|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-1366 |
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: 834.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 43 PNPVDDAGLLSFATFSWLTPVMIRSYKHTLTVDTLPPLSPYDSSDINAKRFQILWEEEIKRVG----------------- 105
Cdd:TIGR00957 201 PCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRkqpvsavygkkdpskpk 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 106 ---------------------PEKASLGRVVWKFQRTRVLMDVVANILCIVMAALGPTVLihQILQHITSISSGHIGIGI 164
Cdd:TIGR00957 281 gssqldaneevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQIL--SLLIRFVNDPMAPDWQGY 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 165 CLCLALFTTEFTKVLFWALAWAINYRTAIRLKVALSTLIFENLLSFKTLTHISA--GEVLNILSSDSYSLFEAALFCPLP 242
Cdd:TIGR00957 359 FYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSStvGEIVNLMSVDAQRFMDLATYINMI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 243 ATIPiLMVVCAVYAFFI-LGSTALVGISVYLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEES 321
Cdd:TIGR00957 439 WSAP-LQVILALYFLWLnLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 322 FINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCHIFLKRK--LTAPVAFSVIAMFNVMKFSIAILPFSV 399
Cdd:TIGR00957 518 FLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 400 KAVAEASVSLRRMKKILiaksppsyiTQPE-DPDTI------------LLLANATLTWEQeinrkSDPPkaqiqkrhvfk 466
Cdd:TIGR00957 598 SSIVQASVSLKRLRIFL---------SHEElEPDSIerrtikpgegnsITVHNATFTWAR-----DLPP----------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 467 kqrpelyseqsrsdqgvaspewqsgspksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAY 546
Cdd:TIGR00957 653 -----------------------------TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAY 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 547 VSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYL 626
Cdd:TIGR00957 704 VPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 627 LDDPLSAVDAHVGKHVFEECI--KKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN-- 702
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTya 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 703 --------------LRGLQFKDPEHIYNVAMVETLKESPAQRDEDAvlASGDEKDEGKE-PETEEFVDTNAPAH--QLIQ 765
Cdd:TIGR00957 864 pdeqqghledswtaLVSGEGKEAKLIENGMLVTDVVGKQLQRQLSA--SSSDSGDQSRHhGSSAELQKAEAKEEtwKLME 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 766 TESPQEGIVTWKTYHTYIKASGgYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDrgSQVVCASQNNKTacnvdqtlqdtkh 845
Cdd:TIGR00957 942 ADKAQTGQVELSVYWDYMKAIG-LFITFLSIFLFVCNHVSALASNYWLSLWTD--DPMVNGTQNNTS------------- 1005
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 846 hmYQL-VYIAsmvsvlmFGIIKGFTFTNTTL-------MASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD 917
Cdd:TIGR00957 1006 --LRLsVYGA-------LGILQGFAVFGYSMavsiggiQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVD 1076
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 918 VRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGV 997
Cdd:TIGR00957 1077 SMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSV 1156
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 998 IHAYDKKDDCISKFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLL 1077
Cdd:TIGR00957 1157 IRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYL 1236
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1078 QVCVRTGTETQAKFTSAELLREYILTcvpEHTHPFKV-GTCPKD-WPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQ 1155
Cdd:TIGR00957 1237 NWLVRMSSEMETNIVAVERLKEYSET---EKEAPWQIqETAPPSgWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGE 1313
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1156 TVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWH 1235
Cdd:TIGR00957 1314 KVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWW 1393
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1236 VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTV 1315
Cdd:TIGR00957 1394 ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTV 1473
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1316 LTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMllAAEVGL 1366
Cdd:TIGR00957 1474 LTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM--AKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
45-1357 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 809.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 45 PVDDAGLLSFATFSWLTPVMIRSYKHTLTVDTLPPLSPYDSSDINAKRFQILWEEEIKRVGPE-----KASLGRVVWKFQ 119
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKPWllralNNSLGGRFWLGG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 120 RTRVLMDVVANIlcivmaalGPtVLIHQILQhitSISSGH-IGIGICLCLALFTTEFTKVLFWALAWAINYRTAIRLKVA 198
Cdd:PLN03130 308 FFKIGNDLSQFV--------GP-LLLNLLLE---SMQNGEpAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRST 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 199 LSTLIFENLLSfktLTHIS-----AGEVLNILSSDSYSLFEaalFCPLPATI---PILMVVCAVYAFFILGSTALVGISV 270
Cdd:PLN03130 376 LVAAVFRKSLR---LTHEGrkkftSGKITNLMTTDAEALQQ---ICQQLHTLwsaPFRIIIAMVLLYQQLGVASLIGSLM 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 271 YLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSAL 350
Cdd:PLN03130 450 LVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFI 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 351 APIVSTIAIVSTFTCHIFLKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRMKKILIAksppsyitqped 430
Cdd:PLN03130 530 LNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLA------------ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 431 pDTILLLANATLTWEQeinrksdpPKAQIQkrhvfkkqrpelyseqsrsdQGVASpeWQSGSPKSVLHNISFVVRKGKVL 510
Cdd:PLN03130 598 -EERVLLPNPPLEPGL--------PAISIK--------------------NGYFS--WDSKAERPTLSNINLDVPVGSLV 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 511 GICGNVGSGKSSLISALLGQM-QLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSL 589
Cdd:PLN03130 647 AIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLL 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 590 PYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC 669
Cdd:PLN03130 727 PGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 670 DEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRGLQFKDPEHiyNVAMVETLKESPAQRDEDAVLA-SGDEKDEGKEP 748
Cdd:PLN03130 807 DRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEEN--GEEEDDQTSSKPVANGNANNLKkDSSSKKKSKEG 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 749 ETeefvdtnapahQLIQTESPQEGIVTWKTYHTYIKASGGYLVsflVLCLFFLMMGSSAF---STWWLGIWLDRGsqvvc 825
Cdd:PLN03130 885 KS-----------VLIKQEERETGVVSWKVLERYKNALGGAWV---VMILFLCYVLTEVFrvsSSTWLSEWTDQG----- 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 826 asqnnktacnvdqTLQDTKHHMYQLVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRL 905
Cdd:PLN03130 946 -------------TPKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRI 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 906 MNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWF 985
Cdd:PLN03130 1013 INRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVY 1092
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 986 SHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTL-----SFSSISA 1060
Cdd:PLN03130 1093 AQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMqngraENQAAFA 1172
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1061 SSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI-----LTCVPEHTHPfkvgtcPKDWPSRGEITFKDYRMR 1135
Cdd:PLN03130 1173 STMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIdlpseAPLVIENNRP------PPGWPSSGSIKFEDVVLR 1246
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1136 YRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFV 1215
Cdd:PLN03130 1247 YRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFS 1326
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1216 GTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 1295
Cdd:PLN03130 1327 GTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1296 SKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFA 1357
Cdd:PLN03130 1407 VRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
45-1360 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 771.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 45 PVDDAGLLSFATFSWLTPVMIRSYKHTLTVDTLPPLSPYDSSDINAKRFQILWEEEIKRVGP-----EKASLGRVVWKFQ 119
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKPwllraLNNSLGGRFWLGG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 120 RTRVLMDVVANIlcivmaalGPTVLIHqILQHITSISSGHIGIGICLCLalftteFTKVLFWALAWAINY----RTAIRL 195
Cdd:PLN03232 308 IFKIGHDLSQFV--------GPVILSH-LLQSMQEGDPAWVGYVYAFLI------FFGVTFGVLCESQYFqnvgRVGFRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 196 KVALSTLIFENLLSfktLTH-----ISAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGISV 270
Cdd:PLN03232 373 RSTLVAAIFHKSLR---LTHearknFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLI 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 271 YLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSAL 350
Cdd:PLN03232 450 LFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFI 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 351 APIVSTIAIVSTFTCHIFLKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRMKKILI------AKSPPsy 424
Cdd:PLN03232 530 LNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLseerilAQNPP-- 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 425 iTQPEDPdtILLLANATLTWEqeinrksdppkaqiqkrhvfkkqrpelyseqsrsdqgvaspewqSGSPKSVLHNISFVV 504
Cdd:PLN03232 608 -LQPGAP--AISIKNGYFSWD--------------------------------------------SKTSKPTLSDINLEI 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 505 RKGKVLGICGNVGSGKSSLISALLGQM-QLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQ 583
Cdd:PLN03232 641 PVGSLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQ 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 584 KDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL 663
