGKISEMGSYQE 848
Cdd:PRK09452 201 VTHdqeealTMS-----DRIVVMRDGRIEQDGTPRE 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1303-1511 |
1.18e-10 |
|
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: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSL--TLGlfRINESAEGEIIIDGiNIAKI-----GLH-DL--RfkitiipqDPV 1372
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLlkLIA--GILEPTSGRVEVNG-RVSALlelgaGFHpELtgR--------ENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1373 LFSGSLrMNLDPfSQYSD--EEVwtsLELAHLKDFVSaLPDKldhecaeggeNLSVGQRqlvclAR-----ALLRKTKIL 1445
Cdd:COG1134 110 YLNGRL-LGLSR-KEIDEkfDEI---VEFAELGDFID-QPVK----------TYSSGMR-----ARlafavATAVDPDIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1446 VLDEATAAVDLE----TDDLIQSTIRtqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:COG1134 169 LVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
761-852 |
1.26e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 65.12 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI---FENvigpkgmLKNKTRI---LVTHSMsylPQV----D 830
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIlpyLER-------LRDELDIpilYVSHSL---DEVarlaD 202
|
90 100
....*....|....*....|..
gi 2462549072 831 VIIVMSGGKISEMGSYQELLAR 852
Cdd:COG4148 203 HVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1314-1503 |
1.26e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1314 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHDLRFKITIIPQDPVlfsgslrMNLDPFSQ--Y 1388
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDPRQTvgD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1389 SDEE---VWTSLE-------LAHLKDFVSALPD---KLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1455
Cdd:PRK10261 423 SIMEplrVHGLLPgkaaaarVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1456 LET-DDLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYG 1503
Cdd:PRK10261 496 VSIrGQIINLLLDLQRDfGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1293-1503 |
1.27e-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: 62.70 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1293 CLRYREDLDFVLRHINVTINGgEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGINI----AKIGLHDLRFKIT 1365
Cdd:cd03297 3 CVDIEKRLPDFTLKIDFDLNE-EVTGIFGASGAGKSTLlrcIAGLEKPDG---GTIVLNGTVLfdsrKKINLPPQQRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1366 IIPQDPVLFSG-SLRMNL--------DPFSQYSDEEVWTSLELAHLKDfvsALPDKLdhecaeggenlSVGQRQLVCLAR 1436
Cdd:cd03297 79 LVFQQYALFPHlNVRENLafglkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1437 ALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYG 1503
Cdd:cd03297 145 ALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLAdRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1303-1511 |
1.32e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 64.78 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLfrinESA-EGEIIIDGiNIAKIGLHDLRFKITIIPQDPVLFS-- 1375
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL-LriiaGL----ETPdSGRIVLNG-RDLFTNLPPRERRVGFVFQHYALFPhm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1376 --------GsLRMnLDPFSQYSDEEVWTSLELAHLKDFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVL 1447
Cdd:COG1118 91 tvaeniafG-LRV-RPPSKAEIRARVEELLELVQLEGLADRYPS-----------QLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1448 DEATAAVDletddliqSTIRTQFE----------DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:COG1118 158 DEPFGALD--------AKVRKELRrwlrrlhdelGGTTVFVTHDQEEALELAdRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
697-840 |
1.42e-10 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 63.15 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalrgralrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 -----------------------------------------------------------------LSGGQKQRVSLARAV 776
Cdd:COG3638 82 igmifqqfnlvprlsvltnvlagrlgrtstwrsllglfppedreralealervgladkayqradqLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 777 YSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHsmsylpQVDV-------IIVMSGGKI 840
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMD-------LLRriaredGITVVVNLH------QVDLarryadrIIGLRDGRV 225
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
966-1257 |
1.51e-10 |
|
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: 63.96 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 966 LFISFLSIFLFMcnhVSALASNYWLSLWTDDpIVNGTQEHTKVRLS-VYGALGISQGIAVFG--------YSMAVSIGGI 1036
Cdd:cd18547 1 LILVIILAIIST---LLSVLGPYLLGKAIDL-IIEGLGGGGGVDFSgLLRILLLLLGLYLLSalfsylqnRLMARVSQRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1037 LASrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGAcIVILLAT--PIAAIIIP 1114
Cdd:cd18547 77 VYD--LRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGT-LIMMLYIspLLTLIVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1115 PLGLIYFFV-------QRFYVASSRQLKRLEsvsrspvySHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSI 1187
Cdd:cd18547 154 TVPLSLLVTkfiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQ 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 1188 VANRWL--AVRLecVGN----CIVLFAALFAVisRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVER 1257
Cdd:cd18547 226 FYSGLLmpIMNF--INNlgyvLVAVVGGLLVI--NGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1305-1495 |
1.59e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1305 RHINVTINGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGINIAKIG---LHDLrfkitiipqdpvLFSG-- 1376
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLlrILaGLAR---PDAGEVLWQGEPIRRQRdeyHQDL------------LYLGhq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 -----------SLRMNLDPFSQYSDEEVWTSLELAHLKDFvsalpdkLDHECAeggeNLSVGQRQLVCLARALLRKTKIL 1445
Cdd:PRK13538 83 pgikteltaleNLRFYQRLHGPGDDEALWEALAQVGLAGF-------EDVPVR----QLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1446 VLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLD 1495
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQggMVILTTHQDLPVASDKVRKLRLG 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
762-860 |
1.59e-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: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgkHIFENVIgpkGMLK------NKTRILVTHSMS-YLPQVDVIIV 834
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDV----RTKEKLR---EELKkirkefGVTVLHVTHDFEeAWALADKVAI 202
|
90 100
....*....|....*....|....*...
gi 2462549072 835 MSGGKISEMGSYQELLAR--DGAFAEFL 860
Cdd:cd03299 203 MLNGKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
762-849 |
1.70e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.72 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNkTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKF-TSVFVTHDQEEAMEVaDRVVVMSQGNI 215
|
....*....
gi 2462549072 841 SEMGSYQEL 849
Cdd:PRK10851 216 EQAGTPDQV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1254-1502 |
1.72e-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: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1254 AVERLKEYSETEKEAPWQIQETAPPSSWPQVgrVEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSltlg 1333
Cdd:COG0488 285 ALEKLEREEPPRRDKTVEIRFPPPERLGKKV--LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1334 LFRI----NESAEGEIIIdGINIakiglhdlrfKITIIPQDPVLFSGSLRMnLDPFSQYSDEevWTSLEL-AHLKDFvsa 1408
Cdd:COG0488 357 LLKLlageLEPDSGTVKL-GETV----------KIGYFDQHQEELDPDKTV-LDELRDGAPG--GTEQEVrGYLGRF--- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1409 L--PDKLDHECaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETddliqstiRTQFEDC------TVLTIAH 1480
Cdd:COG0488 420 LfsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgTVLLVSH 487
|
250 260
....*....|....*....|....*
gi 2462549072 1481 -R--LNTIMDytRVIVLDKGEIQEY 1502
Cdd:COG0488 488 dRyfLDRVAT--RILEFEDGGVREY 510
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1294-1514 |
1.87e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1294 LRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHDLRFKITIIPQDP 1371
Cdd:PRK13638 9 FRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1372 vlfsgslrmNLDPFSQYSDEEVWTSL--------ELAHLKDFVSALPDKlDHECAEGGENLSVGQRQLVCLARALLRKTK 1443
Cdd:PRK13638 87 ---------EQQIFYTDIDSDIAFSLrnlgvpeaEITRRVDEALTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1444 ILVLDEATAAVDLE-TDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAP------SDLLQQRGL 1514
Cdd:PRK13638 157 YLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISdAVYVLRQGQILTHGAPgevfacTEAMEQAGL 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1303-1489 |
1.87e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidginiakiglHDLRFKITIIPQ----DPVL-FSGS 1377
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1378 LRMNLDPFSQYSD-EEVWTSLELAHLKDFVSalpdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVD- 1455
Cdd:PRK09544 88 RFLRLRPGTKKEDiLPALKRVQAGHLIDAPM--------------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDv 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462549072 1456 ---LETDDLIQStIRTQFeDCTVLTIAHRLNTIMDYT 1489
Cdd:PRK09544 154 ngqVALYDLIDQ-LRREL-DCAVLMVSHDLHLVMAKT 188
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1257-1511 |
2.00e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.08 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1257 RLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFR 1336
Cdd:PRK13536 12 RRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1337 INESAEGEIIIDGINI-AKIGLhdLRFKITIIPQ-DPVLFSGSLRMNLDPFSQY------SDEEVWTSL-ELAHLKDfvs 1407
Cdd:PRK13536 90 MTSPDAGKITVLGVPVpARARL--ARARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstrEIEAVIPSLlEFARLES--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1408 alpdKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-EDCTVLTIAHrlntIM 1486
Cdd:PRK13536 165 ----KADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FM 232
|
250 260 270
....*....|....*....|....*....|
gi 2462549072 1487 DYT-----RVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:PRK13536 233 EEAerlcdRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1013-1184 |
2.27e-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: 63.65 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1013 YGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSL 1092
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1093 FNVIGACIV----------ILLATpiaaiiIPPLGLIYFFVQRFYV-ASSRQLKRLESVSrspvySHFNETLLGVSVIRA 1161
Cdd:cd18577 133 STFIAGFIIafiyswkltlVLLAT------LPLIAIVGGIMGKLLSkYTKKEQEAYAKAG-----SIAEEALSSIRTVKA 201
|
170 180
....*....|....*....|...
gi 2462549072 1162 FEEQERFIHQSDLKVDENQKAYY 1184
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAGI 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1307-1511 |
2.34e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1307 INVTINGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG---INIAKIGLHDLRF-KITIIPQDPVlfsgslr 1379
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAfalMGLLAANGRIGGSATFNGreiLNLPEKELNKLRAeQISMIFQDPM------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1380 MNLDPFSQYSDE--EVwtsLELAHLKDFVSALPDK---LD---------------HEcaeggenLSVGQRQLVCLARALL 1439
Cdd:PRK09473 108 TSLNPYMRVGEQlmEV---LMLHKGMSKAEAFEESvrmLDavkmpearkrmkmypHE-------FSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1440 RKTKILVLDEATAAVDLEtddlIQSTIRTQFED------CTVLTIAHRLNT---IMDytRVIVLDKGEIQEYGAPSDLLQ 1510
Cdd:PRK09473 178 CRPKLLIADEPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVvagICD--KVLVMYAGRTMEYGNARDVFY 251
|
.
gi 2462549072 1511 Q 1511
Cdd:PRK09473 252 Q 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
693-853 |
2.35e-10 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 62.69 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 693 GTNSITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN----------- 761
Cdd:COG1127 2 SEPMIEVRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglsekelye 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 --------------------------------------------------------------LSGGQKQRVSLARAVYSN 779
Cdd:COG1127 80 lrrrigmlfqggalfdsltvfenvafplrehtdlseaeirelvleklelvglpgaadkmpseLSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 780 ADIYLFDDPLSAVDAhVGKHIFENVIgpkgmLK-----NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARD 853
Cdd:COG1127 160 PEILLYDEPTAGLDP-ITSAVIDELI-----RElrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLASD 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1303-1509 |
2.47e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.76 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGI------NIAKIGLHDLRFKITIIPQDPVLFSG 1376
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 -SLRMNLD-PFSQY---SDEEVWTSLELAHLK-DFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1450
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEECLRKvGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1451 TAAVDLETDDLIQSTIRTQFEDCTVLTIAH---RLNTIMDYtrVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEWGSSNEIF 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1303-1509 |
2.54e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFRINESAE---GEIIIDG---INIAKIGLHDLRFKITIIPQDpvlf 1374
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTirvGDITIDTarsLSQQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1375 sgslrMNLDPFSqysdeevwTSLE---------LAHLKDFVSALPDKLDHECA-EGGEN-----LSVGQRQLVCLARALL 1439
Cdd:PRK11264 94 -----FNLFPHR--------TVLEniiegpvivKGEPKEEATARARELLAKVGlAGKETsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1440 RKTKILVLDEATAAVDLETDDLIQSTIRTQFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1304-1486 |
2.73e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDGINIAKIGLHDLRFK-ITIIPQDPVL------- 1373
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAgIAIIHQELALvkelsvl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1374 ---FSGSL-----RMNLDpfSQYSDEEVWtsleLAHLKdfvsalpdkLDHECAEGGENLSVGQRQLVCLARALLRKTKIL 1445
Cdd:PRK13549 101 eniFLGNEitpggIMDYD--AMYLRAQKL----LAQLK---------LDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462549072 1446 VLDEATAAV-DLETDDLIqSTIRT-QFEDCTVLTIAHRLNTIM 1486
Cdd:PRK13549 166 ILDEPTASLtESETAVLL-DIIRDlKAHGIACIYISHKLNEVK 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1301-1468 |
3.06e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1301 DFVLRHINVTINGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGiniAKIGLHDLRFKITII-PQD---PVL 1373
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrLIaGLLPP---AAGTIKLDG---GDIDDPDVAEACHYLgHRNamkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1374 fsgSLRMNLDpF-------SQYSDEEVWTSLELAHLKDfvsaLPdkldhecaegGENLSVGQRQLVCLARALLRKTKILV 1446
Cdd:PRK13539 89 ---TVAENLE-FwaaflggEELDIAAALEAVGLAPLAH----LP----------FGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180
....*....|....*....|..