Cdd:PLN03232 721 HDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 664 QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRGLqfkDPEHIYNVAMVETLKESP-AQRD-EDAVLASGDE 741
Cdd:PLN03232 801 HFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKM---DATQEVNTNDENILKLGPtVTIDvSERNLGSTKQ 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 742 KDEGKEpeteefvdtnapahQLIQTESPQEGIVTWKTYHTYIKASGG-YLVSFLVLCLFFLMMGSSAFSTWwLGIWLDRg 820
Cdd:PLN03232 878 GKRGRS--------------VLVKQEERETGIISWNVLMRYNKAVGGlWVVMILLVCYLTTEVLRVSSSTW-LSIWTDQ- 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 821 sqvvcasqnnktacnvdQTLQDTKHHMYQLVYiasmvSVLMFGIIkGFTFTNT------TLMASSSLHNRVFNKIVRSPM 894
Cdd:PLN03232 942 -----------------STPKSYSPGFYIVVY-----ALLGFGQV-AVTFTNSfwlissSLHAAKRLHDAMLNSILRAPM 998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 895 SFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELK 974
Cdd:PLN03232 999 LFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVR 1078
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 975 QVENISRSPWFSHITSSIQGLGVIHAYdKKDDCISKF--KTLnDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVT 1052
Cdd:PLN03232 1079 RLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRMAKIngKSM-DNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAV 1156
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1053 LSF-----SSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI-----LTCVPEHTHPfkvgtcPKDWP 1122
Cdd:PLN03232 1157 LRNgnaenQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIdlpseATAIIENNRP------VSGWP 1230
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1123 SRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRT 1202
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1203 KLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 1282
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1283 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLL 1360
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
106-1362 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 717.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 106 PEKASLGRVVWKFQRTRVLMDVVANILCIVMAALGPTVLihQILQHITSISSGHIGIGICLCLALFTTEFTKVLFWALAW 185
Cdd:PTZ00243 229 PKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLL--KYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFY 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 186 AINYRTAIRLKVALSTLIFEN--LLSFKTLTH--ISAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILG 261
Cdd:PTZ00243 307 YISIRCGLQYRSALNALIFEKcfTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 262 STALVGISVYLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKag 341
Cdd:PTZ00243 387 WCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRD-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 342 yVQSGNSAL------APIVsTIAIVstFTCHIFLKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRMKKI 415
Cdd:PTZ00243 465 -VQLARVATsfvnnaTPTL-MIAVV--FTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTF 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 416 L---------IAKSPPSYITQPEDPDTILLLA---NATLT--------------------------WEQEINRKSDPP-- 455
Cdd:PTZ00243 541 LecdnatcstVQDMEEYWREQREHSTACQLAAvleNVDVTafvpvklprapkvktsllsralrmlcCEQCRPTKRHPSps 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 456 ---------KAQIQKRHVFKKQRPELYSEQSRSDQGVASPEWQSGS-----PKSVLHNISFVVRKGKVLGICGNVGSGKS 521
Cdd:PTZ00243 621 vvvedtdygSPSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDffelePKVLLRDVSVSVPRGKLTVVLGATGSGKS 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 522 SLISALLGQMQLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERG 601
Cdd:PTZ00243 701 TLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKG 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 602 VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEIC 681
Cdd:PTZ00243 781 VNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 682 EKGTHKELMEergryAKLIHNLRGLQFKDPEhiynvamvetLKESPAQRDEDAV-LASGDEKDEGKEPETEEFVD----- 755
Cdd:PTZ00243 861 FSGSSADFMR-----TSLYATLAAELKENKD----------SKEGDADAEVAEVdAAPGGAVDHEPPVAKQEGNAeggdg 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 756 --TNAPAHQLIQTESPQEGIVTWKTYHTYIKASGGYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVCASqnnkta 833
Cdd:PTZ00243 926 aaLDAAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMWSTRSFKLSAAT------ 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 834 cnvdqtlqdtkhhmYQLVYIAsMVSVLMFGIIKGFTFTNTTL-MASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKD 912
Cdd:PTZ00243 1000 --------------YLYVYLG-IVLLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRD 1064
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 913 MDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSI 992
Cdd:PTZ00243 1065 IDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEAL 1144
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 993 QGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALL----VTLSFSSISASSKGLSLS 1068
Cdd:PTZ00243 1145 QGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIgvigTMLRATSQEIGLVSLSLT 1224
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1069 YIIQLSGLLQVCVRTGTETQAKFTSAELLREYIL-----------------------------TCVPEHTHPfkVGTCPK 1119
Cdd:PTZ00243 1225 MAMQTTATLNWLVRQVATVEADMNSVERLLYYTDevphedmpeldeevdalerrtgmaadvtgTVVIEPASP--TSAAPH 1302
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1120 DWPSrGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED 1199
Cdd:PTZ00243 1303 PVQA-GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 1279
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1280 -RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAM 1358
Cdd:PTZ00243 1462 kKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHS 1541
|
....
gi 52138554 1359 LLAA 1362
Cdd:PTZ00243 1542 MVEA 1545
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-1343 |
6.75e-159 |
|
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: 517.16 E-value: 6.75e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 44 NPVDDAGLLSFATFSWLTPVMIRSYKHTLTVDTLPPLSPYDSSDINAKRFQILWEEEI---KRVGPEKASLGRV-VWKFQ 119
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELasaKKNPKLLNALRRCfFWRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 120 RTRVLMDVVANILCIVMAALGPTVLIHQILQHITSISSGHIGIGICLclaLFTTEFtkvLFWALAWAINYRTAIRLKVAL 199
Cdd:TIGR01271 84 FYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCL---LFIVRT---LLLHPAIFGLHHLGMQMRIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 200 STLIFENLL--SFKTLTHISAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGISVYLIFIPI 277
Cdd:TIGR01271 158 FSLIYKKTLklSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 278 QMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTI 357
Cdd:TIGR01271 238 QACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 358 AIVSTFTCHIFLK----RKLTAPVAFSVIAMFNVMKfsiaILPFSVKAVAEASVSLRRMKKILIA---KSPPSYITQPEd 430
Cdd:TIGR01271 318 VVFLSVVPYALIKgiilRRIFTTISYCIVLRMTVTR----QFPGAIQTWYDSLGAITKIQDFLCKeeyKTLEYNLTTTE- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 431 pdtiLLLANATLTWEQEINRKSDPPKAQIQKRhvfkkqrpelysEQSRSDQGVASPEWQS-GSPksVLHNISFVVRKGKV 509
Cdd:TIGR01271 393 ----VEMVNVTASWDEGIGELFEKIKQNNKAR------------KQPNGDDGLFFSNFSLyVTP--VLKNISFKLEKGQL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 510 LGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSL 589
Cdd:TIGR01271 455 LAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 590 PYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC 669
Cdd:TIGR01271 535 PEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKA 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 670 DEVILLEDGEICEKGTHKELMEERGRYAKLIHNL------------------------------------RGLQFKDPEH 713
Cdd:TIGR01271 615 DKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLeafdnfsaerrnsiltetlrrvsidgdstvfsgpetIKQSFKQPPP 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 714 IYNVAMVETLKESP------------------AQRDEDAVLASGD-------EKDEGKEPETEEFVDTNAPAHQ------ 762
Cdd:TIGR01271 695 EFAEKRKQSIILNPiasarkfsfvqmgpqkaqATTIEDAVREPSErkfslvpEDEQGEESLPRGNQYHHGLQHQaqrrqs 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 763 ---LIQTESPQEGIV--------------------------------------------------------------TWK 777
Cdd:TIGR01271 775 vlqLMTHSNRGENRReqlqtsfrkkssitqqnelaseldiysrrlskdsvyeiseeineedlkecfaderenvfettTWN 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 778 TYHTYIKASGGyLVSFLVLCLFFLMMGSSAFstwWLGIWLDRGSQVVCASQNNKTACNVDQTLQ------DTKHHMYQLV 851
Cdd:TIGR01271 855 TYLRYITTNRN-LVFVLIFCLVIFLAEVAAS---LLGLWLITDNPSAPNYVDQQHANASSPDVQkpviitPTSAYYIFYI 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 852 YIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQF 931
Cdd:TIGR01271 931 YVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLT 1010
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 932 FMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKF 1011
Cdd:TIGR01271 1011 LIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLF 1090
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1012 -KTLNDENSSHLLYFNcALRWFALRMDILMnIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAK 1090
Cdd:TIGR01271 1091 hKALNLHTANWFLYLS-TLRWFQMRIDIIF-VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGL 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1091 FTSAELLREYIlTCVPEHTHPFKVGT--------------CPKDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQT 1156
Cdd:TIGR01271 1169 MRSVSRVFKFI-DLPQEEPRPSGGGGkyqlstvlvienphAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQR 1247
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1157 VGIVGRTGSGKSSLGMALFRLVEpASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHV 1236
Cdd:TIGR01271 1248 VGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKV 1326
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1237 LERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVL 1316
Cdd:TIGR01271 1327 AEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI 1406
|
1450 1460
....*....|....*....|....*..