gi 2462549072 1447 LDEATAAVDLETDDLIQSTIRT 1468
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRA 172
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
695-849 |
3.68e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 695 NSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALLAEMDKVEGHVAIKGV----------- 760
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGItltaktvwdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 -----------------------------------------------------------NLSGGQKQRVSLARAVYSNAD 781
Cdd:PRK13640 84 ekvgivfqnpdnqfvgatvgddvafglenravprpemikivrdvladvgmldyidsepaNLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 782 IYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQEL 849
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKK-NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1288-1511 |
3.70e-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: 64.32 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1288 EFRNYCLRYREDLDF--VLRHINVTINGGEKVGIVGRTGAGKS--SL-TLGLF-RINESAEGEIIIDGINIAKIGLHDLR 1361
Cdd:COG4172 8 SVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtALsILRLLpDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1362 ----FKITIIPQDPvlfsgslrMN-LDPfsqysdeeVWT-------SLELaHLKdfVSA---------------LPD--- 1411
Cdd:COG4172 88 rirgNRIAMIFQEP--------MTsLNP--------LHTigkqiaeVLRL-HRG--LSGaaararalellervgIPDper 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1412 KLD---HEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetddliqsTIRTQF----------EDCTVLTI 1478
Cdd:COG4172 149 RLDaypHQ-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV--------TVQAQIldllkdlqreLGMALLLI 213
|
250 260 270
....*....|....*....|....*....|....
gi 2462549072 1479 AHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:COG4172 214 THDLGVVRRFAdRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1304-1489 |
3.98e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.49 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLHDLRFKITIIPQDPVLFSG 1376
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 SLRMNL------DPFSQYSDEEVWTSLELAHLKDFVSalpDKLDhecaEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1450
Cdd:PRK14243 106 SIYDNIaygariNGYKGDMDELVERSLRQAALWDEVK---DKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549072 1451 TAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNT---IMDYT 1489
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQaarVSDMT 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1303-1503 |
4.71e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLG---LFRINESA--EGEIIIDGINI--AKIGLHDLRFKITIIPQDPVLF- 1374
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1375 ------SGSLRMNLDPFSQySDEEVWTSLELAHLKdfvSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1448
Cdd:PRK14267 99 hltiydNVAIGVKLNGLVK-SKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1449 EATAAVDLETDDLIQSTIRTQFEDCTVLTIAH---RLNTIMDYTRVIVLdkGEIQEYG 1503
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYL--GKLIEVG 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
762-840 |
4.92e-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: 61.16 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFENVIgpKGMLK--NKTRILVTHSMSYLPQV-DVIIVMSGG 838
Cdd:cd03297 132 LSGGEKQRVALARALAAQPELLLLDEPFSALDRAL-RLQLLPEL--KQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDG 208
|
..
gi 2462549072 839 KI 840
Cdd:cd03297 209 RL 210
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
966-1224 |
5.14e-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: 62.49 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 966 LFISFLSIFLFMcnhVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFG--YSMAVSIGGILASrcLH 1043
Cdd:cd18545 2 LLLALLLMLLST---AASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLriYLMAKVGQRILYD--LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1044 VDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGAcIVILLA-----TPIAAIIIPPLGL 1118
Cdd:cd18545 77 QDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGI-VIIMFSlnvrlALVTLAVLPLLVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1119 IYFFVQRFyvasSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANR--WLAVR 1196
Cdd:cd18545 156 VVFLLRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNAlfWPLVE 231
|
250 260
....*....|....*....|....*....
gi 2462549072 1197 L-ECVGNCIVLFAALFAVISrHSLSAGLV 1224
Cdd:cd18545 232 LiSALGTALVYWYGGKLVLG-GAITVGVL 259
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
721-868 |
5.17e-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: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 721 IPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG---------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 791
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGitpvykpqyIDLSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 792 VDAHVGKHIfENVIGPKGMLKNKTRILVTHSMSYLPQV-DVIIVMSGgkisEMGSYQELLARDG---AFAEFLRTYASTE 867
Cdd:cd03222 102 LDIEQRLNA-ARAIRRLSEEGKKTALVVEHDLAVLDYLsDRIHVFEG----EPGVYGIASQPKGtreGINRFLRGYLITF 176
|
.
gi 2462549072 868 Q 868
Cdd:cd03222 177 R 177
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1303-1507 |
5.67e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKIGLHDlRFKITIIPQ----------DP 1371
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV-LRLIAGFETPdSGRIMLDGQDITHVPAEN-RHVNTVFQSyalfphmtvfEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1372 VLFSgsLRMNLDPFSQYsDEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1451
Cdd:PRK09452 107 VAFG--LRMQKTPAAEI-TPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1452 AAVDLETDDLIQSTIRT-QFE-DCTVLTIAHRLN---TIMDytRVIVLDKGEIQEYGAPSD 1507
Cdd:PRK09452 173 SALDYKLRKQMQNELKAlQRKlGITFVFVTHDQEealTMSD--RIVVMRDGRIEQDGTPRE 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
714-852 |
6.09e-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: 62.38 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVAIKGVN----------------------------- 761
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDGEDllklsekelrkirgreiqmifqdpmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 --------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSA 791
Cdd:COG0444 101 pvmtvgdqiaeplrihgglskaeareraiellervglpdperrldrypheLSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 792 VDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 852
Cdd:COG0444 181 LDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1287-1503 |
6.48e-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: 60.73 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDlRfKITI 1366
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-R-DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDPVLF---------SGSLRMNLDPFSQYSD--EEVWTSLELAHLkdfvsalpdkLDHECAEggenLSVGQRQLVCLA 1435
Cdd:cd03301 77 VFQNYALYphmtvydniAFGLKLRKVPKDEIDErvREVAELLQIEHL----------LDRKPKQ----LSGGQRQRVALG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1436 RALLRKTKILVLDEATAAVDLetddLIQSTIRTQFEdctvlTIAHRLNTIMDY------------TRVIVLDKGEIQEYG 1503
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDA----KLRVQMRAELK-----RLQQRLGTTTIYvthdqveamtmaDRIAVMNDGQIQQIG 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1303-1510 |
7.10e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQD-PVLFSGSLRM- 1380
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVREl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 ----------NLDPFSQYSDEEVWTSLELAHLKDFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEA 1450
Cdd:PRK10575 106 vaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1451 TAAVDL----ETDDLIQSTirTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQ 1510
Cdd:PRK10575 175 TSALDIahqvDVLALVHRL--SQERGLTVIAVLHDINMAARYCdYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
696-848 |
7.18e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWARSDP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN----------- 761
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ---------------------------------------------------------------LSGGQKQRVSLARAVYS 778
Cdd:PRK13637 82 rkkvglvfqypeyqlfeetiekdiafgpinlglseeeienrvkramnivgldyedykdkspfeLSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 779 NADIYLFDDPLSAVDAHVGKHIFENVigpKGMLK--NKTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSYQE 848
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKI---KELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
974-1257 |
7.19e-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: 61.79 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 974 FLFMCnhVSALAS---NYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVF--GYSMAVsIGGILASRcLHVDLLH 1048
Cdd:cd18572 2 FVFLV--VAALSElaiPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGlrGGCFSY-AGTRLVRR-LRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1049 SILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQ 1124
Cdd:cd18572 78 SLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1125 RFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF--EEQE--RFIHQSDLKVDENQK---AYypsiVANRWLAVRL 1197
Cdd:cd18572 158 RYY----RKLSKEIQDALAEANQVAEEALSNIRTVRSFatEEREarRYERALDKALKLSVRqalAY----AGYVAVNTLL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1198 ECVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVER 1257
Cdd:cd18572 230 QNGTQVLVLFYGGHLVLS-GRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEK 288
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1303-1500 |
7.35e-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: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGI--------NIAKIGLHdLRFKITIIPQDPVLf 1374
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkFLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1375 sGSLRMNLDPFSqysdeevwtsLELAHLKDFVSALPDKLD--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1452
Cdd:cd03267 114 -DSFYLLAAIYD----------LPPARFKKRLDELSELLDleELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1453 AVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDY-TRVIVLDKGEIQ 1500
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKGRLL 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1304-1510 |
8.81e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSL----------TLGLFRINEsaegEIIIDGINIAKigLHDLRFKITIIPQDP-- 1371
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlngllqpTSGTVTIGE----RVITAGKKNKK--LKPLRKKVGIVFQFPeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1372 VLFSGSLR-------MNLDpfsqYSDEEvwtSLELA-HLKDFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTK 1443
Cdd:PRK13634 97 QLFEETVEkdicfgpMNFG----VSEED---AKQKArEMIELVGLPEELLARSPFE----LSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1444 ILVLDEATAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQ 1510
Cdd:PRK13634 166 VLVLDEPTAGLDpkgrKEMMEMFYKLHKEK--GLTTVLVTHSMEDAARYAdQIVVMHKGTVFLQGTPREIFA 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
696-852 |
9.29e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG--VN----------- 761
Cdd:PRK11650 3 GLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGrvVNelepadrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ------------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDD 787
Cdd:PRK11650 81 vfqnyalyphmsvrenmayglkirgmpkaeieervaeaarileleplldrkpreLSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 788 PLSAVDAHVGKHifenvigpkgM---LK------NKTRILVTHSmsylpQV------DVIIVMSGGKISEMGSYQELLAR 852
Cdd:PRK11650 161 PLSNLDAKLRVQ----------MrleIQrlhrrlKTTSLYVTHD-----QVeamtlaDRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
761-852 |
1.02e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.13 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK--NK----TRILVTHSMSYLPQV-DVII 833
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdiNRelglTIVLITHEMDVVKRIcDRVA 212
|
90
....*....|....*....
gi 2462549072 834 VMSGGKISEMGSYQELLAR 852
Cdd:PRK11153 213 VIDAGRLVEQGTVSEVFSH 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
753-852 |
1.16e-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: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 753 GHVAIKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI---FENvigpkgmLKNKTRI---LVTHSMSY 825
Cdd:TIGR02142 122 GHLLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIlpyLER-------LHAEFGIpilYVSHSLQE 194
|
90 100
....*....|....*....|....*...
gi 2462549072 826 LPQV-DVIIVMSGGKISEMGSYQELLAR 852
Cdd:TIGR02142 195 VLRLaDRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1303-1510 |
1.23e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLF--RINESAE-------GEIIIDGINIAKIGLHDLRFKITIIPQ--DP 1371
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTL-LKALagDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1372 VL-FSGSLRMNLDPF---------SQYSDEEVWTSLELAHlkdfvsalPDKLDhecAEGGENLSVGQRQLVCLARAL--- 1438
Cdd:PRK13547 95 AFaFSAREIVLLGRYpharragalTHRDGEIAWQALALAG--------ATALV---GRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1439 ------LRKTKILVLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHAdRIAMLADGAIVAHGAPADVL 243
|
.
gi 2462549072 1510 Q 1510
Cdd:PRK13547 244 T 244
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
762-861 |
1.31e-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: 60.74 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKnKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDLDEALRLgDRIAIMKDGRL 239
|
90 100
....*....|....*....|...
gi 2462549072 841 SEMGSYQELLAR--DGAFAEFLR 861
Cdd:cd03294 240 VQVGTPEEILTNpaNDYVREFFR 262
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1287-1510 |
1.32e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHdLRFKITI 1366
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQ----DPVLfsgSLRMNLDPFSQY-------SDEEVWTSLELAHLKDfvsalpdKLDHECAEggenLSVGQRQLVCLA 1435
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1436 RALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-EDCTVLTIAH------RLntimdYTRVIVLDKGEIQEYGAPSDL 1508
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
..
gi 2462549072 1509 LQ 1510
Cdd:PRK13537 226 IE 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1287-1511 |
1.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDFVLR---HINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG----LHD 1359
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1360 LRFKITIIPQDP--VLFSGSL-------RMNLDPFSQYSDEEVWTSLELAHL-KDFVSALPDKldhecaeggenLSVGQR 1429
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFE-----------LSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1430 QLVCLARALLRKTKILVLDEATAAVD----LETDDLIQSTIRTqfeDCTVLTIAHRLNTIMDYTR-VIVLDKGEIQEYGA 1504
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADYADyVYLLEKGHIISCGT 227
|
....*..
gi 2462549072 1505 PSDLLQQ 1511
Cdd:PRK13643 228 PSDVFQE 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1287-1458 |
2.26e-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: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRY---REDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKI---GLHD 1359
Cdd:COG4181 9 IELRGLTKTVgtgAGELT-ILKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPtSGTVRLAGQDLFALdedARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1360 LRF-KITIIPQDPVLFsGSLRMnLdpfsqysdEEVWTSLELAHLKD-FVSA--------LPDKLDHECAEggenLSVGQR 1429
Cdd:COG4181 87 LRArHVGFVFQSFQLL-PTLTA-L--------ENVMLPLELAGRRDaRARArallervgLGHRLDHYPAQ----LSGGEQ 152
|
170 180
....*....|....*....|....*....
gi 2462549072 1430 QLVCLARALLRKTKILVLDEATAAVDLET 1458
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
995-1248 |
2.35e-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: 60.19 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 995 DDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKEL 1074
Cdd:cd18543 27 DGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1075 DTVD---SMIPevikMFMGSLFNVIGACIVILLATP----IAAIIIPPLGLI-YFFVQRFYVASSRQLKRLESVSrspvy 1146
Cdd:cd18543 107 SLVQrflAFGP----FLLGNLLTLVVGLVVMLVLSPplalVALASLPPLVLVaRRFRRRYFPASRRAQDQAGDLA----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1147 SHFNETLLGVSVIRAF----EEQERFIHQSD-LKVDENQKAyypSIVANRWLAVR-LECVGNCIVLFAALFAVIsRHSLS 1220
Cdd:cd18543 178 TVVEESVTGIRVVKAFgrerRELDRFEAAARrLRATRLRAA---RLRARFWPLLEaLPELGLAAVLALGGWLVA-NGSLT 253
|
250 260
....*....|....*....|....*....