gi 52138554 1317 TIAHRLNTVLNCDLVLVMENGKVIEFD 1343
Cdd:TIGR01271 1407 LSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
788-1101 |
3.58e-144 |
|
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: 440.85 E-value: 3.58e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 788 GYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVcASQNNKTACNVDQTLQDTKHHMYQLVYIASMVSVLMFGIIKG 867
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNT-TNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 868 FTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPV 947
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 948 VLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNC 1027
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1028 ALRWFALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 1101
Cdd:cd18599 240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
125-412 |
1.86e-127 |
|
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: 395.39 E-value: 1.86e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 125 MDVVANILCIVMAALGPTVLIHQILQHITSiSSGHIGIGICLCLALFTTEFTKVLFWALAWAINYRTAIRLKVALSTLIF 204
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLED-SDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 205 ENLLSFKTLTHISAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGISVYLIFIPIQMFMAKL 284
Cdd:cd18592 80 KKILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 285 NSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFT 364
Cdd:cd18592 160 TGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 52138554 365 CHIFLKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18592 240 AHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1125-1345 |
2.03e-126 |
|
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: 389.93 E-value: 2.03e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 1204
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 1284
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1285 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP 1345
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
484-679 |
2.09e-105 |
|
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: 332.13 E-value: 2.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 484 ASPEWQSGS--PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIFHGNVREN 561
Cdd:cd03250 6 ASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 641
Cdd:cd03250 86 ILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 52138554 642 VFEECIKKTLK-GKTVVLVTHQLQFLESCDEVILLEDGE 679
Cdd:cd03250 166 IFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
850-1365 |
1.63e-104 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 344.07 E-value: 1.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 850 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQ 929
Cdd:COG1132 65 LLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 930 QFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCIS 1009
Cdd:COG1132 145 SVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1010 KFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSFSSisassKGLS-------LSYIIQLSGLLQVCVR 1082
Cdd:COG1132 225 RFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLS-----GSLTvgdlvafILYLLRLFGPLRQLAN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1083 TGTETQAKFTSAELLREYILTCV----PEHTHPFKvgtcpkdwPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVG 1158
Cdd:COG1132 300 VLNQLQRALASAERIFELLDEPPeipdPPGAVPLP--------PVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1159 IVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHV 1236
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGrpDATDEEVEEA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1237 LERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVL 1316
Cdd:COG1132 450 AKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTI 529
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 52138554 1317 TIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKpDSAFAMLLAAEVG 1365
Cdd:COG1132 530 VIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQFG 577
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1121-1345 |
3.05e-88 |
|
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: 285.08 E-value: 3.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1121 WPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL 1200
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1201 RTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLertfmrdtimklpeklqaEVTENGENFSVGERQLLCMARALLR 1280
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1281 NSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP 1345
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
850-1351 |
2.40e-82 |
|
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: 285.96 E-value: 2.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 850 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSkDMDELDVRLPFHAENFLQ 929
Cdd:COG2274 200 IGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 930 QFFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLRIFHRGVQ-ELKQVENISRSpwFSHITSSIQGLGVIHAYDkkddC 1007
Cdd:COG2274 279 DLLFVLIFLIVLFFYsPPLALVVLLLIPLYVLLGLLFQPRLRRlSREESEASAKR--QSLLVETLRGIETIKALG----A 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1008 ISKFKTLNDENSSHLLYFNCALRWFALRMDILMN--------IVTFVVALLV-----TLSFSSISASSKGLSLSYIIQLS 1074
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGllqqlatvALLWLGAYLVidgqlTLGQLIAFNILSGRFLAPVAQLI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1075 GLLQvcvrtgtETQAKFTSAELLREyILTCVPEHTHPFKVGTCPKDwpsRGEITFKDYRMRYRDNTPLVLDGLNLNIQSG 1154
Cdd:COG2274 433 GLLQ-------RFQDAKIALERLDD-ILDLPPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDNISLTIKPG 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1155 QTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL---DPlgSHTDE 1231
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1232 MLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK 1311
Cdd:COG2274 580 EIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK 659
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 52138554 1312 SCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:COG2274 660 GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
792-1101 |
5.01e-79 |
|
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: 262.44 E-value: 5.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 792 SFLVLCLFFLMMGSSAFSTWWLGIWLDRgsqvvcasqnnktacNVDQTLQDTKHHMYqLVYIASMVSVLMFGIIKGFTFT 871
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD---------------WSSSPNSSSGYYLG-VYAALLVLASVLLVLLRWLLFV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 872 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 951
Cdd:cd18580 65 LAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 952 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 1031
Cdd:cd18580 145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1032 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 1101
Cdd:cd18580 225 LGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1125-1363 |
7.46e-76 |
|
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: 252.14 E-value: 7.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 1204
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 1284
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1285 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAE 1363
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
107-710 |
3.49e-75 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 261.64 E-value: 3.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 107 EKASLGRVVWKF---QRTRVLMDVVANILCIVMAALGPTVLIHQILQHITSISSGHIGIGICLCLALFtteFTKVLFWAL 183
Cdd:COG1132 4 SPRKLLRRLLRYlrpYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLA---LLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 184 AWAINYRTAIRLKVALSTLIFENL--LSFKTLTHISAGEVLNILSSDSYSLFEAALFCPLPA-TIPILMVVCAVYAFFI- 259
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLlrLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLvRSVVTLIGALVVLFVId 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 260 --LGSTALVGISVYLIFIPIqmFMAKLNSTFRRSAISVtDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLL 337
Cdd:COG1132 161 wrLALIVLLVLPLLLLVLRL--FGRRLRKLFRRVQEAL-AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 338 EKAGYVQSGNSALAPIVSTIAIVSTFT--CHIFLKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRMKKI 415
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVLLvgGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 416 LIAKSPpsyITQPEDPDTIlllanatltweqeinrksDPPKAQIQKRHV-FKkqrpelYSEQsrsdqgvaspewqsgspK 494
Cdd:COG1132 318 LDEPPE---IPDPPGAVPL------------------PPVRGEIEFENVsFS------YPGD-----------------R 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PL-------AYVSQQAWIFHGNVREN 561
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdlTLeslrrqiGVVPQDTFLFSGTIREN 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGK 640
Cdd:COG1132 434 IRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 641 HVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHnlrgLQFKD 710
Cdd:COG1132 514 LIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR----LQFGE 578
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
131-412 |
4.05e-72 |
|
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: 242.78 E-value: 4.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 131 ILCIVMAALGPtVLIHQILQHITSISSGHIGIGICLCLALFTTEFTKVLFWALAWAINYRTAIRLKVALSTLIFE--NLL 208
Cdd:cd18579 7 LLEDLLSLAQP-LLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRkaLRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 209 SFKTLTHISAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGISVYLIFIPIQMFMAKLNSTF 288
Cdd:cd18579 86 SSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLISKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 289 RRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCHIF 368
Cdd:cd18579 166 RKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFATYVL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 52138554 369 LKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18579 246 LGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