gi 2462549072 1221 AG-LVGLSvSYSlqvtTYLNWLVRMSSEM 1248
Cdd:cd18543 254 LGtLVAFS-AYL----TMLVWPVRMLGWL 277
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
762-861 |
2.72e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE--NVIGPKGMlknkTRILVTHSMSYLPQV-DVIIVMSGG 838
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEiiRELSQTGI----TQVIVTHEVEFARKVaSQVVYMEKG 217
|
90 100
....*....|....*....|....*
gi 2462549072 839 KISEMGSyQELLA--RDGAFAEFLR 861
Cdd:COG4161 218 RIIEQGD-ASHFTqpQTEAFAHYLS 241
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
714-844 |
2.74e-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: 58.10 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH-----------VAIK--------GVN----------LSG 764
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLIsflpkfsrnklIFIDqlqflidvGLGyltlgqklstLSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 765 GQKQRVSLARAVYSNAD--IYLFDDPLSAVDaHVGKHIFENVIGPKGMLKNkTRILVTHSMSYLPQVDVIIVM------S 836
Cdd:cd03238 91 GELQRVKLASELFSEPPgtLFILDEPSTGLH-QQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSSADWIIDFgpgsgkS 168
|
....*...
gi 2462549072 837 GGKISEMG 844
Cdd:cd03238 169 GGKVVFSG 176
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1310-1487 |
3.22e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1310 TINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA---KIGLHDLRFKITIIPQDPVlfsGSlrmnLDPFS 1386
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPY---GS----LNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1387 QYSD--EE---VWTSLELAHLKDFVSALPDK--LDHECAEGGENL-SVGQRQLVCLARALLRKTKILVLDEATAAVDLet 1458
Cdd:PRK11308 110 KVGQilEEpllINTSLSAAERREKALAMMAKvgLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDV-- 187
|
170 180
....*....|....*....|....*....
gi 2462549072 1459 ddliqsTIRTQFedctvltiahrLNTIMD 1487
Cdd:PRK11308 188 ------SVQAQV-----------LNLMMD 199
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
686-854 |
3.24e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 686 RPVKDGggtnSITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--------------------- 744
Cdd:PRK10790 334 RPLQSG----RIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLmgyypltegeirldgrplssl 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 745 ----------------------------------------------LAEM-----DKVEGHVAIKGVNLSGGQKQRVSLA 773
Cdd:PRK10790 409 shsvlrqgvamvqqdpvvladtflanvtlgrdiseeqvwqaletvqLAELarslpDGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 774 RAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARD 853
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQAL---AAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
.
gi 2462549072 854 G 854
Cdd:PRK10790 566 G 566
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
762-851 |
3.49e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 59.47 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeNVigpkgMLKNKTR-----ILVTHSMSYLPQV-DVIIVM 835
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQII-NL-----MLELQEKlgisyIYVSQHLGIVKHIsDKVLVM 223
|
90
....*....|....*.
gi 2462549072 836 SGGKISEMGSYQELLA 851
Cdd:COG4167 224 HQGEVVEYGKTAEVFA 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
697-840 |
3.63e-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: 59.12 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV------------------- 755
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLngLVEPTSGSVLIdgtdinklkgkalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 756 ---------------AIKGVN--------------------------------------------LSGGQKQRVSLARAV 776
Cdd:cd03256 80 igmifqqfnlierlsVLENVLsgrlgrrstwrslfglfpkeekqralaalervglldkayqradqLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 777 YSNADIYLFDDPLSAVD---AHVGKHIFENvigpKGMLKNKTRILVTHsmsylpQVDV-------IIVMSGGKI 840
Cdd:cd03256 160 MQQPKLILADEPVASLDpasSRQVMDLLKR----INREEGITVIVSLH------QVDLareyadrIVGLKDGRI 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
709-840 |
5.05e-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: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 709 SDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV---------------------------- 760
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagiayvpedrkreglv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 -------N------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahVG--KHIFENVIGPKGmlKNKTRILVThsmSY 825
Cdd:cd03215 91 ldlsvaeNialsslLSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VGakAEIYRLIRELAD--AGKAVLLIS---SE 163
|
170
....*....|....*....
gi 2462549072 826 LPQV----DVIIVMSGGKI 840
Cdd:cd03215 164 LDELlglcDRILVMYEGRI 182
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
694-852 |
5.29e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.97 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 694 TNSITVRNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSS-------LLSA----------LLAEMD------ 749
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrlidgLLEAesgqiiidgdLLTEENvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 750 ----------------KVEGHVAI----KGV---------------------------NLSGGQKQRVSLARAVYSNADI 782
Cdd:PRK13650 82 kigmvfqnpdnqfvgaTVEDDVAFglenKGIpheemkervnealelvgmqdfkerepaRLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 783 YLFDDPLSAVDahvgkhifenvigPKGMLK------------NKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELL 850
Cdd:PRK13650 162 IILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
..
gi 2462549072 851 AR 852
Cdd:PRK13650 229 SR 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
696-849 |
5.45e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.04 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS--------------------------------- 742
Cdd:PRK11000 3 SVTLRNVTKAYG--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRmiagleditsgdlfigekrmndvppaergvgmv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 743 ----AL---------------LAEMDKVE-----GHVAI----------KGVNLSGGQKQRVSLARAVYSNADIYLFDDP 788
Cdd:PRK11000 81 fqsyALyphlsvaenmsfglkLAGAKKEEinqrvNQVAEvlqlahlldrKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 789 LSAVDA--HVGKHIfenVIGPKGMLKNKTRILVTHSmsylpQV------DVIIVMSGGKISEMGSYQEL 849
Cdd:PRK11000 161 LSNLDAalRVQMRI---EISRLHKRLGRTMIYVTHD-----QVeamtlaDKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1509 |
5.76e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLT--LGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDP----VLFSG 1376
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 SLRMNLD---PFSQY--------------------SDEEvwtSLELAhlKDFVSALpdKLDHECAEGGE-NLSVGQRQLV 1432
Cdd:PRK13651 102 EIRRRVGvvfQFAEYqlfeqtiekdiifgpvsmgvSKEE---AKKRA--AKYIELV--GLDESYLQRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1433 CLARALLRKTKILVLDEATAAVDLE-TDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTkRTIFFKDGKIIKDGDTYDIL 253
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
697-776 |
7.05e-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: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTwaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSGGQKQRVSLARAV 776
Cdd:COG4559 2 LEAENLSVR--LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1301-1508 |
7.58e-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: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1301 DFV-LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKiGLHDLRFKITIIPQDPVLFSG-SL 1378
Cdd:cd03265 12 DFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1379 RMNLDPFSQ---YSDEEvWTSlELAHLKDFVsALPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1455
Cdd:cd03265 91 WENLYIHARlygVPGAE-RRE-RIDELLDFV-GLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1456 LETDDLIQSTIRTQFE--DCTVLTIAHRL---NTIMDytRVIVLDKGEIQEYGAPSDL 1508
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 ... |
1303-1494 |
8.34e-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: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1382
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 DPFSQY-SDEEVWTSLELAHLKDFVsalpdklDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1461
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGFE-------DRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 2462549072 1462 IQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVL 1494
Cdd:cd03231 164 FAEAMAGHCARggMVVLTTHQDLGLSEAGARELDL 198
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1304-1499 |
8.36e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGINIAKIG--LHDLR----------------F 1362
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSAGSHIELLGRTVQREGrlARDIRksrantgyifqqfnlvN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1363 KITIIPQDPVLFSGSL---RMNLDPFSQYSDEEVWTSLELAHLKDFVsalpdkldHECAEggeNLSVGQRQLVCLARALL 1439
Cdd:PRK09984 100 RLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFA--------HQRVS---TLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1440 RKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEI 1499
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
714-823 |
8.86e-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: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGVN--------------------------- 761
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEDiydpdvdvvelrrrvgmvfqkpnpfpk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 793
Cdd:COG1117 107 siydnvayglrlhgikskseldeiveeslrkaalwdevkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
170 180 190
....*....|....*....|....*....|.
gi 2462549072 794 AHVGKHIfENVIgpkGMLKNK-TRILVTHSM 823
Cdd:COG1117 187 PISTAKI-EELI---LELKKDyTIVIVTHNM 213
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1303-1482 |
1.01e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEG-----EIIIDGINIAKI-GLHDLRFKITIIPQDPVLFSG 1376
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 SLRMNLDP---FSQYSDEEVWTSLELAHLKDFvsALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1453
Cdd:PRK14271 116 SIMDNVLAgvrAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180
....*....|....*....|....*....
gi 2462549072 1454 VDLETDDLIQSTIRTQFEDCTVLTIAHRL 1482
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
749-823 |
1.16e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 1.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 749 DKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGpkgmLKNK-TRILVTHSM 823
Cdd:PRK14239 136 DEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG----LKDDyTMLLVTRSM 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1303-1455 |
1.33e-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: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INI--------AKIGL-------------HD 1359
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIrsprdairAGIAYvpedrkgeglvldLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1360 LRFKITIipqdPVLFSGSLRMNLDPfsqysdeevwtSLELAHLKDFVSAL---PDKLDHECAeggeNLSVGQRQLVCLAR 1436
Cdd:COG1129 347 IRENITL----ASLDRLSRGGLLDR-----------RRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAK 407
|
170
....*....|....*....
gi 2462549072 1437 ALLRKTKILVLDEATAAVD 1455
Cdd:COG1129 408 WLATDPKVLILDEPTRGID 426
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
996-1242 |
1.33e-08 |
|
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: 58.19 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 996 DPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGilASRclHV------DLLHSILRSPMSFFERTPSGNLVNR 1069
Cdd:cd18541 27 DALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFG--ASR--RIeydlrnDLFAHLLTLSPSFYQKNRTGDLMAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1070 FSKELDTVDSMIPEVIKMFMGSLFnVIGACIVILLAT--PIAAIIIPPLGLIYFFVQRFyvasSRQL-KRLESVSRSpvY 1146
Cdd:cd18541 103 ATNDLNAVRMALGPGILYLVDALF-LGVLVLVMMFTIspKLTLIALLPLPLLALLVYRL----GKKIhKRFRKVQEA--F 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1147 SHFN----ETLLGVSVIRAF----EEQERFIHQSDLKVDENQK------AYYPSIVanrwLAVRLecvGNCIVLFAALFA 1212
Cdd:cd18541 176 SDLSdrvqESFSGIRVIKAFvqeeAEIERFDKLNEEYVEKNLRlarvdaLFFPLIG----LLIGL---SFLIVLWYGGRL 248
|
250 260 270
....*....|....*....|....*....|.
gi 2462549072 1213 VIsRHSLSAG-LVglsvsyslQVTTYLNWLV 1242
Cdd:cd18541 249 VI-RGTITLGdLV--------AFNSYLGMLI 270
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1303-1498 |
1.51e-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: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtlglfrinesaegeiiidginiakiglhdlrfkITIIPQDPVLFSGSLRmnl 1382
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKLIAGELEPDEGIVT--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1383 dpfsqysdeevWTS-LELAHLkdfvsalpdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1461
Cdd:cd03221 59 -----------WGStVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462549072 1462 IQSTIRTQfeDCTVLTIAH-R--LNTIMdyTRVIVLDKGE 1498
Cdd:cd03221 109 LEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1307-1511 |
1.93e-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: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1307 INVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII----DGINIAKIGLhDLRFKIT-----------IIPQDP 1371
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigilhqeydLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1372 VLFSGSLRMNLD-PFSQYSDEEVWTSLELAHLKDFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1450
Cdd:TIGR03269 382 VLDNLTEAIGLElPDELARMKAVITLKMVGFDEEKAEEILDKYPDE-------LSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1451 TAAVDLETDDLIQSTI---RTQFEDcTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:TIGR03269 455 TGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVCdRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1305-1499 |
2.05e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1305 RHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQD---PVLF-SGSLR 1379
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqsSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1380 MNLDPFSqYSDEEVW--TSLELAHLKDFVSALPDKLDHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1457
Cdd:PRK15439 360 WNVCALT-HNRRGFWikPARENAVLERYRRALNIKFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549072 1458 TDDLIQSTIRTQFEDCT-VLTIAHRLNTIMDYT-RVIVLDKGEI 1499
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEI 481
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1303-1499 |
2.21e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL----RFKITIIPQDPVLFSG-S 1377
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1378 LRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1457
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ----LSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549072 1458 TDDLIQSTIRtQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEI 1499
Cdd:PRK10535 179 SGEEVMAILH-QLRDrgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
762-849 |
2.67e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGmlKNKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMEHVLEVaDEVIVMDKGKI 254
|
....*....
gi 2462549072 841 SEMGSYQEL 849
Cdd:PRK13631 255 LKTGTPYEI 263
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
695-849 |
3.30e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.63 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 695 NSITVRNATFTWARSD----PPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLA---------EMDK-------- 750
Cdd:PRK13633 3 EMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIpsegkvyvdGLDTsdeenlwd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 751 --------------------VEGHVA--------------------IKGVN-----------LSGGQKQRVSLARAVYSN 779
Cdd:PRK13633 83 irnkagmvfqnpdnqivatiVEEDVAfgpenlgippeeirervdesLKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 780 ADIYLFDDPLSAVDAhVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQEL 849
Cdd:PRK13633 163 PECIIFDEPTAMLDP-SGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1290-1462 |
3.43e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1290 RNYCLRYRED--LDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLR-FK 1363
Cdd:PRK11629 9 DNLCKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1364 ITIIPQ------D---------PVLFSGSLRMNldpfSQYSDEEVWTSLELAHlkdfvsalpdKLDHECAEggenLSVGQ 1428
Cdd:PRK11629 89 LGFIYQfhhllpDftalenvamPLLIGKKKPAE----INSRALEMLAAVGLEH----------RANHRPSE----LSGGE 150
|
170 180 190
....*....|....*....|....*....|....
gi 2462549072 1429 RQLVCLARALLRKTKILVLDEATAAVDLETDDLI 1462
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
762-861 |
4.07e-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: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH-VGKhifenVIGPKGMLKN--KTRILVTHSMSYLPQV-DVIIVMSG 837
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPElVGE-----VLKVMRDLAEegRTMLVVTHEMGFARDVsSHVVFLHQ 229
|
90 100
....*....|....*....|....*.