879-1351 |
8.01e-70 |
|
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: 245.44 E-value: 8.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 879 SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlPFHAeNFLQQFFMVVFI-LVIMAAVFP------VVLVV 951
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALD---GYFA-RYLPQLFLAALVpLLILVAVFPldwlsgLILLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 952 LAGLAVIFLILLRIFHRGVQElKQVENISR-SpwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDE------------- 1017
Cdd:COG4988 167 TAPLIPLFMILVGKGAAKASR-RQWRALARlS---GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrtmkvlrvaf 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1018 NSShllyfncalrwFALrmDILMNIVTFVVALLVtlsfssisasskGLSLSYI-IQLSGLLQVCV---------RT-GTE 1086
Cdd:COG4988 243 LSS-----------AVL--EFFASLSIALVAVYI------------GFRLLGGsLTLFAALFVLLlapefflplRDlGSF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1087 TQAKF---TSAELLREYILTCVPEHTHpfkvGTCPKDWPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRT 1163
Cdd:COG4988 298 YHARAngiAAAEKIFALLDAPEPAAPA----GTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1164 GSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTF 1241
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR-LGRPdaSDEELEAALEAAG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1242 MRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR 1321
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
490 500 510
....*....|....*....|....*....|
gi 52138554 1322 LNTVLNCDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1125-1351 |
1.04e-68 |
|
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: 230.58 E-value: 1.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 1204
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 1282
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIR-LGRPnaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1283 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
792-1100 |
1.71e-68 |
|
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: 232.75 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 792 SFLVLCLFFLMMGSSAFSTWWLGIWLDrgsqvvcasqnnKTACNVDQTLQDTkhHMYQLVYIASMVSVLMFGIIKGFTFT 871
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSD------------DPALNGTQDTEQR--DYRLGVYGALGLGQAIFVFLGSLALA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 872 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 951
Cdd:cd18603 67 LGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 952 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 1031
Cdd:cd18603 147 IIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1032 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 1100
Cdd:cd18603 227 LAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
851-1352 |
3.08e-66 |
|
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: 235.43 E-value: 3.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 851 VYIASmVSVLMFGIIKGFT------FT-NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD-----V 918
Cdd:COG4987 54 LFVPI-VGVRAFAIGRTVFrylerlVShDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 919 RLPFHAenflqqFFMVVFILVIMAAVF--PVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLG 996
Cdd:COG4987 133 LLPLLV------ALLVILAAVAFLAFFspALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 997 VIHAYDKKDDCISKFKTLNDENSSHLLyfncALRWFALRMDILMNIVTFVVALLVtLSFSSISASSKGLSLSYII----- 1071
Cdd:COG4987 207 ELAAYGALDRALARLDAAEARLAAAQR----RLARLSALAQALLQLAAGLAVVAV-LWLAAPLVAAGALSGPLLAllvla 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1072 ------QLSGLLQVCVRTGtETQAkftSAELLREyILTCVPEHTHPfkvgTCPKDWPSRGEITFKDYRMRYRDNTPLVLD 1145
Cdd:COG4987 282 alalfeALAPLPAAAQHLG-RVRA---AARRLNE-LLDAPPAVTEP----AEPAPAPGGPSLELEDVSFRYPGAGRPVLD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1146 GLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL--- 1222
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrla 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1223 DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV 1302
Cdd:COG4987 433 RP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 52138554 1303 QSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 1352
Cdd:COG4987 511 LADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
793-1100 |
8.37e-66 |
|
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: 224.66 E-value: 8.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 793 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVvcaSQNNktacnvdqtlqdtkhhmYQLVYIASMVSVLMFGIIKGFTFTN 872
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDFFGL---SQGF-----------------YIGIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 873 TTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVL 952
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 953 AGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISK-FKTLNDENSSHLLYFNCAlRW 1031
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKnEKLIDNMNRAYFLTIANQ-RW 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1032 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 1100
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
788-1100 |
2.55e-62 |
|
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: 215.65 E-value: 2.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 788 GYLVSFLVLCLFFLMMGSSAFSTWWLGIW--LDRGSQVVCASQNNKTACNVDQTLQDTKHHMYqlVYIASMVSVLMFGII 865
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLG--IYAGLTAATFVFGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 866 KGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVF 945
Cdd:cd18601 79 RSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 946 PVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYF 1025
Cdd:cd18601 159 PWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1026 NCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 1100
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
793-1101 |
1.39e-61 |
|
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: 212.71 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 793 FLVLCLFFLMMGSSAFSTWWLGIWldrgsqvvcASQNNKTAcnvdqTLQDTKHHM--YQLVYIASMVSVLMFGIIKGFTF 870
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIW---------ASAYETSS-----ALPPSEVSVlyYLGIYALISLLSVLLGTLRYLLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 871 TNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLV 950
Cdd:cd18604 68 FFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 951 VLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALR 1030
Cdd:cd18604 148 PAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1031 WFALRMDILMNIVTFVVALLVTLSFSSISASSkGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 1101
Cdd:cd18604 228 WLSVRIDLLGALFSFATAALLVYGPGIDAGLA-GFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1127-1341 |
3.69e-61 |
|
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: 209.32 E-value: 3.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRY--RDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 1204
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 1282
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1283 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 1341
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1127-1338 |
4.59e-61 |
|
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: 206.47 E-value: 4.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIIL 1286
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1287 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGK 1338
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1127-1351 |
6.40e-61 |
|
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: 208.62 E-value: 6.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVGTVRYNL---DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSK 1283
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1284 IILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
71-702 |
7.76e-61 |
|
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: 222.79 E-value: 7.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 71 TLTVDTLPPLSPYDSSDINAKRFQILWeeeiKRVGPEKASLGRVVwkfqrtrvlmdvVANILCIVMAALGP--------T 142
Cdd:COG2274 122 TGVALLLEPTPEFDKRGEKPFGLRWFL----RLLRRYRRLLLQVL------------LASLLINLLALATPlftqvvidR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 143 VLIHQILQHITSISsghIGIGIclcLALFTTeftkVLFWALAWAINyRTAIRLKVALSTLIFENLLSFKT--LTHISAGE 220
Cdd:COG2274 186 VLPNQDLSTLWVLA---IGLLL---ALLFEG----LLRLLRSYLLL-RLGQRIDLRLSSRFFRHLLRLPLsfFESRSVGD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 221 VLN----------ILSSDSYSLFEAALFcplpatIPILMVVCAVY----AFFILGSTALVGISVYLIFIPIQmfmAKLNS 286
Cdd:COG2274 255 LASrfrdvesireFLTGSLLTALLDLLF------VLIFLIVLFFYspplALVVLLLIPLYVLLGLLFQPRLR---RLSRE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 287 TFRRSAisvtdKRVQTMNEFLTCIKLIKMYA--------WEESFINTIHDIRKREKKLLekagYVQSGNSALAPIVSTIA 358
Cdd:COG2274 326 ESEASA-----KRQSLLVETLRGIETIKALGaesrfrrrWENLLAKYLNARFKLRRLSN----LLSTLSGLLQQLATVAL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 359 IVstFTCHIFLKRKLTAP--VAFSVIA-MFN--VMKFSIAILPFsvkavAEASVSLRRMKKILiaksppsyiTQPEDPDt 433
Cdd:COG2274 397 LW--LGAYLVIDGQLTLGqlIAFNILSgRFLapVAQLIGLLQRF-----QDAKIALERLDDIL---------DLPPERE- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 434 illlanatltwEQEINRKSDPPKAQIQKRHV-FKkqrpelYSEQSrsdqgvaspewqsgspKSVLHNISFVVRKGKVLGI 512
Cdd:COG2274 460 -----------EGRSKLSLPRLKGDIELENVsFR------YPGDS----------------PPVLDNISLTIKPGERVAI 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 513 CGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVH 578
Cdd:COG2274 507 VGRSGSGKSTLLKLLLGLYEPTSGRILIDGiDLrqidpaslrrqiGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAAR 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 579 VCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFeECIKKTLKGKTVVL 658
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL-ENLRRLLKGRTVII 665