gi 2462549072 838 GKISEMGSYQELLA--RDGAFAEFLR 861
Cdd:COG4598 230 GRIEEQGPPAEVFGnpKSERLRQFLS 255
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1287-1511 |
4.91e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.29 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1287 VEFRNYCLRYREDLDF---VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG----LHD 1359
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1360 LRFKITIIPQDP--VLFSGSLRMNL----DPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHEcaeggenLSVGQRQLVC 1433
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFE-------LSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1434 LARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
724-821 |
5.16e-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: 53.53 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 724 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---------------------AIKGVNLSGGQKQRVSLARAVYSNADI 782
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllliivGGKKASGSGELRLRLALALARKLKPDV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462549072 783 YLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTR----ILVTH 821
Cdd:smart00382 82 LILDEITSLLDAEQEALLLLLEELRLLLLLKSEKnltvILTTN 124
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1303-1508 |
5.85e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGINIAKigLHDLRFKITIIPQDPVLF---- 1374
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiaglEHQTSGHIRFHGTDVSR--LHARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1375 -----SGSLRM---NLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILV 1446
Cdd:PRK10851 91 vfdniAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1447 LDEATAAVDLETDDLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1508
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1304-1497 |
6.15e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGlHDLRFK--ITIIPQD-PVLFSGSLRM 1380
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NLdPFSQYSDEEVW--TSLELAHLKDFVSALPDKLD--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV-D 1455
Cdd:PRK09700 100 NL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRVGlkVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462549072 1456 LETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKG 1497
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1303-1455 |
6.80e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.13 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID----GINIAKIG---LHDLRfKITI--------- 1366
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALR-RRTIgyvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1367 IPQDP---VLFSGSLRMNLDPFSQYSDEEVWtsleLAHLKdfvsaLPDKLDHecaeggenL-----SVGQRQLVCLARAL 1438
Cdd:COG4778 105 IPRVSaldVVAEPLLERGVDREEARARAREL----LARLN-----LPERLWD--------LppatfSGGEQQRVNIARGF 167
|
170
....*....|....*..
gi 2462549072 1439 LRKTKILVLDEATAAVD 1455
Cdd:COG4778 168 IADPPLLLLDEPTASLD 184
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
708-840 |
8.49e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 708 RSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVAIKGVN----------------------- 761
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPykefaekypgeiiyvseedvhfp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ----------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKNKTRILV 819
Cdd:cd03233 97 tltvretldfalrckgnefvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK-------CIRTMADVLK 169
|
170 180
....*....|....*....|....*....
gi 2462549072 820 THSMSYLPQ--------VDVIIVMSGGKI 840
Cdd:cd03233 170 TTTFVSLYQasdeiydlFDKVLVLYEGRQ 198
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
762-860 |
8.65e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD----AHVGKHIFEnvIGPKGMlknkTRILVTHsmsylpQVDV------ 831
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIRE--LAETGI----TQVIVTH------EVEVarktas 209
|
90 100 110
....*....|....*....|....*....|.
gi 2462549072 832 -IIVMSGGKISEMGSYQELLA-RDGAFAEFL 860
Cdd:PRK11124 210 rVVYMENGHIVEQGDASCFTQpQTEAFKNYL 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
714-844 |
8.86e-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: 54.46 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLL--------------------SALLA--------------------------- 746
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLrllagiyppdsgtvtvrgrvSSLLGlgggfnpeltgreniylngrllglsrk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 747 EMDKVEGHVA------------IKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIFEnvigpkgM 810
Cdd:cd03220 118 EIDEKIDEIIefselgdfidlpVK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRE-------L 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462549072 811 LKN-KTRILVTHSMSYLPQV-DVIIVMSGGKISEMG 844
Cdd:cd03220 189 LKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1298-1481 |
9.19e-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: 56.68 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1298 EDLDFVLRHinvtingGEKVGIVGRTGAGKSSLtlglFRInesaEGEII-IDGINIAKiglhDLRFKITIIPQDPVLFSG 1376
Cdd:TIGR00954 469 ESLSFEVPS-------GNNLLICGPNGCGKSSL----FRI----LGELWpVYGGRLTK----PAKGKLFYVPQRPYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1377 SLR------MNLDPFSQ--YSDEEVWTSLELAHLKDFV------SALPDKLDHecaeggenLSVGQRQLVCLARALLRKT 1442
Cdd:TIGR00954 530 TLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQLTHILereggwSAVQDWMDV--------LSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549072 1443 KILVLDEATAAVDLETDDLIqstirtqFEDC-----TVLTIAHR 1481
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYM-------YRLCrefgiTLFSVSHR 638
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
697-774 |
9.61e-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: 9.61e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 697 ITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSGGQKQRVSLAR 774
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1023-1257 |
1.01e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 55.21 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1023 AVFGYSMAVsIGGILASRcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVI 1102
Cdd:cd18563 61 ILRGRLLAR-LGERITAD-LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1103 L-----LAtpiAAIIIP-PL--GLIYFFVQRFYVASSRQLKRlesvsRSPVYSHFNETLLGVSVIRAF----EEQERFIH 1170
Cdd:cd18563 139 FslnwkLA---LLVLIPvPLvvWGSYFFWKKIRRLFHRQWRR-----WSRLNSVLNDTLPGIRVVKAFgqekREIKRFDE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1171 QSDLKVDENQKA------YYPSIVAnrwlavrLECVGNCIVLFAALFAVISRHsLSAGLVGLSVSYSLQVTTYLNWLVRM 1244
Cdd:cd18563 211 ANQELLDANIRAeklwatFFPLLTF-------LTSLGTLIVWYFGGRQVLSGT-MTLGTLVAFLSYLGMFYGPLQWLSRL 282
|
250
....*....|...
gi 2462549072 1245 SSEMETNIVAVER 1257
Cdd:cd18563 283 NNWITRALTSAER 295
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
717-860 |
1.05e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 54.38 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 717 ITFSIPEGALVAVVGQVGCGKSSLLSAL---------------------------------------------------- 744
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIagflppdsgrilwngqdltalppaerpvsmlfqennlfphltvaqniglglr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 745 ----LAEMDKVEGHVAIKGVN-----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAvdahvgkhifenvIGP-- 807
Cdd:COG3840 98 pglkLTAEQRAQVEQALERVGlaglldrlpgqLSGGQRQRVALARCLVRKRPILLLDEPFSA-------------LDPal 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 808 -KGMLK---------NKTRILVTHSmsylPQ-----VDVIIVMSGGKISEMGSYQELLARDG--AFAEFL 860
Cdd:COG3840 165 rQEMLDlvdelcrerGLTVLMVTHD----PEdaariADRVLLVADGRIAADGPTAALLDGEPppALAAYL 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
739-874 |
1.16e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 739 SLLSALLaeMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRIL 818
Cdd:PRK14243 131 SLRQAAL--WDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELM---HELKEQYTIII 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 819 VTHSMSYLPQVDVIIVMSGGKISEMGSyqellaRDGAFAEFLRTYA--STEQEQDAEE 874
Cdd:PRK14243 206 VTHNMQQAARVSDMTAFFNVELTEGGG------RYGYLVEFDRTEKifNSPQQQATRD 257
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1015-1258 |
1.31e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 55.21 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1015 ALGISQGIAVFG--YSMAvSIGGILASRcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSL 1092
Cdd:cd18564 62 GIALLRGLASYAgtYLTA-LVGQRVVLD-LRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1093 FNVIGACIVIL-----LATpIAAIIIPplgLIYFFVQRFY---VASSRQLKRLESVsrspVYSHFNETLLGVSVIRAF-- 1162
Cdd:cd18564 140 LTLVGMLGVMFwldwqLAL-IALAVAP---LLLLAARRFSrriKEASREQRRREGA----LASVAQESLSAIRVVQAFgr 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1163 --EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSAGlvGLSVsyslqVTTYLNW 1240
Cdd:cd18564 212 eeHEERRFARENRKSLRAGLRAARLQALLSPVVDV-LVAVGTALVLWFGAWLVL-AGRLTPG--DLLV-----FLAYLKN 282
|
250 260
....*....|....*....|....*
gi 2462549072 1241 L---VRMSSEMETNI----VAVERL 1258
Cdd:cd18564 283 LykpVRDLAKLTGRIakasASAERV 307
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
697-842 |
1.34e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.90 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 761
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlkrreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ---------------------------------------------------------LSGGQKQRVSLARAVYSNADIYL 784
Cdd:COG2884 81 igvvfqdfrllpdrtvyenvalplrvtgksrkeirrrvrevldlvglsdkakalpheLSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 785 FDDPLSAVDAHVGKHIFEnvigpkgMLK--NK---TRILVTHSMSYLPQVDV-IIVMSGGKISE 842
Cdd:COG2884 161 ADEPTGNLDPETSWEIME-------LLEeiNRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
714-845 |
1.37e-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: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD-KV-EGHVAIKGVNL----------------------------- 762
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyEVtEGEILFKGEDItdlppeerarlgiflafqyppeipgvkna 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 763 ----------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfENVIgpKGML-KNKTRILVTHSMSYLPQV-- 829
Cdd:cd03217 96 dflryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV-AEVI--NKLReEGKSVLIITHYQRLLDYIkp 172
|
170
....*....|....*.
gi 2462549072 830 DVIIVMSGGKISEMGS 845
Cdd:cd03217 173 DRVHVLYDGRIVKSGD 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
714-852 |
1.38e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLL--------------------SALL---------------------------A 746
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLkliagileptsgrvevngrvSALLelgagfhpeltgreniylngrllglsrK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 747 EMDKVEGHVA------------IKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIFEnvigpkgM 810
Cdd:COG1134 122 EIDEKFDEIVefaelgdfidqpVK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE-------L 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 811 LKN-KTRILVTHSMSYLPQV-DVIIVMSGGKISEMGS-------YQELLAR 852
Cdd:COG1134 193 RESgRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDpeeviaaYEALLAG 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
762-840 |
1.65e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhifENVIGPKGMLKNK--TRILVTHSMSYLPQVDVIIVMSGGK 839
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG----EEVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGE 220
|
.
gi 2462549072 840 I 840
Cdd:PRK10535 221 I 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1299-1455 |
1.78e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1299 DLDFVLRHinvtingGEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDG--INIaKIGLHDLRFKITIIPQD----- 1370
Cdd:PRK13549 280 DVSFSLRR-------GEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGkpVKI-RNPQQAIAQGIAMVPEDrkrdg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 --PVLFSG--SLRMNLDPFSQYS--DEevwtSLELAHLKDFVSALPDKLDHECAEGGeNLSVGQRQLVCLARALLRKTKI 1444
Cdd:PRK13549 352 ivPVMGVGknITLAALDRFTGGSriDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKI 426
|
170
....*....|.
gi 2462549072 1445 LVLDEATAAVD 1455
Cdd:PRK13549 427 LILDEPTRGID 437
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
762-851 |
1.84e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.22 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKIS 841
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERI--KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
90
....*....|
gi 2462549072 842 EMGSYQELLA 851
Cdd:PRK13644 215 LEGEPENVLS 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
696-776 |
2.56e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.62 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSGGQKQRVSLARA 775
Cdd:PRK13548 2 MLEARNLSV--RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
.
gi 2462549072 776 V 776
Cdd:PRK13548 80 V 80
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
714-852 |
2.81e-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: 55.08 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVAIKGVNL------------------------------- 762
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLdglsrralrplrrrmqvvfqdpfgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 763 ----------------------------------------------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 796
Cdd:COG4172 381 vgqiiaeglrvhgpglsaaerrarvaealeevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 797 GKHIFEnvigpkgMLKnktRILVTHSMSYL-----PQV-----DVIIVMSGGKISEMGSYQELLAR 852
Cdd:COG4172 461 QAQILD-------LLR---DLQREHGLAYLfishdLAVvralaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
717-852 |
2.93e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.87 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 717 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIK-------------------------------------- 758
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkknkklkplrkkvgivfqfpehqlfeetvek 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 759 ---------GV----------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI- 800
Cdd:PRK13634 106 dicfgpmnfGVseedakqkaremielvglpeellarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMm 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 801 --FENVIGPKGMlknkTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSYQELLAR 852
Cdd:PRK13634 186 emFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1303-1449 |
2.94e-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: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI-----AKIglhdLRFKITIIPQDPVLFSgs 1377
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtAKI----MREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 1378 lRM----NLDPFSQYSDEEVWTSlelaHLKDFVSALPDKLDHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDE 1449
Cdd:PRK11614 94 -RMtveeNLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
694-870 |
2.98e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.73 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 694 TNSITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV------------- 760
Cdd:PRK15056 4 QAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvay 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 -----------------------------------------------------------NLSGGQKQRVSLARAVYSNAD 781
Cdd:PRK15056 83 vpqseevdwsfpvlvedvvmmgryghmgwlrrakkrdrqivtaalarvdmvefrhrqigELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 782 IYLFDDPLSAVDAHVGKHIfenvIGPKGMLKN--KTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDG---AF 856
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARI----ISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENlelAF 238
|
250
....*....|....
gi 2462549072 857 AEFLRTYASTEQEQ 870
Cdd:PRK15056 239 SGVLRHVALNGSEE 252
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1310-1503 |
3.17e-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: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1310 TINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAkiglhdlrFKI-TIIPQDPVLFSGSLRMNLDPF--S 1386
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPqYIKADYEGTVRDLLSSITKDFytH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1387 QYSDEEVWTSLELAHLKDfvSALPDkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTI 1466
Cdd:cd03237 93 PYFKTEIAKPLQIEQILD--REVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549072 1467 RTQFE--DCTVLTIAHrlNTIM-DYT--RVIVLDkGEIQEYG 1503
Cdd:cd03237 159 RRFAEnnEKTAFVVEH--DIIMiDYLadRLIVFE-GEPSVNG 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
697-858 |
3.29e-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: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVAIKGVN--------------- 761
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrkafgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 ---------------------------------------------------------LSGGQKQRVSLARAVYSNADIYL 784
Cdd:cd03289 82 ipqkvfifsgtfrknldpygkwsdeeiwkvaeevglksvieqfpgqldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 785 FDDPLSAVDAhVGKHIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 858
Cdd:cd03289 162 LDEPSAHLDP-ITYQVIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
714-850 |
4.00e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGV---------------------------- 760
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRniyspdvdpievrrevgmvfqypnpfph 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 -------------------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSA 791
Cdd:PRK14267 100 ltiydnvaigvklnglvkskkeldervewalkkaalwdevkdrlndypsNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 792 VDAHVGKHIFENVIGPKgmlKNKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELL 850
Cdd:PRK14267 180 IDPVGTAKIEELLFELK---KEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVF 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1290-1504 |
4.19e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1290 RNYCLRYREDLDFV--LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-------------IIDGINIAK 1354
Cdd:PRK10261 16 ENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1355 IGLHDLR-------FKITIIPQDPVLFSG-----SLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALpDKLDHEcaegge 1422
Cdd:PRK10261 96 AQMRHVRgadmamiFQEPMTSLNPVFTVGeqiaeSIRLHQGASREEAMVEAKRMLDQVRIPEAQTIL-SRYPHQ------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1423 nLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCT--VLTIAHRLNTIMDYT-RVIVLDKGEI 1499
Cdd:PRK10261 169 -LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIAdRVLVMYQGEA 247
|
....*
gi 2462549072 1500 QEYGA 1504
Cdd:PRK10261 248 VETGS 252
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1042-1188 |
4.20e-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: 53.31 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1042 LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPI-AAIIIPPLGLIY 1120
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKlALLTLIPIPFLA 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1121 FFVqRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKA------YYPSIV 1188
Cdd:cd18778 155 LGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFgreeEEAKRFEALSRRYRKAQLRAmklwaiFHPLME 231
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1012-1222 |
4.59e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 53.26 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1012 VYGALGISQGIAVFGYSMAVsigGILASRCLH---VDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMF 1088
Cdd:cd18546 44 AYLAVVLAGWVAQRAQTRLT---GRTGERLLYdlrLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1089 MGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQRfyvASSRQLKRL-ESVSRspVYSHFNETLLGVSVIRAF- 1162
Cdd:cd18546 121 VVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRWFRR---RSSRAYRRArERIAA--VNADLQETLAGIRVVQAFr 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1163 ---EEQERFIHQSDLKVDENQKA------YYPSIvanRWLAVrlecVGNCIVLFAALFAVIsRHSLSAG 1222
Cdd:cd18546 196 rerRNAERFAELSDDYRDARLRAqrlvaiYFPGV---ELLGN----LATAAVLLVGAWRVA-AGTLTVG 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
736-873 |
4.93e-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: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 736 GKSSLLSAL-LAEMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIgpKGMLKNK 814
Cdd:TIGR03269 142 GKEAVGRAVdLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASG 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 815 TRILVThsmSYLPQV-----DVIIVMSGGKISEMGSYQELLARdgafaeFLRTYASTEQEQDAE 873
Cdd:TIGR03269 220 ISMVLT---SHWPEViedlsDKAIWLENGEIKEEGTPDEVVAV------FMEGVSEVEKECEVE 274
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1304-1511 |
5.71e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.17 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSS----LTlGLfrINESAeGEIIIDGINIAKiGLHDLRFKITIIpqdpvlfsgslr 1379
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLT-GI--LVPTS-GEVRVLGYVPFK-RRKEFARRIGVV------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1380 mnldpFSQYS----DEEVWTSLELahLKDfVSALPDK-----LDhECAEG---GE-------NLSVGQRQLVCLARALLR 1440
Cdd:COG4586 101 -----FGQRSqlwwDLPAIDSFRL--LKA-IYRIPDAeykkrLD-ELVELldlGElldtpvrQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1441 KTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQQ 1511
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1045-1222 |
6.05e-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: 52.82 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1045 DLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACI-----------VILLATPIAAIII 1113
Cdd:cd18551 74 RLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVlmflldwvltlVTLAVVPLAFLII 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1114 PPLGliyffvQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF--EEQErfihqSDLKVDENQKAYYPSIVANR 1191
Cdd:cd18551 154 LPLG------RRIRKASKRAQDALGELS-----AALERALSAIRTVKASnaEERE-----TKRGGEAAERLYRAGLKAAK 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462549072 1192 WLAVrLECVGNcIVLFAALFAVI-------SRHSLSAG 1222
Cdd:cd18551 218 IEAL-IGPLMG-LAVQLALLVVLgvggarvASGALTVG 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
697-876 |
7.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.79 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWAR-SDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG---------------- 759
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrrkig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 -------------------------------------------VN-----------LSGGQKQRVSLARAVYSNADIYLF 785
Cdd:PRK13642 85 mvfqnpdnqfvgatveddvafgmenqgipreemikrvdeallaVNmldfktreparLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 786 DDPLSAVDAhVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEF-LRTYA 864
Cdd:PRK13642 165 DESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIgLDVPF 243
|
250
....*....|..
gi 2462549072 865 STEQEQDAEENG 876
Cdd:PRK13642 244 SSNLMKDLRKNG 255
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
759-862 |
7.46e-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: 52.22 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 759 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkhifENVIGPKGMLKNKTRILVT--HSMSYLPQVDVIIVMS 836
Cdd:cd03288 154 GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-----ENILQKVVMTAFADRTVVTiaHRVSTILDADLVLVLS 228
|
90 100
....*....|....*....|....*..
gi 2462549072 837 GGKISEMGSYQELLAR-DGAFAEFLRT 862
Cdd:cd03288 229 RGILVECDTPENLLAQeDGVFASLVRT 255
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
712-794 |
8.16e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 712 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLA------------EMDKVEGHVAIKGV------------------- 760
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLN-LIAgfvpyqhgsitlDGKPVEGPGAERGVvfqnegllpwrnvqdnvaf 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 761 ----------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 794
Cdd:PRK11248 94 glqlagvekmqrleiahqmlkkvglegaekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1304-1485 |
8.92e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglHDLRFK---------ITIIPQD---- 1370
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG--------QEMRFAsttaalaagVAIIYQElhlv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1371 P---V---LFSGSLrmnldP----FSQYSDEEVWTSLELAHLKDFVSalPD-KLDHecaeggenLSVGQRQLVCLARALL 1439
Cdd:PRK11288 92 PemtVaenLYLGQL-----PhkggIVNRRLLNYEAREQLEHLGVDID--PDtPLKY--------LSIGQRQMVEIAKALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462549072 1440 RKTKILVLDEATAAVDL-ETDDLIQSTIRTQFEDCTVLTIAHRLNTI 1485
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEI 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
762-852 |
1.22e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIaDEVIVMHEGKV 229
|
90
....*....|....*...
gi 2462549072 841 SEMG------SYQELLAR 852
Cdd:PRK13645 230 ISIGspfeifSNQELLTK 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
706-793 |
1.24e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 706 WARSDPPTL---NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSG-GQKQRvslaRAVYSnaD 781
Cdd:PRK15079 26 WFWQPPKTLkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEW----RAVRS--D 99
|
90
....*....|...
gi 2462549072 782 IYL-FDDPLSAVD 793
Cdd:PRK15079 100 IQMiFQDPLASLN 112
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
745-849 |
1.48e-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: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 745 LAEMDKV--EGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD---AHVGKHIFENVIGPKGmlknKTRILV 819
Cdd:TIGR02315 127 LSALERVglADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDpktSKQVMDYLKRINKEDG----ITVIIN 202
|
90 100 110
....*....|....*....|....*....|.
gi 2462549072 820 THSMSYLPQ-VDVIIVMSGGKISEMGSYQEL 849
Cdd:TIGR02315 203 LHQVDLAKKyADRIVGLKAGEIVFDGAPSEL 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1301-1508 |
1.53e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1301 DFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDgINIAkiglhdlrFK---ITIIPQDPVlfSGS 1377
Cdd:PRK13409 352 DFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS--------YKpqyIKPDYDGTV--EDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1378 LRMNLDPF-SQYSDEEVWTSLELAHLkdfvsalpdkLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1456
Cdd:PRK13409 421 LRSITDDLgSSYYKSEIIKPLQLERL----------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1457 ETDDLIQSTIRTQFE--DCTVLTIAHRLnTIMDY--TRVIVLDkGEIQEYG---APSDL 1508
Cdd:PRK13409 487 EQRLAVAKAIRRIAEerEATALVVDHDI-YMIDYisDRLMVFE-GEPGKHGhasGPMDM 543
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
745-850 |
1.81e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 51.76 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 745 LAEMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGML-KNKTRILVTHSM 823
Cdd:PRK13536 156 LLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL---RSLLaRGKTILLTTHFM 232
|
90 100
....*....|....*....|....*....
gi 2462549072 824 SYLPQV-DVIIVMSGG-KISEmGSYQELL 850
Cdd:PRK13536 233 EEAERLcDRLCVLEAGrKIAE-GRPHALI 260
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
762-863 |
2.01e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.96 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK-HQRTIVFISHDLDEAMRIgDRIAIMQNGEV 243
|
90 100
....*....|....*....|...
gi 2462549072 841 SEMGSYQELLarDGAFAEFLRTY 863
Cdd:PRK10070 244 VQVGTPDEIL--NNPANDYVRTF 264
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
761-856 |
2.01e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvIGPKGMLKNKTRILVTHSM-SYLPQVDVIIVMSGGK 839
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
90
....*....|....*..
gi 2462549072 840 ISEMGSYQELLaRDGAF 856
Cdd:PRK13651 243 IIKDGDTYDIL-SDNKF 258
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
714-849 |
2.48e-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: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLS--------------------------------------------------- 742
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNlisglaqptsggvilegkqitepgpdrmvvfqnysllpwltvrenialavd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 743 ALLAEMDK------VEGHVAIKGV---------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkhifenvigp 807
Cdd:TIGR01184 81 RVLPDLSKserraiVEEHIALVGLteaadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT----------- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 808 KGMLKNK----------TRILVTHSM-SYLPQVDVIIVMSGGKISEMGSYQEL 849
Cdd:TIGR01184 150 RGNLQEElmqiweehrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
761-868 |
2.91e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE--NVIGPKGMlknkTRILVTHSMsylPQV----DVIIV 834
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQliNQFKAEGL----SIILVSSEM---PEVlgmsDRILV 467
|
90 100 110
....*....|....*....|....*....|....
gi 2462549072 835 MSGGKISemgsyqellardgafAEFLRTYASTEQ 868
Cdd:PRK10762 468 MHEGRIS---------------GEFTREQATQEK 486
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1291-1515 |
3.35e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1291 NYCLRYREDLDFVLRHIN---VTINGGEKVGIVGRTGAGKSS---LTLGLFrINESAE---GEIIIDGiNIAKIG-LHDL 1360
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTmiqLTNGLI-ISETGQtivGDYAIPA-NLKKIKeVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1361 RFKITIIPQDP--VLFSGSLRMNL--DPFSQYSD-EEVWTslELAHLKDFVSALPDKLDHECAEggenLSVGQRQLVCLA 1435
Cdd:PRK13645 89 RKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENkQEAYK--KVPELLKLVQLPEDYVKRSPFE----LSGGQKRRVALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1436 RALLRKTKILVLDEATAAVDLE-TDDLIQSTIRTQFEDCT-VLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQR 1512
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKgEEDFINLFERLNKEYKKrIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEIFSNQ 242
|
...
gi 2462549072 1513 GLF 1515
Cdd:PRK13645 243 ELL 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1424-1505 |
3.35e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.00 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1424 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-DLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQE 1501
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILK 256
|
....
gi 2462549072 1502 YGAP 1505
Cdd:PRK13631 257 TGTP 260
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1010-1222 |
4.08e-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: 50.24 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1010 LSVYGAlgisQGIAVFGY-SMAVSIGGILASRcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMF 1088
Cdd:cd18574 49 LGLYLL----QSLLTFAYiSLLSVVGERVAAR-LRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1089 MGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRspvySHFNETLLGVSVIRAF-- 1162
Cdd:cd18574 124 LRSVTQTVGCVVSLYLISPkltlLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKAT----GVADEALGNIRTVRAFam 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1163 --EEQERFIhqsdlkvDENQKAyypsIVANRWLAVRLEC-------VGNCIVLfAALFA---VISRHSLSAG 1222
Cdd:cd18574 200 edRELELYE-------EEVEKA----AKLNEKLGLGIGIfqglsnlALNGIVL-GVLYYggsLVSRGELTAG 259
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
714-852 |
4.25e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNL------------------------------- 762
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqkllrqkiqivfqnpygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 763 ---------------------------------------------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 797
Cdd:PRK11308 111 vgqileepllintslsaaerrekalammakvglrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 798 KHIFeNVIgpkgM-LK---NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 852
Cdd:PRK11308 191 AQVL-NLM----MdLQqelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
749-889 |
4.76e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.09 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 749 DKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQ 828
Cdd:PRK14271 151 DAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI---RSLADRLTVIIVTHNLAQAAR 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 829 V-DVIIVMSGGKISEMGSYQELlardgafaeflrtYASTEQEQDAEEngVTGVSGPGKEAKQ 889
Cdd:PRK14271 228 IsDRAALFFDGRLVEEGPTEQL-------------FSSPKHAETARY--VAGLSGDVKDAKR 274
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
714-844 |
5.60e-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: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGaLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG---------------------------------- 759
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrrigylpqefgvypnftvrefld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 -----------------------VNL-----------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVI 805
Cdd:cd03264 95 yiawlkgipskevkarvdevlelVNLgdrakkkigslSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EERIRFRNLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462549072 806 GPKGmlKNKTRILVTHSMSylpqvDV------IIVMSGGKISEMG 844
Cdd:cd03264 174 SELG--EDRIVILSTHIVE-----DVeslcnqVAVLNKGKLVFEG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
749-852 |
5.82e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 749 DKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKgmlKNKTRILVTHsmsYLPQ 828
Cdd:PRK14247 134 DEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK---KDMTIVLVTH---FPQQ 207
|
90 100
....*....|....*....|....*...