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 52138554 659 VTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 702
Cdd:COG2274 666 IAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
836-1341 |
2.04e-58 |
|
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: 212.27 E-value: 2.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 836 VDQTLQDTKHHMyqLVYIASMVSVLMfgIIKGFT-FTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 908
Cdd:TIGR02203 41 LDDGFGGRDRSV--LWWVPLVVIGLA--VLRGICsFVSTYLLSWVSnkvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 909 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIM-------AAVFPVVLVVLAGLAVIFLILLRIFHRGVQELK-QVENIs 980
Cdd:TIGR02203 117 ITFDSEQVASAATDAFIVLVRETLTVIGLFIVLlyyswqlTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMgQVTTV- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 981 rspwfshITSSIQGLGVIHAYDKKDDCISKFKTLNDENsshllyfncalRWFALRMD----ILMNIVTFVVA------LL 1050
Cdd:TIGR02203 196 -------AEETLQGYRVVKLFGGQAYETRRFDAVSNRN-----------RRLAMKMTsagsISSPITQLIASlalavvLF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1051 VTLSFSSISASSKGLSLSYIIQLsGLLQVCVRTGTETQAKFTSAELLREYILTCVPEHTHPFKvGTCPKDwPSRGEITFK 1130
Cdd:TIGR02203 258 IALFQAQAGSLTAGDFTAFITAM-IALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT-GTRAIE-RARGDVEFR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1131 DYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQD 1210
Cdd:TIGR02203 335 NVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1211 PVLFVGTVRYNL--DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLD 1288
Cdd:TIGR02203 415 VVLFNDTIANNIayGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1289 EATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 1341
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
488-678 |
7.32e-58 |
|
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: 199.09 E-value: 7.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVN-----------------GPLAYVSQQ 550
Cdd:cd03290 10 WGSGLA--TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 551 AWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 52138554 631 LSAVDAHVGKHVFEECIKKTLKG--KTVVLVTHQLQFLESCDEVILLEDG 678
Cdd:cd03290 168 FSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1127-1341 |
6.57e-57 |
|
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: 197.07 E-value: 6.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVGTVRYNLdPLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 1284
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1285 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 1341
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1123-1341 |
9.18e-56 |
|
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: 205.44 E-value: 9.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1123 SRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRT 1202
Cdd:COG5265 354 GGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1203 KLTMIPQDPVLFVGTVRYNL---DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 1279
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1280 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 1341
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
496-694 |
2.31e-55 |
|
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: 203.07 E-value: 2.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHGNVRENI 562
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRENL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 641
Cdd:COG4988 432 RLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 642 VFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 694
Cdd:COG4988 512 ILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
131-412 |
2.91e-55 |
|
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: 195.02 E-value: 2.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 131 ILCIVMAAL--GPTVLIHQILQHITSISSGHIGIGICLCLALFTTEFTKVLFWALAWAINYRTAIRLKVALSTLIFENLL 208
Cdd:cd18596 4 LLAVLSSVLsfAPPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 209 SFKTLTHI---------------------SAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVG 267
Cdd:cd18596 84 RRRDKSGSsksseskkkdkeededekssaSVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 268 ISVYLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGN 347
Cdd:cd18596 164 LAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLL 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 348 SALAPIVSTIAIVSTFTCHIFL-KRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18596 244 SLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
491-700 |
1.76e-53 |
|
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: 188.91 E-value: 1.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNH 570
Cdd:cd03291 49 GAP--VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 571 QRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKT 650
Cdd:cd03291 127 YRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 52138554 651 LKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 700
Cdd:cd03291 207 MANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
792-1101 |
6.35e-53 |
|
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: 188.12 E-value: 6.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 792 SFLVLCLFFLMMGSSAFSTWWLGIWLdrgsqvvcasqnNKTACNVDQTLQDTKHhMYQLVYIASMVSVLMFGIIKGFTFT 871
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWV------------SHSNNSFFNFINDSFN-FFLTVYGFLAGLNSLFTLLRAFLFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 872 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 951
Cdd:cd18605 68 YGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 952 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDdcisKFktlNDENSSHLLYFNCAL-- 1029
Cdd:cd18605 148 LLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQE----RF---LKEYLEKLENNQRAQla 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1030 -----RWFALRMDILMNIVTFVVALLVTLSFSSISASSK---GLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 1101
Cdd:cd18605 221 sqaasQWLSIRLQLLGVLIVTFVALTAVVQHFFGLSIDAgliGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
190-699 |
6.72e-53 |
|
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: 196.14 E-value: 6.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 190 RTAIRLKVALSTLIFENL--LSFKTLTHISAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFI----LGST 263
Cdd:COG4987 81 DATLRLLADLRVRLYRRLepLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFfspaLALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 264 ALVGISVYLIFIPIqMFMAKLNSTFRRSAISVTDKRVQTMnEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYV 343
Cdd:COG4987 161 LALGLLLAGLLLPL-LAARLGRRAGRRLAAARAALRARLT-DLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 344 QSGNSALAPIVSTIAIVST--FTCHIFLKRKLTAP----VAFSVIAMFNVmkfsIAILPFSVKAVAEASVSLRRMKKILI 417
Cdd:COG4987 239 SALAQALLQLAAGLAVVAVlwLAAPLVAAGALSGPllalLVLAALALFEA----LAPLPAAAQHLGRVRAAARRLNELLD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 418 AK----SPPSYITQPEDPDtiLLLANATLTWEqeinrksdppkaqiqkrhvfkkqrpelyseqsrsdqgvaspewqsGSP 493
Cdd:COG4987 315 APpavtEPAEPAPAPGGPS--LELEDVSFRYP---------------------------------------------GAG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRE 560
Cdd:COG4987 348 RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvDLrdldeddlrrriAVVPQRPHLFDTTLRE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGekynhqRYQHT----VHVC---GLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSA 633
Cdd:COG4987 428 NLRLA------RPDATdeelWAALervGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 634 VDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 699
Cdd:COG4987 502 LDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1125-1348 |
2.35e-51 |
|
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: 182.75 E-value: 2.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEpASGTIIIDEVDICTVGLEDLRTKL 1204
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 1284
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1285 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVL 1348
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1127-1341 |
1.73e-50 |
|
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: 178.83 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVGTVRYNLdplgSHTDEM--LWHVLERTFM---RDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRN 1281
Cdd:cd03252 81 VLQENVLFNRSIRDNI----ALADPGmsMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1282 SKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 1341
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
886-1362 |
2.91e-50 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 188.63 E-value: 2.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 886 FNKIVRSPMSFFDTTPTGRLMNRFSKDMDEL-DVRLPFHAENFLQqfFMVVFILVIMAAVFPVVL-VVLAGLAVIFLILL 963
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTLLRGTDALfGLWLEFMREHLAT--LVALVVLLPLALFMNWRLsLVLVVLGIVYTLIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 964 RIFHRGVQELK-QVENiSRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLndenSSHLLYF-NCALRWFAL-----RM 1036
Cdd:PRK13657 174 TLVMRKTKDGQaAVEE-HYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDI----ADNLLAAqMPVLSWWALasvlnRA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1037 D--ILMNIVTFVVALLVTlsfssisassKG-LSLSYIIQLSGLLQVCVR-----TGTETQAkFTSAELLREY--ILTCVP 1106
Cdd:PRK13657 249 AstITMLAILVLGAALVQ----------KGqLRVGEVVAFVGFATLLIGrldqvVAFINQV-FMAAPKLEEFfeVEDAVP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1107 EHTHPFKVGTCPKdwpSRGEITFKDYRMRYrDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTII 1186
Cdd:PRK13657 318 DVRDPPGAIDLGR---VKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1187 IDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENF 1264
Cdd:PRK13657 394 IDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-VGrpDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1265 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE--- 1341
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgs 552
|
490 500
....*....|....*....|.