gi 2462549072 829 V----DVIIVMSGGKISEMGSYQELLAR 852
Cdd:PRK14247 208 AarisDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
710-869 |
6.64e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.24 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 710 DPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--------------------------------------------- 744
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqsgtvflgdkpismlssrqlarrlallpqhhltpegitv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 745 -----------------LAEMDK--VE--------GHVAIKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHv 796
Cdd:PRK11231 94 relvaygrspwlslwgrLSAEDNarVNqameqtriNHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 797 gkHIFEnVIGPKGMLKN--KTRILVTHSmsyLPQV----DVIIVMSGGKISEMGSYQELLArdgafAEFLRTYASTEQE 869
Cdd:PRK11231 173 --HQVE-LMRLMRELNTqgKTVVTVLHD---LNQAsrycDHLVVLANGHVMAQGTPEEVMT-----PGLLRTVFDVEAE 240
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1021-1244 |
7.25e-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: 49.70 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1021 GIAVFGYSMAVsIGGILASRC-------LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLF 1093
Cdd:cd18548 47 LLALLGLIAGI-LAGYFAAKAsqgfgrdLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1094 NVIGACIVILLATP----IAAIIIPPLGLIYFFVQRF-YVASSRQLKRLESVSRSpvyshFNETLLGVSVIRAF----EE 1164
Cdd:cd18548 126 MLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKaIPLFKKVQKKLDRLNRV-----VRENLTGIRVIRAFnredYE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1165 QERFIhqsdlkvDENQKAYYPSIVANRWLAVR---LECVGN----CIVLFAALFavISRHSLSAG-LVGLsVSYSLQVTT 1236
Cdd:cd18548 201 EERFD-------KANDDLTDTSLKAGRLMALLnplMMLIMNlaivAILWFGGHL--INAGSLQVGdLVAF-INYLMQILM 270
|
....*...
gi 2462549072 1237 YLNWLVRM 1244
Cdd:cd18548 271 SLMMLSMV 278
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1021-1166 |
7.34e-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: 49.43 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1021 GIAVFG--YSMAVSIGGILASrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGA 1098
Cdd:cd18573 55 AAANFGrvYLLRIAGERIVAR--LRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGG 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1099 CIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQLkrLESVSRSpvySHF-NETLLGVSVIRAF--EEQE 1166
Cdd:cd18573 133 IGMMLYISPkltlVMLLVVPPIAVGAVFYGRYVRKLSKQV--QDALADA---TKVaEERLSNIRTVRAFaaERKE 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1304-1499 |
9.93e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1304 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD---LRFKITIIPQDPVLFsgslrM 1380
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLL-----M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1381 NLDPFSQYSDEEVWTSLELAHLKDFVSALPDK--LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDlet 1458
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKvgLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD--- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462549072 1459 DDLIQSTIRTqFED-----CTVLTIAHRLNTIMDYT-RVIVLDKGEI 1499
Cdd:PRK10908 170 DALSEGILRL-FEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
753-805 |
1.00e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.33 E-value: 1.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 753 GHVA-IKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENVI 805
Cdd:PRK13539 118 APLAhLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELI 170
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
697-822 |
1.01e-05 |
|
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: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKV-EGHVAIKGVN-------------- 761
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWgSGRIGMPEGEdllflpqrpylplg 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 762 -------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKNK--TRILVTHS 822
Cdd:cd03223 79 tlreqliypwddvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ-------LLKELgiTVISVGHR 147
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
695-853 |
1.09e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.96 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 695 NSITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLL------------------SALLAEMDK-VEGHV 755
Cdd:PRK13647 3 NIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgrvkvmgREVNAENEKwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 756 ----------------------------------------AIKGVN-----------LSGGQKQRVSLARAVYSNADIYL 784
Cdd:PRK13647 82 glvfqdpddqvfsstvwddvafgpvnmgldkdeverrveeALKAVRmwdfrdkppyhLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 785 FDDPLSAVDAHVGKHIFE--NVIGPKGmlknKTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSyQELLARD 853
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEilDRLHNQG----KTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDE 228
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1015-1182 |
1.16e-05 |
|
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: 48.99 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1015 ALGISQGIAVF--GYSMAVSiGGILASRcLHVDLLHSILRSPMSFFERTP--SGNLVNRFSKELDTVDSMIPEVIKMFMG 1090
Cdd:cd18578 60 VLAIVAGIAYFlqGYLFGIA-GERLTRR-LRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1091 SLFNVIGACIVILLA----TPIAAIIIPPLGLIYFFVQRFYVASSRQLKR-LESVSRspvysHFNETLLGVSVIRAFEEQ 1165
Cdd:cd18578 138 AIVTLVAGLIIAFVYgwklALVGLATVPLLLLAGYLRMRLLSGFEEKNKKaYEESSK-----IASEAVSNIRTVASLTLE 212
|
170
....*....|....*..
gi 2462549072 1166 ERFIHQSDLKVDENQKA 1182
Cdd:cd18578 213 DYFLEKYEEALEEPLKK 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
745-853 |
1.16e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.03 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 745 LAEMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGML-KNKTRILVTHSM 823
Cdd:PRK13537 122 LLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERL---RSLLaRGKTILLTTHFM 198
|
90 100 110
....*....|....*....|....*....|..
gi 2462549072 824 SYLPQV--DVIIVMSGGKISEmGSYQELLARD 853
Cdd:PRK13537 199 EEAERLcdRLCVIEEGRKIAE-GAPHALIESE 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
748-844 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 748 MDKVEGHVAIKGV------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNkTRILVTH 821
Cdd:cd03298 109 IEVALARVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKM-TVLMVTH 187
|
90 100
....*....|....*....|....
gi 2462549072 822 SMSYLPQV-DVIIVMSGGKISEMG 844
Cdd:cd03298 188 QPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
995-1257 |
1.28e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 49.01 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 995 DDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKEL 1074
Cdd:cd18540 30 DHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1075 DTVDSMIPEVIKMFMGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVsrspVYSHFN 1150
Cdd:cd18540 110 QRLGEIISWGLVDLVWGITYMIGILIVMLILNWklalIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1151 ETLLGVSVIRAF--EEQerfiHQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLV---G 1225
Cdd:cd18540 186 EGITGAKTTKTLvrEEK----NLREFKEL-TEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAItigT 260
|
250 260 270
....*....|....*....|....*....|....
gi 2462549072 1226 LSV--SYSLQVTTYLNWLVRMSSEMETNIVAVER 1257
Cdd:cd18540 261 LVAfiSYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1046-1161 |
1.38e-05 |
|
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: 48.74 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1046 LLHSILRSPMSFFERTPSGNLVNRFSkELDTV-DSMIPEVIKMFMGSLFNVIgACIVILLATP----IAAIIIPPLGLIY 1120
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIrGFLTGTALTTLLDVLFSVI-YIAVLFSYSPlltlVVLATVPLQLLLT 158
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462549072 1121 FFVQRFYvasSRQLKRLESvSRSPVYSHFNETLLGVSVIRA 1161
Cdd:cd18782 159 FLFGPIL---RRQIRRRAE-ASAKTQSYLVESLTGIQTVKA 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1274-1458 |
1.67e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1274 ETAPPSSwPQVGRVeFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDginia 1353
Cdd:COG2401 18 SSVLDLS-ERVAIV-LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1354 kiglhdlrFKITIIPQDPVLfsgslrmnLDPFsqYSDEEVWTSLELAH---LKDFVSALpDKLDHecaeggenLSVGQRQ 1430
Cdd:COG2401 91 --------VPDNQFGREASL--------IDAI--GRKGDFKDAVELLNavgLSDAVLWL-RRFKE--------LSTGQKF 143
|
170 180
....*....|....*....|....*...
gi 2462549072 1431 LVCLARALLRKTKILVLDEATAAVDLET 1458
Cdd:COG2401 144 RFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
697-856 |
1.68e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 49.07 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTwaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG----------------- 759
Cdd:PRK09536 4 IDVSDLSVE--FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrrvas 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 --------------------------------------------------------VNLSGGQKQRVSLARAVYSNADIY 783
Cdd:PRK09536 82 vpqdtslsfefdvrqvvemgrtphrsrfdtwtetdraaveramertgvaqfadrpvTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 784 LFDDPLSAVDAHVGKHIFENV--IGPKGmlknKTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSYQELLARD---GAF 856
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVrrLVDDG----KTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTADtlrAAF 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
762-853 |
1.68e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.62 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQ-VDVIIV 834
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMR-------LLKslqtdeNKTIILVSHDMNEVARyADEVIV 218
|
90
....*....|....*....
gi 2462549072 835 MSGGKISEMGSYQELLARD 853
Cdd:PRK13646 219 MKEGSIVSQTSPKELFKDK 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-829 |
1.75e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.11 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 696 SITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMD---KVEGHV--------------- 755
Cdd:PRK14258 7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELEsevRVEGRVeffnqniyerrvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 756 ---------------------------------------------AIK---------------GVNLSGGQKQRVSLARA 775
Cdd:PRK14258 85 rlrrqvsmvhpkpnlfpmsvydnvaygvkivgwrpkleiddivesALKdadlwdeikhkihksALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 776 VYSNADIYLFDDPLSAVDAHVGKHIfENVIGPKGMLKNKTRILVTHSMsylPQV 829
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHNL---HQV 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1310-1514 |
1.76e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.01 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1310 TINGGEKVGIVGRTGAGKSSL---TLGLFrineSAEGEIIIDGINIAKIGLHDL-RFKITIIPQDPVLFSgslrMnldpf 1385
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLlarMAGLL----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFA----M----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1386 sqysdeEVWTSLEL-----AHLKDFVSALPD-----KLDHECAEGGENLSVGQRQLVCLARALLR-------KTKILVLD 1448
Cdd:PRK03695 85 ------PVFQYLTLhqpdkTRTEAVASALNEvaealGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 1449 EATAAVDLETDDLIQSTIRtqfEDC----TVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQQRGL 1514
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLS---ELCqqgiAVVMSSHDLNHTLRHaDRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1424-1508 |
1.87e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1424 LSVGQRQLVCLARALLRKTKILVLDEATAAV-DLETDDLIqSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE-I 1499
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEICdDVTVFRDGQfI 220
|
....*....
gi 2462549072 1500 QEYgAPSDL 1508
Cdd:PRK10762 221 AER-EVADL 228
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1314-1498 |
2.14e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.21 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1314 GEKVGIVGRTGAGKSSLTLGLFR-INESAEGEIIIDGINIAKIGLHDLRFKITiipqdpvlfsgslrmnldpfsqysdee 1392
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1393 vwtslelahlkdfvsalpdkldhecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-- 1470
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462549072 1471 -----EDCTVLTIAHRLNTIMD------YTRVIVLDKGE 1498
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPallrrrFDRRIVLLLIL 148
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
762-848 |
2.79e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-----------HVGKHIfenvigpkgmlknKTRIL-VTHSMSYLPQV 829
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrellpyleRLAREI-------------NIPILyVSHSLDEILRL 195
|
90 100
....*....|....*....|
gi 2462549072 830 -DVIIVMSGGKISEMGSYQE 848
Cdd:PRK11144 196 aDRVVVLEQGKVKAFGPLEE 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
714-851 |
2.90e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.76 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLL-------------------------SALLA---------------------- 746
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFlhfngilkptsgevlikgepikydkKSLLEvrktvgivfqnpddqlfaptve 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 747 ------------EMDKVEGHV--AIKGV-----------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 801
Cdd:PRK13639 98 edvafgplnlglSKEEVEKRVkeALKAVgmegfenkpphHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 802 ENV--IGPKGMlknkTRILVTHSMSYLP-QVDVIIVMSGGKISEMGSYQELLA 851
Cdd:PRK13639 178 KLLydLNKEGI----TIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
1050-1171 |
3.01e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 47.89 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1050 ILRSPMSFFERTPSGNLVNRFSkELDTVDSMIPE-VIKMFMGSLFnVIGACIVILLATPIAAIIIPPLGLIYFFvqrFYV 1128
Cdd:cd18555 85 LLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNqVISLIIDLLL-LVIYLIYMLYYSPLLTLIVLLLGLLIVL---LLL 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462549072 1129 ASSRQLKRL---ESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQ 1171
Cdd:cd18555 160 LTRKKIKKLnqeEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKK 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1303-1509 |
3.68e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGINIAKIGLHDLRF----KITIIPQDPVL 1373
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1374 fsgslrmNLDPFSQYSDE------------------EVWTSLELAHLKDFVSALPDkLDHEcaeggenLSVGQRQLVCLA 1435
Cdd:PRK15134 104 -------SLNPLHTLEKQlyevlslhrgmrreaargEILNCLDRVGIRQAAKRLTD-YPHQ-------LSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549072 1436 RALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1509
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLAdRVAVMQNGRCVEQNRAATLF 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
705-788 |
4.37e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.14 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 705 TWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLL------------------------------------------- 741
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLkilagelepdsgevsipkglrigylpqeppldddltvldtvld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 742 -----SALLAEMDKVEGHVA---------------------------IKGV----------------NLSGGQKQRVSLA 773
Cdd:COG0488 85 gdaelRALEAELEELEAKLAepdedlerlaelqeefealggweaearAEEIlsglgfpeedldrpvsELSGGWRRRVALA 164
|
170
....*....|....*
gi 2462549072 774 RAVYSNADIYLFDDP 788
Cdd:COG0488 165 RALLSEPDLLLLDEP 179
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
761-853 |
4.46e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKI 840
Cdd:PRK10522 449 KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
90
....*....|....