gi 52138554 1342 FDkpEVLAEkpDSAFAMLLAA 1362
Cdd:PRK13657 553 FD--ELVAR--GGRFAALLRA 569
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
793-1100 |
2.36e-49 |
|
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: 177.80 E-value: 2.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 793 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVCASQNNKtacnvDQTLQDTKHHMYQLVYIA-SMVSVLMFGIIKGFTFT 871
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNIT-----SSSLEDDEVSYYISVYAGlSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 872 nTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 951
Cdd:cd18602 77 -AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 952 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 1031
Cdd:cd18602 156 LIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1032 FALRMDILMNIVTFVVALLVTLSFSSISASSK--GLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 1100
Cdd:cd18602 236 LGIRLDYLGAVIVFLAALSSLTAALAGYISPSlvGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
127-412 |
6.65e-49 |
|
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: 176.10 E-value: 6.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 127 VVANILCIVMAALGPtVLIHQILQHITS----ISSGHIGIGICLCLALFTTEFTKVLFWALAWAINYRTAIRLKVALSTL 202
Cdd:cd18597 3 GLLKLLADVLQVLSP-LLLKYLINFVEDaylgGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 203 IFEN--LLSFKTLTHISAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGISVYLIFIPIQMF 280
Cdd:cd18597 82 IYRKslRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 281 MAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIV 360
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 52138554 361 STFTCHIFLKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18597 242 LSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
851-1359 |
1.70e-48 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 185.70 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 851 VYIASMVSVL--MFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFL 928
Cdd:TIGR00958 204 IFFMCLLSIAssVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 929 QQFFMVVFILVIMAAVFP-VVLVVLAGLAVIFLI--LLRIFHRGVQELKQvENISRSPWFS-HITSSIQ--------GLG 996
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPrLTMVTLINLPLVFLAekVFGKRYQLLSEELQ-EAVAKANQVAeEALSGMRtvrsfaaeEGE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 997 VIHAYDKKDDCISKFKTlndENSSHLLYFncalrWFALRMDILMnivtFVVALLVTLSFSSISASSKGLSLSYII---QL 1073
Cdd:TIGR00958 363 ASRFKEALEETLQLNKR---KALAYAGYL-----WTTSVLGMLI----QVLVLYYGGQLVLTGKVSSGNLVSFLLyqeQL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1074 SGLLQVCVRTGTETQAKFTSAELLREYIlTCVPEHTHPfkVGTCPKdwPSRGEITFKDYRMRY--RDNTPlVLDGLNLNI 1151
Cdd:TIGR00958 431 GEAVRVLSYVYSGMMQAVGASEKVFEYL-DRKPNIPLT--GTLAPL--NLEGLIEFQDVSFSYpnRPDVP-VLKGLTFTL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1152 QSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLD-PLGSHTD 1230
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPD 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1231 EMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKeaF 1310
Cdd:TIGR00958 585 EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--R 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 52138554 1311 KSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAML 1359
Cdd:TIGR00958 663 ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1125-1340 |
1.48e-47 |
|
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: 169.69 E-value: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 1204
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 1282
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNIT-LGapLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1283 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVI 1340
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
163-412 |
4.26e-47 |
|
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: 170.86 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 163 GICLCLALFTTEFTKVLFWALawainyRTAIRLKVALSTLIFENLL--SFKTLTHISAGEVLNILSSDSYSLFEAALFCP 240
Cdd:cd18593 45 GVSLCSFLFIITHHPYFFGMQ------RIGMRLRVACSSLIYRKALrlSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 241 LPATIPILMVVCAVYAFFILGSTALVGISVYLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEE 320
Cdd:cd18593 119 YLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 321 SFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCHIFLKRKLTAPVAFSVIAMFNVMKFSIAI-LPFSV 399
Cdd:cd18593 199 AFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLfFPFAI 278
|
250
....*....|...
gi 52138554 400 KAVAEASVSLRRM 412
Cdd:cd18593 279 QFGSELSVSIRRI 291
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
161-411 |
2.37e-46 |
|
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: 168.58 E-value: 2.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 161 GIGICLCLALFTteftkvLFWALAWAINYRTAIRLKVALSTLIFENLLSFKT--LTHISAGEVLNILSSDSYSLFEAALF 238
Cdd:cd18594 42 ALGLSLCAFLRV------LLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSsaLSKITTGHIVNLLSNDVQKFDEVLVY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 239 CPLPATIPILMVVCAVYAFFILGSTALVGISVYLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAW 318
Cdd:cd18594 116 LHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTW 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 319 EESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCHIFLKRKLTAPVAFSVIAMFNVMKFSIAI-LPF 397
Cdd:cd18594 196 EESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTARKVFTVISLLNALRMTITRfFPE 275
|
250
....*....|....
gi 52138554 398 SVKAVAEASVSLRR 411
Cdd:cd18594 276 SIQTLSESRVSLKR 289
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
127-412 |
3.80e-46 |
|
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: 168.03 E-value: 3.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 127 VVANILCIVMAALGPTVLihQILQHITSISSGHIGIGICLCLALFTTEFTKVLFWALAWAINYRTAIRLKVALSTLIFEn 206
Cdd:cd18595 3 ALLKLLSDILLFASPQLL--KLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 207 llsfKTLThIS--------AGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGISVYLIFIPIQ 278
Cdd:cd18595 80 ----KALR-LSnsarkkstVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 279 MFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIA 358
Cdd:cd18595 155 AVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 359 IVSTFTCHIFL--KRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18595 235 SLATFATYVLSdpDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
491-699 |
4.04e-46 |
|
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: 165.87 E-value: 4.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGN 557
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:cd03251 92 VAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 637 hVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 699
Cdd:cd03251 172 -ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
494-694 |
3.41e-43 |
|
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: 157.39 E-value: 3.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRE 560
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYNHQ-RYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:cd03254 96 NIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 640 KHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 694
Cdd:cd03254 176 KLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
881-1341 |
1.16e-42 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 166.05 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 881 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMD---ELDVRLpfhAENFLQQFFMVVFILVIM-----------AAVFP 946
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEvirDLYVTV---VATVLRSAALIGAMLVAMfsldwrmalvaIMIFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 947 VVLVVLAglaviflillrIFHRGVQELkqVENIsRSpWFSHITS----SIQGLGVIHAYDKKddciSKF-KTLNDENSSH 1021
Cdd:PRK10790 177 AVLVVMV-----------IYQRYSTPI--VRRV-RA-YLADINDgfneVINGMSVIQQFRQQ----ARFgERMGEASRSH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1022 LLyfncaLRWFALRMD--ILMNIVTFVVALLVTlsfssisasskGLSLSYIIQLSGLLQVCVRTG--------------- 1084
Cdd:PRK10790 238 YM-----ARMQTLRLDgfLLRPLLSLFSALILC-----------GLLMLFGFSASGTIEVGVLYAfisylgrlnepliel 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1085 TETQAKFTSAELLREYILTCVPEHTHPFKVGTCPKdwpSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTG 1164
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPL---QSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1165 SGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLdPLGSH-TDEMLWHVLERTFMR 1243
Cdd:PRK10790 378 SGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRDiSEEQVWQALETVQLA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1244 DTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLN 1323
Cdd:PRK10790 457 ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLS 536
|
490
....*....|....*...
gi 52138554 1324 TVLNCDLVLVMENGKVIE 1341
Cdd:PRK10790 537 TIVEADTILVLHRGQAVE 554
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
496-702 |
1.50e-42 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 155.78 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHGNVRENI 562
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFGEKYNHQryQHTVHVCGL---QKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:cd03249 98 RYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 640 KHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 702
Cdd:cd03249 176 KLV-QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
490-679 |
1.83e-42 |
|
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: 152.92 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 490 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHG 556
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvDLrdldleslrkniAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENILfgekynhqryqhtvhvcglqkdlnslpygdlteigergvnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:cd03228 91 TIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52138554 637 HvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGE 679
Cdd:cd03228 130 E-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
850-1322 |
7.79e-42 |
|
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: 162.14 E-value: 7.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 850 LVYIASMVSVLMFGIIKGF-------TFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD---VR 919
Cdd:TIGR02868 50 LYLSVAAVAVRAFGIGRAVfrylerlVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyVR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 920 --LPfhaenflqqffMVVFILVIMAAV-------FPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITS 990
Cdd:TIGR02868 130 viVP-----------AGVALVVGAAAVaaiavlsVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 991 SIQGLGVIHAYDKKDDCISKFKtlnDENSSHLLYFNCALRWFALR--MDILMNIVTfVVALLVTLSFSSISASSKGLSLS 1068
Cdd:TIGR02868 199 ALDGAAELVASGALPAALAQVE---EADRELTRAERRAAAATALGaaLTLLAAGLA-VLGALWAGGPAVADGRLAPVTLA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1069 YIIqlsgLLQVCVrtgTETQAKFTSA-ELLREYI-----LTCVPEHTHPFKVGTCPKDWPSRGE---ITFKDYRMRYRDN 1139
Cdd:TIGR02868 275 VLV----LLPLAA---FEAFAALPAAaQQLTRVRaaaerIVEVLDAAGPVAEGSAPAAGAVGLGkptLELRDLSAGYPGA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1140 TPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVR 1219
Cdd:TIGR02868 348 PP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 YNLD-PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKT 1298
Cdd:TIGR02868 427 ENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
490 500
....*....|....*....|....
gi 52138554 1299 DTLVQSTIKEAFKSCTVLTIAHRL 1322
Cdd:TIGR02868 507 ADELLEDLLAALSGRTVVLITHHL 530
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
496-675 |
2.02e-41 |
|
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: 160.92 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRENI 562
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvPLadadadswrdqiAWVPQHPFLFAGTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFGEKY-NHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 641
Cdd:TIGR02857 417 RLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
170 180 190
....*....|....*....|....*....|....
gi 52138554 642 VFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILL 675
Cdd:TIGR02857 497 VLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
491-680 |
3.20e-41 |
|
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: 151.20 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P------LAYVSQQAWIFHGN 557
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldPadlrrnIGYVPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILFGEKY-NHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:cd03245 94 LRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 637 HVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:cd03245 174 NSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1122-1359 |
4.59e-41 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 160.95 E-value: 4.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1122 PSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 1201
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TKLTMIPQDPVLFVGTVRYNLD--PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 1279
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1280 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKpDSAFAML 1359
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYAQL 575
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
496-699 |
5.39e-41 |
|
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: 151.48 E-value: 5.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENI 562
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDaHVGKH 641
Cdd:cd03252 97 ALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 642 VFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 699
Cdd:cd03252 176 AIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
877-1334 |
6.55e-41 |
|
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: 159.37 E-value: 6.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 877 ASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVrlpfHAENFLQQFFMVVFI-LVIMAAVFP------VVL 949
Cdd:TIGR02857 75 VKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDG----YFARYLPQLVLAVIVpLAILAAVFPqdwisgLIL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 950 VVLAGLAVIFLILLrifhrgvqeLKQVENISRSPWFS------HITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLL 1023
Cdd:TIGR02857 151 LLTAPLIPIFMILI---------GWAAQAAARKQWAAlsrlsgHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTM 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1024 YfncalrwfALRMDILMnivTFVVALLVTLSFSSISASSkGLSLSY--IIQLSGLL-------------QVCVRTGTETQ 1088
Cdd:TIGR02857 222 R--------VLRIAFLS---SAVLELFATLSVALVAVYI-GFRLLAgdLDLATGLFvlllapefylplrQLGAQYHARAD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1089 AKFTSAELLREYILTCVPEHthpfkvGTCPKDWPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKS 1168
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLA------GKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKS 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1169 SLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL---DPLGShtDEMLWHVLERTFMRDT 1245
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDAS--DAEIREALERAGLDEF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1246 IMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV 1325
Cdd:TIGR02857 441 VAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALA 520
|
....*....
gi 52138554 1326 LNCDLVLVM 1334
Cdd:TIGR02857 521 ALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
494-699 |
7.09e-41 |
|
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: 150.84 E-value: 7.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRE 560
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:cd03253 94 NIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 640 KHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 699
Cdd:cd03253 174 REIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
775-1101 |
2.30e-40 |
|
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: 152.65 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 775 TWKTYHTYIKASGGYLVsFLVLCLFFLMMGSSAFSTWwlgIW-LDRGSQVVCASQNNKTACNVDQTLQDTKHHMYQLVYI 853
Cdd:cd18600 2 TWNTYLRYITSHKSLIF-VLILCLVIFAIEVAASLVG---LWlLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 854 ASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFM 933
Cdd:cd18600 78 GVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 934 VVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKF-K 1012
Cdd:cd18600 158 VIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFhK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1013 TLNDENSSHLLYFNcALRWFALRMDILMnIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFT 1092
Cdd:cd18600 238 ALNLHTANWFLYLS-TLRWFQMRIEMIF-VIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMR 315
|
....*....
gi 52138554 1093 SAELLREYI 1101
Cdd:cd18600 316 SVSRIFKFI 324
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1124-1339 |
1.59e-39 |
|
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: 146.85 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1124 RGEITFKDYRMRYRdNTP--LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 1201
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TKLTMIPQDPVLFVGTVRYNLD-PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLR 1280
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1281 NSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKV 1339
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
160-411 |
5.00e-39 |
|
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: 148.15 E-value: 5.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 160 IGIGICLCLALFTTEFTKVLFWALAWAINYRTAIRLKVALSTLIFENLLSFKTLT----HISAGEVLNILSSDSYSLFEA 235
Cdd:cd18591 52 FSNGYVLAVILFLALLLQATFSQASYHIVIREGIRLKTALQAMIYEKALRLSSWNlssgSMTIGQITNHMSEDANNIMFF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 236 ALFCPLPATIPILMVVCAVYAFFILGSTALVGISVYLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKM 315
Cdd:cd18591 132 FWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 316 YAWEESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCHIFLKRK-LTAPVAFSVIAMFNVMKFSIAI 394
Cdd:cd18591 212 YAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFI 291
|
250
....*....|....*..
gi 52138554 395 LPFSVKAVAEASVSLRR 411
Cdd:cd18591 292 FPVVIPILINAVVSTRR 308
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1147-1365 |
9.30e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.23 E-value: 9.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1147 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLdPLG 1226
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNV-LLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1227 SH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQS 1304
Cdd:PRK11174 447 NPdaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1305 TIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPdSAFAMLLAAEVG 1365
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLAHRQE 586
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
491-710 |
1.57e-38 |
|
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: 152.95 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGN 557
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlaslrrQVALVSQDVVLFNDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILFGE--KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:TIGR02203 422 IANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 636 AHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLiHNlrgLQFKD 710
Cdd:TIGR02203 502 NESERLV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL-HN---MQFRE 571
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
494-702 |
3.59e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 152.31 E-value: 3.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQkGVVAVNG-------------PLAYVSQQAWIFHGNVRE 560
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEK-YNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:PRK11174 442 NVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 640 KHVFeECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 702
Cdd:PRK11174 522 QLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1135-1339 |
5.60e-38 |
|
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: 140.43 E-value: 5.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLF 1214
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1215 VGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASM 1294
Cdd:cd03246 89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52138554 1295 DSKTDTLVQSTIKEA-FKSCTVLTIAHRLNTVLNCDLVLVMENGKV 1339
Cdd:cd03246 128 DVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
491-701 |
2.05e-37 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 149.86 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-------------AVNGPLAYVSQQAWIFHGN 557
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:PRK10789 405 VANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 637 HVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 701
Cdd:PRK10789 485 RT-----EHQILHNLrqwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1127-1341 |
7.82e-37 |
|
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: 137.06 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 1206
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIIL 1286
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1287 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 1341
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1122-1341 |
2.49e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 146.51 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1122 PSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 1201
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TKLTMIPQDPVLFVGTVRYNLdPLGSH--TDEMLWHVLERTFMrDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 1279
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNL-LLAAPnaSDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1280 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 1341
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
113-708 |
7.47e-36 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 145.23 E-value: 7.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 113 RVVWKFQRtRVLMDVVANILCIVMAA---LGPTVLIHQILQH---------ITSISSGHIGIGICLCLALFtteftkVLF 180
Cdd:TIGR02204 7 AALWPFVR-PYRGRVLAALVALLITAaatLSLPYAVRLMIDHgfskdssglLNRYFAFLLVVALVLALGTA------ARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 181 WALAWaINYR--TAIRLKV-----ALSTLIFENLLSfktlthisaGEVLNILSSDSySLFEAALFCPLP-ATIPILMVVC 252
Cdd:TIGR02204 80 YLVTW-LGERvvADIRRAVfahliSLSPSFFDKNRS---------GEVVSRLTTDT-TLLQSVIGSSLSmALRNALMCIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 253 AVYAFFILGS--TALVGISVYLIFIPIQMFMAKLNSTFRRSAISVTDKrVQTMNEFLTCIKLIKMYAWEESfintihdIR 330
Cdd:TIGR02204 149 GLIMMFITSPklTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADA-GSYAGETLGAIRTVQAFGHEDA-------ER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 331 KREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTC---------HIFLKRKLTAPV--AFSVIAMFNVMkfSIAILPFSV 399
Cdd:TIGR02204 221 SRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAivgvlwvgaHDVIAGKMSAGTlgQFVFYAVMVAG--SIGTLSEVW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 400 KAVAEASVSLRRMKKILIAKSPpsyITQPEDPDTILLLANATLTWEQeinrksdppkaqiqkRHVFKKQRPELYSeqsrs 479
Cdd:TIGR02204 299 GELQRAAGAAERLIELLQAEPD---IKAPAHPKTLPVPLRGEIEFEQ---------------VNFAYPARPDQPA----- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 480 dqgvaspewqsgspksvLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAY 546
Cdd:TIGR02204 356 -----------------LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMAL 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 547 VSQQAWIFHGNVRENILFG-------EKYNHQRYQHTvhvcglQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVY 619
Cdd:TIGR02204 419 VPQDPVLFAASVMENIRYGrpdatdeEVEAAARAAHA------HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAIL 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 620 ANRQLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 699
Cdd:TIGR02204 493 KDAPILLLDEATSALDAESEQLV-QQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
....*....