gi 2462549072 841 SEM-GSYQELLARD 853
Cdd:PRK10522 528 SELtGEERDAASRD 541
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1303-1462 |
5.63e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.31 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFK--------ITIIP--- 1368
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1369 -QDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAhlkdfvsalpDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVL 1447
Cdd:PRK10584 105 aLENVELPALLRGESSRQSRNGAKALLEQLGLG----------KRLDHLPAQ----LSGGEQQRVALARAFNGRPDVLFA 170
|
170
....*....|....*
gi 2462549072 1448 DEATAAVDLETDDLI 1462
Cdd:PRK10584 171 DEPTGNLDRQTGDKI 185
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
761-870 |
7.34e-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: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahVG-KHIFENVIGpkGMLKNKTRILVThSmSYLPQV----DVIIVM 835
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID--VGaKAEIYRLIR--ELAAEGKAVIVI-S-SELPELlglsDRILVM 467
|
90 100 110
....*....|....*....|....*....|....*
gi 2462549072 836 SGGKISEMgsyqelLARDGAFAEFLRTYASTEQEQ 870
Cdd:COG1129 468 REGRIVGE------LDREEATEEAIMAAATGGAAA 496
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
762-849 |
7.63e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQK-ENMALVLITHDLALVAEAaHKIIVMYAGQV 232
|
....*....
gi 2462549072 841 SEMGSYQEL 849
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
714-824 |
7.70e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.96 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKG--------------------------------- 759
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNGqpmsklssaakaelrnqklgfiyqfhhllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 ----------------------------------------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 799
Cdd:PRK11629 104 alenvamplligkkkpaeinsralemlaavglehranhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|....*
gi 2462549072 800 IFEnVIGPKGMLKNKTRILVTHSMS 824
Cdd:PRK11629 184 IFQ-LLGELNRLQGTAFLVVTHDLQ 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1303-1508 |
7.76e-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: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDG--IN--------IAKI------------- 1355
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTL-LrmvaGLERI---TSGEIWIGGrvVNelepadrdIAMVfqnyalyphmsvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1356 -----GLhdlrfKITIIPQDPVlfsgSLRMnldpfsqysdEEVWTSLELAHLkdfvsalpdkLDHECAEggenLSVGQRQ 1430
Cdd:PRK11650 95 enmayGL-----KIRGMPKAEI----EERV----------AEAARILELEPL----------LDRKPRE----LSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1431 LVCLARALLRKTKILVLDEATAAVD--------LETDDLiQSTIRT--------QFEdctVLTIAHRLntimdytrvIVL 1494
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLEIQRL-HRRLKTtslyvthdQVE---AMTLADRV---------VVM 208
|
250
....*....|....
gi 2462549072 1495 DKGEIQEYGAPSDL 1508
Cdd:PRK11650 209 NGGVAEQIGTPVEV 222
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1047-1258 |
7.93e-05 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 46.28 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1047 LHSILRSPMSFFERTPSGNLVNRFSkelDTvdSMIPEVIKMFMGSLF-NVIGACIV-ILLA------TPIAAIIIPPLGL 1118
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN---DA--NKIREAISSTTISLFlDLLMVIISgIILFfynwklFLITLLIIPLYIL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1119 IYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS---IVANRWLAV 1195
Cdd:cd18570 157 IILLFNKPF----KKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLgklSNLQSSIKG 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 1196 RLECVGNCIVLFAALFAVISrHSLSAG-LVGLsvsYSLQV--TTYLNWLVRMSSEMETNIVAVERL 1258
Cdd:cd18570 233 LISLIGSLLILWIGSYLVIK-GQLSLGqLIAF---NALLGyfLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
758-848 |
8.17e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.86 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 KGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMS 836
Cdd:PRK10247 133 KNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
90
....*....|..
gi 2462549072 837 ggkiSEMGSYQE 848
Cdd:PRK10247 212 ----PHAGEMQE 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1306-1497 |
8.20e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.14 E-value: 8.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1306 HINVTINGGEKVGIVGRTGAGKSS----LTlGLFRineSAEGEIIIDGIN--------IAKIGL-----HDLRFK-ITII 1367
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTvfncLT-GFYK---PTGGTILLRGQHieglpghqIARMGVvrtfqHVRLFReMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1368 PQDPV---------LFSGSLRMnldPFSQYSDEE------VWtsLELAHLKDFVSAlpdkldhecaEGGeNLSVGQRQLV 1432
Cdd:PRK11300 99 ENLLVaqhqqlktgLFSGLLKT---PAFRRAESEaldraaTW--LERVGLLEHANR----------QAG-NLAYGQQRRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1433 CLARALLRKTKILVLDEATAAVD-LETDDLIQ--STIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKG 1497
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) ... |
761-837 |
8.26e-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: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD-------AHVGKHIFENvigpkgmlKNKTRILVTHSM---SYLpqVD 830
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaSKVIRRFAEN--------NEKTAFVVEHDIimiDYL--AD 184
|
....*..
gi 2462549072 831 VIIVMSG 837
Cdd:cd03237 185 RLIVFEG 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
717-759 |
8.83e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.13 E-value: 8.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2462549072 717 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG 759
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG 68
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
762-852 |
9.12e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.85 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF---ENVI---GPkGMLknktriLVTHSMSYLPQV-DVIIV 834
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILdllESIVqkrAL-GML------LVTHDMGVVARLaDDVAV 213
|
90
....*....|....*...
gi 2462549072 835 MSGGKISEMGSYQELLAR 852
Cdd:PRK10418 214 MSHGRIVEQGDVETLFNA 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
666-788 |
9.44e-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: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 666 LKRLriflshEELEPDSIERR--------PVKDGGGTNSITVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGK 737
Cdd:COG0488 283 IKAL------EKLEREEPPRRdktveirfPPPERLGKKVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 738 SSLLSALLAEMDKVEGHVAIkGVN-------------------------------------------------------L 762
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKL-GETvkigyfdqhqeeldpdktvldelrdgapggteqevrgylgrflfsgddafkpvgvL 433
|
170 180
....*....|....*....|....*.
gi 2462549072 763 SGGQKQRVSLARAVYSNADIYLFDDP 788
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1018-1167 |
1.07e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 45.94 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1018 ISQGIAVFGYSMAVSIGG--ILASrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNV 1095
Cdd:cd18576 47 LLQAVFSFFRIYLFARVGerVVAD--LRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTL 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 1096 IGACIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQlkRLESVSRSPVysHFNETLLGVSVIRAF--EEQER 1167
Cdd:cd18576 125 IGGVVLLFFISWkltlLMLATVPVVVLVAVLFGRRIRKLSKK--VQDELAEANT--IVEETLQGIRVVKAFtrEDYEI 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
761-841 |
1.08e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhIFE-----NVIgpKGMLKNKTRILVTHSMS---YLpqVDVI 832
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQrlnvaRLI--RELAEGKYVLVVEHDLAvldYL--ADNV 281
|
90
....*....|....
gi 2462549072 833 IVMSG-----GKIS 841
Cdd:PRK13409 282 HIAYGepgayGVVS 295
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
762-850 |
1.13e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.81 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVIGPkgmLKNK-TRILVTHSMSYLPQV-DVIIVMSGGK 839
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITE---LKNEiAIVIVSHNPQQVARVaDYVAFLYNGE 229
|
90
....*....|.
gi 2462549072 840 ISEMGSYQELL 850
Cdd:PRK14246 230 LVEWGSSNEIF 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
714-821 |
1.30e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG-------------------HVAIKG--------------- 759
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVagcvdvpdnqfgreaslidAIGRKGdfkdavellnavgls 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 760 ---------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD---AHVGKHIFENVIGPKGmlknKTRILVTH 821
Cdd:COG2401 126 davlwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARRAG----ITLVVATH 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1424-1518 |
1.37e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1424 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIrTQFEDcTVLTIAH-RL---NTIMdyTRVIVLDKGEI 1499
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHdRQfvdNTVT--ECWIFEGNGKI 516
|
90 100
....*....|....*....|
gi 2462549072 1500 QEY-GAPSDLLQQRGLFYSM 1518
Cdd:PRK11147 517 GRYvGGYHDARQQQAQYLAL 536
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
681-849 |
1.38e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.98 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 681 DSIERRPVKDGGG-TNSITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG 759
Cdd:PRK11607 3 DAIPRPQAKTRKAlTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 VN-------------------------------------------------------------------LSGGQKQRVSL 772
Cdd:PRK11607 81 VDlshvppyqrpinmmfqsyalfphmtveqniafglkqdklpkaeiasrvnemlglvhmqefakrkphqLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 773 ARAVYSNADIYLFDDPLSAVDAHVGKH-------IFENVigpkgmlkNKTRILVTHSM-SYLPQVDVIIVMSGGKISEMG 844
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRmqlevvdILERV--------GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIG 232
|
....*
gi 2462549072 845 SYQEL 849
Cdd:PRK11607 233 EPEEI 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1423-1486 |
1.51e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549072 1423 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDlETD-----DLIQStIRTQfeDCTVLTIAHRLNTIM 1486
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 ... |
705-794 |
1.63e-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: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 705 TWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------------------AIKG 759
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngtplaeqrdephenilylghlpGLKP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 760 ----------------------------VNLSG-----------GQKQRVSLARAVYSNADIYLFDDPLSAVDA 794
Cdd:TIGR01189 87 elsalenlhfwaaihggaqrtiedalaaVGLTGfedlpaaqlsaGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
726-793 |
1.79e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.57 E-value: 1.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549072 726 LVAVVGQVGCgkSSLLSALLAEmdkveghvaikgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 793
Cdd:PRK10771 110 LHAIARQMGI--EDLLARLPGQ--------------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
762-876 |
2.09e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLkNKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQEL-NMGLLFITHNLSIVRKLaDRVAVMQNGRC 235
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462549072 841 SEMGSYQELLARDgafaeflrTYASTEQEQDAEENG 876
Cdd:PRK15134 236 VEQNRAATLFSAP--------THPYTQKLLNSEPSG 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
714-794 |
2.31e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.68 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSG-GQKQRVSLARAVYsnadiYLFDDPLSAV 792
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQ-----MVFQDSISAV 102
|
..
gi 2462549072 793 DA 794
Cdd:PRK10419 103 NP 104
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1319-1466 |
2.77e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1319 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGL-------HDLRFKITIIPQDpvlfsgslrmNLDPFSqysde 1391
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyigHNLGLKLEMTVFE----------NLKFWS----- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 1392 EVWTSLELAHLKDFVSALPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTI 1466
Cdd:PRK13541 96 EIYNSAETLYAAIHYFKLHDLLDEKCY----SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1023-1187 |
3.18e-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: 44.48 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1023 AVFGYSMAVSIGGiLASRCLH---VDLLHSILRSPMSFFERTPSGNL-------VNRFSKELDTvdsMIPEVIKMFMGSL 1092
Cdd:cd18565 68 SLFQYLSGVLWRR-FAQRVQHdlrTDTYDHVQRLDMAFFEDRQTGDLmsvlnndVNQLERFLDD---GANSIIRVVVTVL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1093 fnVIGAcIVILLATPIAAIIIPPLGLIYFFVQRFyvasSRQLKRLESVSRSPV---YSHFNETLLGVSVIRAF----EEQ 1165
Cdd:cd18565 144 --GIGA-ILFYLNWQLALVALLPVPLIIAGTYWF----QRRIEPRYRAVREAVgdlNARLENNLSGIAVIKAFtaedFER 216
|
170 180
....*....|....*....|....*...
gi 2462549072 1166 ERFIHQSDLKVDENQKA------YYPSI 1187
Cdd:cd18565 217 ERVADASEEYRDANWRAirlraaFFPVI 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
762-850 |
3.24e-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: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGM-LKNKTRILVTHSMSY--LPQVDVIIVMSGG 838
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVL---KGLaQKGKTIICTIHQPSSelFELFDKIILMAEG 243
|
90
....*....|..
gi 2462549072 839 KISEMGSYQELL 850
Cdd:TIGR00955 244 RVAYLGSPDQAV 255
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
754-872 |
3.47e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.23 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 754 HVAIKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNK--TRILVTHSMSY-LPQV 829
Cdd:PRK09984 144 HFAHQRVStLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL---RDINQNDgiTVVVTLHQVDYaLRYC 220
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462549072 830 DVIIVMSGGKISEMGSYQELlaRDGAFAEFLRTYASTEQEQDA 872
Cdd:PRK09984 221 ERIVALRQGHVFYDGSSQQF--DNERFDHLYRSINRVEENAKA 261
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
720-821 |
4.65e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 720 SIPEGALVAVVGQVGCGKSSLLSA----LLAEMDKVEGHVAIK-GVN--------------LSGGQKQRVSLARAV---- 776
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAiglaLGGAQSATRRRSGVKaGCIvaavsaeliftrlqLSGGEKELSALALILalas 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462549072 777 YSNADIYLFDDPLSAVDAHVGkHIFENVIgpKGMLKNKTR-ILVTH 821
Cdd:cd03227 97 LKPRPLYILDEIDRGLDPRDG-QALAEAI--LEHLVKGAQvIVITH 139
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1307-1503 |
5.06e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1307 INVTINGGEKVGIVGRTGAGKSSLtlglfrINESA------EGEIIIDGINiakigLHDLRFKITIIP---------QDP 1371
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSL------INAISgltrpqKGRIVLNGRV-----LFDAEKGICLPPekrrigyvfQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1372 VLF-----SGSLRMNLDPFSQYSDEEVWTSLELAHLkdfVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILV 1446
Cdd:PRK11144 86 RLFphykvRGNLRYGMAKSMVAQFDKIVALLGIEPL---LDRYP-----------GSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1447 LDEATAAVD----------LETddLIQsTIRTqfedcTVLTIAHRLNTIM---DytRVIVLDKGEIQEYG 1503
Cdd:PRK11144 152 MDEPLASLDlprkrellpyLER--LAR-EINI-----PILYVSHSLDEILrlaD--RVVVLEQGKVKAFG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
761-851 |
5.41e-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: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDP---LSAVDAHVGKHIFENvIGPKGMlknkTRILVTHSMSYLPQV-DVIIVMS 836
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPaagLNPEETEELAELIRE-LRERGI----TVLLVEHDMDVVMSLaDRVTVLD 217
|
90
....*....|....*
gi 2462549072 837 GGKISEMGSYQELLA 851
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) ... |
761-793 |
5.50e-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: 5.50e-04
10 20 30
....*....|....*....|....*....|...
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 793
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
1042-1161 |
6.04e-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: 43.73 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1042 LHVDLLHSILRSPMSFFERTPSGNLVNRFsKELDTV-DSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIiipPLGLIY 1120
Cdd:cd18566 77 LSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIrEFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLV---PLVLLG 152
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462549072 1121 FFVQRFYVASSRQLKRLESVSRSPV--YSHFNETLLGVSVIRA 1161
Cdd:cd18566 153 LFVLVAILLGPILRRALKERSRADErrQNFLIETLTGIHTIKA 195
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1282-1510 |
6.31e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.15 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1282 PQVgrVEFRNYCLRYREDLdfvLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRI-----NESAeGEIIIDGINIAkig 1356
Cdd:PRK10418 2 PQQ--IELRNIALQAAQPL---VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagvRQTA-GRVLLDGKPVA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1357 LHDLR-FKITIIPQDPvlfsgslRMNLDPFSQYSDEEVWTSLELAHLKDfVSALPDKLDhecAEGGEN-----------L 1424
Cdd:PRK10418 73 PCALRgRKIATIMQNP-------RSAFNPLHTMHTHARETCLALGKPAD-DATLTAALE---AVGLENaarvlklypfeM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1425 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETD----DLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEI 1499
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQarilDLLESIVQKR--ALGMLLVTHDMGVVARLAdDVAVMSHGRI 219
|
250
....*....|.
gi 2462549072 1500 QEYGAPSDLLQ 1510
Cdd:PRK10418 220 VEQGDVETLFN 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
763-849 |
6.49e-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: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 763 SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLK--NKTRILVTHSMSYLPQV-DVIIVMSGGK 839
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI---EKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGR 209
|
90
....*....|
gi 2462549072 840 ISEMGSYQEL 849
Cdd:cd03265 210 IIAEGTPEEL 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
716-795 |
6.71e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 716 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------------------AIKG----------- 759
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhqdllylghqpGIKTeltalenlrfy 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 760 ------------------VNLSG-----------GQKQRVSLARAVYSNADIYLFDDPLSAVDAH 795
Cdd:PRK13538 99 qrlhgpgddealwealaqVGLAGfedvpvrqlsaGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1057-1258 |
6.89e-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: 43.56 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1057 FFERTPSGNLVNRFSKELD-TVDSMIPEVIKMFMGSLFNVIGACIVILL---ATPIAAIIIPplglIYFFVQRFYVASSR 1132
Cdd:cd18554 96 YYANNRSGEIISRVINDVEqTKDFITTGLMNIWLDMITIIIAICIMLVLnpkLTFVSLVIFP----FYILAVKYFFGRLR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1133 QLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDlkvDENQKAYYPSIVANRWLAVRLECV------GNCIVL 1206
Cdd:cd18554 172 KLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVntitdlAPLLVI 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 1207 FAALFAVISrHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1258
Cdd:cd18554 249 GFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1046-1236 |
7.84e-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: 43.22 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1046 LLHSILRSPMSFFERTPSGNLVNRFSkELDTVDSMIpevIKMFMGSLFN---VIGACIVILLATPIAAIIIPPLGLIYFF 1122
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFG-SLDEIQQTL---TTGFVEALLDglmAILTLVMMFLYSPKLALIVLAAVALYAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1123 VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIHQSDLKVDENQKayypSIVANRWLAVR----- 1196
Cdd:cd18567 157 LRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFgREAEREARWLNLLVDAINA----DIRLQRLQILFsaang 232
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549072 1197 -LECVGNCIVLFAALFAVISRHsLSAG-LVGLsVSYSLQVTT 1236
Cdd:cd18567 233 lLFGLENILVIYLGALLVLDGE-FTVGmLFAF-LAYKDQFSS 272
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1307-1455 |
8.91e-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: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1307 INVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIaKIGLHDLRFKITIIPQDPVLFSG-SLRMNLDPF 1385
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549072 1386 SQY---SDEEVWTSLElAHLKDfvsalpDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1455
Cdd:TIGR01257 1028 AQLkgrSWEEAQLEME-AMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1050-1258 |
9.97e-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: 42.93 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1050 ILRSPMSFFERTPSGNLVNRFsKELDTVDSMI-PEVIKMFMGSLFNVIgaCIVILLA-----TPIAAIIIPPLGLIyffv 1123
Cdd:cd18568 85 LLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFI--YLGLMFYynlqlTLIVLAFIPLYVLL---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1124 qrfYVASSRQLKRLES---VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVanrwLAVRLECV 1200
Cdd:cd18568 158 ---TLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQK----LSIVLQLI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549072 1201 -------GNCIVLFAALFAVISrHSLSAG-LVGLSVSYSLqVTTYLNWLVRMSSEMETNIVAVERL 1258
Cdd:cd18568 231 sslinhlGTIAVLWYGAYLVIS-GQLTIGqLVAFNMLFGS-VINPLLALVGLWDELQETRISVERL 294
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
762-851 |
1.03e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.85 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeNVigpkgMLKNKTR-----ILVTHSMSYLPQV-DVIIVM 835
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI-NL-----MLELQEKqgisyIYVTQHLGMMKHIsDQVLVM 223
|
90
....*....|....*.
gi 2462549072 836 SGGKISEMGSYQELLA 851
Cdd:PRK15112 224 HQGEVVERGSTADVLA 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
758-793 |
1.07e-03 |
|
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: 1.07e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2462549072 758 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 793
Cdd:cd03218 130 KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1303-1480 |
1.11e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 42.38 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1303 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFR-INESAEGEIIIDGINIAKIGlhdlrfkitiiPQDPVLFSGSlrmN 1381
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTL-LNLIAgFVPYQHGSITLDGKPVEGPG-----------AERGVVFQNE---G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1382 LDPFSQYSDEeVWTSLELAHL-----KDFVSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKTKILVLDEATAAV 1454
Cdd:PRK11248 81 LLPWRNVQDN-VAFGLQLAGVekmqrLEIAHQMLKKVGLEGAEKRYiwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 2462549072 1455 DLETDDLIQSTIRTQFEDC--TVLTIAH 1480
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETgkQVLLITH 187
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
693-817 |
1.32e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.44 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 693 GTNSITVRNATFTwaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSGGQKQRVSL 772
Cdd:PRK11831 4 VANLVDMRGVSFT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462549072 773 ARAVYSnadiYLFDDPLSAVDAHVgkhiFENVIGPkgmLKNKTRI 817
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 ... |
705-794 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 705 TWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------------------AIKG 759
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfqrdsiargllylghapGIKT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549072 760 V-------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 794
Cdd:cd03231 87 TlsvlenlrfwhadhsdeqveealarvglngfedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
761-837 |
1.37e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD-------AHVGKHIFENvigpkgmlKNKTRILVTH---SMSYLpqVD 830
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE--------REATALVVDHdiyMIDYI--SD 522
|
....*..
gi 2462549072 831 VIIVMSG 837
Cdd:PRK13409 523 RLMVFEG 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
762-851 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLkNKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEM-EQTFIIVSHDMDFVLDVcDRAALMRDGKI 506
|
90
....*....|.
gi 2462549072 841 SEMGSYQELLA 851
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
761-793 |
1.79e-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: 1.79e-03
10 20 30
....*....|....*....|....*....|...
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 793
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
762-851 |
1.83e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.12 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKN-----KTRILVTHSMSYLPQ-VDVIIVM 835
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-------LFKDyqkagHTVILVTHNMDDVAEyADDVLVL 218
|
90
....*....|....*.
gi 2462549072 836 SGGKISEMGSYQELLA 851
Cdd:PRK13641 219 EHGKLIKHASPKEIFS 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
697-853 |
1.83e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.10 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV---------------- 760
Cdd:PRK13652 4 IETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 ------------------------------------------------------NLSGGQKQRVSLARAVYSNADIYLFD 786
Cdd:PRK13652 83 vfqnpddqifsptveqdiafgpinlgldeetvahrvssalhmlgleelrdrvphHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 787 DPLSAVDAHVGKHIFE---NVIGPKGMlknkTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARD 853
Cdd:PRK13652 163 EPTAGLDPQGVKELIDflnDLPETYGM----TVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
762-844 |
2.31e-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: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMlkNKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:cd03266 137 FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL--GKCILFSTHIMQEVERLcDRVVVLHRGRV 214
|
....
gi 2462549072 841 SEMG 844
Cdd:cd03266 215 VYEG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
762-821 |
2.53e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 41.30 E-value: 2.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfENVIGPKGMLKNKTRILVTH 821
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI-ADLLFSLNREHGTTLILVTH 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
741-793 |
3.38e-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: 3.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 741 LSALLAEMDKveGHVA-IKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 793
Cdd:COG1137 117 LEELLEEFGI--THLRkSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
762-849 |
3.39e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpkGMLKNKTR---ILVTHSMSYLPQV-DVIIVMSG 837
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLI----KVLQKEMSmgvIFITHDMGVVAEIaDRVLVMYQ 244
|
90
....*....|..
gi 2462549072 838 GKISEMGSYQEL 849
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
714-840 |
4.00e-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: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI------------------------------------ 757
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiaarnrigylpeerglypkmkvidqlvyla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 758 --KGVN---------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVIGPk 808
Cdd:cd03269 96 qlKGLKkeearrridewlerlelseyankrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRE- 173
|
170 180 190
....*....|....*....|....*....|....*
gi 2462549072 809 gmLK--NKTRILVTHSMSYLPQV-DVIIVMSGGKI 840
Cdd:cd03269 174 --LAraGKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
697-850 |
4.08e-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: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 697 ITVRNATftWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG----------------------- 753
Cdd:COG1119 4 LELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvwelrkrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 754 -----------------HVAIKGV------------------------------------NLSGGQKQRVSLARAVYSNA 780
Cdd:COG1119 82 lvspalqlrfprdetvlDVVLSGFfdsiglyreptdeqrerarellellglahladrpfgTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 781 DIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSYQELL 850
Cdd:COG1119 162 ELLILDEPTAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1046-1127 |
4.27e-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: 40.76 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1046 LLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVIL-LA---TPIAAIIIPplglIYF 1121
Cdd:cd18784 75 LFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFkLSwqlSLVTLIGLP----LIA 150
|
....*.
gi 2462549072 1122 FVQRFY 1127
Cdd:cd18784 151 IVSKVY 156
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
759-793 |
4.63e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 40.65 E-value: 4.63e-03
10 20 30
....*....|....*....|....*....|....*
gi 2462549072 759 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 793
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
762-852 |
4.78e-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: 41.21 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 762 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKNKTR------ILVTHSMSYLPQV-DVIIV 834
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHDLGVVRRFaDRVAV 229
|
90
....*....|....*...
gi 2462549072 835 MSGGKISEMGSYQELLAR 852
Cdd:COG4172 230 MRQGEIVEQGPTAELFAA 247
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
749-840 |
5.11e-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: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 749 DKVEGHVAIKGvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRILVTHSm 823
Cdd:cd03234 133 LTRIGGNLVKG--ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS-------TLSqlarrNRIVILTIHQ- 202
|
90 100
....*....|....*....|...
gi 2462549072 824 sylPQVDV------IIVMSGGKI 840
Cdd:cd03234 203 ---PRSDLfrlfdrILLLSSGEI 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
761-837 |
5.19e-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: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD-------AHVGKHIFENvigpkgmlKNKTRILVTHSMSYLPQV-DVI 832
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAEN--------RGKTAMVVDHDIYLIDYIsDRL 526
|
....*
gi 2462549072 833 IVMSG 837
Cdd:COG1245 527 MVFEG 531
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
761-829 |
6.09e-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: 6.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549072 761 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgkhifENVIGPKGMLKN--KTRILVTHSMSYLPQV 829
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLQEypGTVVAVTHDRYFLDNV 224
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1050-1258 |
6.23e-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: 40.55 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1050 ILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATP----IAAIIIP-PLGLIYFFVQ 1124
Cdd:cd18575 79 LLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltlLVLLVIPlVVLPIILFGR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1125 RFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF--EEQERFIHQSDLkvdenQKAYypsIVANRWLAVRLECVGN 1202
Cdd:cd18575 159 RVRRLSRASQDRLADLS-----AFAEETLSAIKTVQAFtrEDAERQRFATAV-----EAAF---AAALRRIRARALLTAL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549072 1203 CIVL-FAALFAVI-------SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1258
Cdd:cd18575 226 VIFLvFGAIVFVLwlgahdvLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1294-1343 |
6.24e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 6.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462549072 1294 LRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESAEG 1343
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTL-LALLKNEISADG 55
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
760-841 |
6.53e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 760 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahVG-KHIFENVI---GPKGMlknkTRILVThsmSYLPQV----DV 831
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID--VGaKHEIYNVIyelAAQGV----AVLFVS---SDLPEVlgvaDR 465
|
90
....*....|
gi 2462549072 832 IIVMSGGKIS 841
Cdd:PRK11288 466 IVVMREGRIA 475
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
642-794 |
6.74e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 40.95 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 642 FNILRFPLNILPMVISSIVQASVSLKRLRIF---LSHEELEPDSIERRPVKDGGGtnsITVRNATFTwARSDPPTLNGIT 718
Cdd:COG4178 308 FGQVQGALSWFVDNYQSLAEWRATVDRLAGFeeaLEAADALPEAASRIETSEDGA---LALEDLTLR-TPDGRPLLEDLS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549072 719 FSIPEGALVAVVGQVGCGKSSLLSAL--------------------------------LAE------------------- 747
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgriarpagarvlflpqrpylplgtLREallypataeafsdaelrea 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462549072 748 MDKVE-GHVAIK-------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 794
Cdd:COG4178 464 LEAVGlGHLAERldeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
714-746 |
7.52e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 7.52e-03
10 20 30
....*....|....*....|....*....|...
gi 2462549072 714 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLA 746
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS-LIA 48
|
|
| |