gi 52138554 700 IHnlrgLQF 708
Cdd:TIGR02204 572 AR----LQF 576
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
496-699 |
1.12e-35 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 146.04 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENI 562
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawlrrQMGVVLQENVLFSRSIRDNI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKH 641
Cdd:TIGR01846 552 ALCNpGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE-SEA 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 642 VFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 699
Cdd:TIGR01846 631 LIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1135-1339 |
3.25e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.79 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLF 1214
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1215 VGTVRYNLD-PLGSHTDEMLWHVLERTFMRdtiMKLPEK-LQAEVtengENFSVGERQLLCMARALLRNSKIILLDEATA 1292
Cdd:COG4619 87 GGTVRDNLPfPFQLRERKFDRERALELLER---LGLPPDiLDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1293 SMDSKTDTLVQSTIKEAFKSC--TVLTIAH------RLntvlnCDLVLVMENGKV 1339
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
465-702 |
4.27e-35 |
|
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: 144.50 E-value: 4.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 465 FKKQRPELYSEQSRSDQGVASPEWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-P 543
Cdd:TIGR01193 458 FINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 544 LA------------YVSQQAWIFHGNVRENILFGEKYN--HQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQR 609
Cdd:TIGR01193 538 LKdidrhtlrqfinYLPQEPYIFSGSILENLLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 610 QRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKktLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
250
....*....|...
gi 52138554 690 MEERGRYAKLIHN 702
Cdd:TIGR01193 696 LDRNGFYASLIHN 708
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
494-700 |
4.81e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 144.09 E-value: 4.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRE 560
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvPLvqydhhylhrqvALVGQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:TIGR00958 574 NIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 640 KHVFEEcikKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 700
Cdd:TIGR00958 654 QLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
496-685 |
1.35e-34 |
|
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: 132.23 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PL-------AYVSQQAWIFHGNVRENI 562
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiGLhdlrsriSIIPQDPVLFSGTIRSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 -LFGEKYNHQRYQhTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 641
Cdd:cd03244 99 dPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 642 VfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 685
Cdd:cd03244 178 I-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1127-1342 |
9.81e-34 |
|
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: 129.93 E-value: 9.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRdntplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 1203
Cdd:cd03257 9 VSFPTGGGSVK-----ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1204 LTMIPQDPVLfvgtvryNLDPL---GSHTDEMLWHVleRTFMRDTIMKLPEKLQAEVTENGEN--------FSVGERQLL 1272
Cdd:cd03257 84 IQMVFQDPMS-------SLNPRmtiGEQIAEPLRIH--GKLSKKEARKEAVLLLLVGVGLPEEvlnrypheLSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1273 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 1342
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1143-1350 |
5.60e-33 |
|
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: 136.03 E-value: 5.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL 1222
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1223 DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV 1302
Cdd:COG4618 427 ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1303 QSTIKEAfKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEF-DKPEVLAE 1350
Cdd:COG4618 507 AAAIRAL-KArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1130-1362 |
1.01e-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: 134.65 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1130 KDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTKLTM 1206
Cdd:COG1123 268 KRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPV--LF-VGTVRYNL-DPLGSHtdemlwHVLERTFMRDTIMKLPEK--LQAEVTEN--GEnFSVGERQLLCMARAL 1278
Cdd:COG1123 347 VFQDPYssLNpRMTVGDIIaEPLRLH------GLLSRAERRERVAELLERvgLPPDLADRypHE-LSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1279 LRNSKIILLDEATASMdsktDTLVQSTIKEAFKS------CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:COG1123 420 ALEPKLLILDEPTSAL----DVSVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
250
....*....|..
gi 52138554 1352 PDSAFA-MLLAA 1362
Cdd:COG1123 496 PQHPYTrALLAA 507
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
491-708 |
1.17e-32 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 135.53 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGN 557
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILF--GEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:PRK11176 433 IANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 636 AHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLiHNlrgLQF 708
Cdd:PRK11176 513 TES-----ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL-HK---MQF 580
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1128-1338 |
1.35e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 124.28 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1128 TFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMI 1207
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1208 PQdpvlfvgtvrynldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILL 1287
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1288 DEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGK 1338
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
496-675 |
2.44e-32 |
|
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: 125.72 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL-------AYVSQQA---WIFHGNVRENILF 564
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkPLekerkriGYVPQRRsidRDFPISVRDVVLM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 565 GekynhqRYQHTVHVCGLQKD-----LNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHV 638
Cdd:cd03235 94 G------LYGHKGLFRRLSKAdkakvDEALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 52138554 639 GKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILL 675
Cdd:cd03235 168 QEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLLL 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1144-1292 |
5.70e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 122.37 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVG-TVRYNL 1222
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1223 -------DPLGSHTDEMLWHVLERtfmrdtiMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATA 1292
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
491-703 |
6.16e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 133.03 E-value: 6.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA------------YVSQQAWIFHGN 557
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqPIAdyseaalrqaisVVSQRVHLFSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTeIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:PRK11160 430 LRDNLLLAaPNASDEALIEVLQQVGLEKLLEDDKGLNAW-LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 637 HVGKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNL 703
Cdd:PRK11160 509 ETERQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
586-1336 |
6.27e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 136.31 E-value: 6.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 586 LNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKT---LKG---KTVVLV 659
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-----EYLVQKTinnLKGnenRITIII 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 660 THQLQFLESCDEVILLEDGE-----------------------------------------------ICEKGTHKELMEE 692
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKN 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 693 R-GRYAKLIHNLRglqfkdpehiynvamVETLKESPAQRDEDAVLASGDEKDE--GKEPE-----------------TEE 752
Cdd:PTZ00265 717 KnGIYYTMINNQK---------------VSSKKSSNNDNDKDSDMKSSAYKDSerGYDPDemngnskhenesasnkkSCK 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 753 FVDTNAPAHQL------------IQTESPQEGIVTWKTYHTYIKASGGYLVSFLV---LCLFFLMMGSSAFSTWWLGIWL 817
Cdd:PTZ00265 782 MSDENASENNAggklpflrnlfkRKPKAPNNLRIVYREIFSYKKDVTIIALSILVaggLYPVFALLYAKYVSTLFDFANL 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 818 DRGSQvvcasqnnktacnvdqtlqdtKHHMYQLVyiasmVSVLMF--GIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMS 895
Cdd:PTZ00265 862 EANSN---------------------KYSLYILV-----IAIAMFisETLKNYYNNVIGEKVEKTMKRRLFENILYQEIS 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 896 FFDT---TPtGRLMNRFSKDMDELDVRLPFHAENFlQQFFMVVFILVIMAAVF-PVVLVVLAGLAVIFLILLRIFHRgVQ 971
Cdd:PTZ00265 916 FFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIF-THFIVLFLVSMVMSFYFcPIVAAVLTGTYFIFMRVFAIRAR-LT 992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 972 ELKQVEN-----------------ISRSPWFShITSSIQGLGVIHAYDKKD---DCISKFKTLNDENSSHLLYFNCALRW 1031
Cdd:PTZ00265 993 ANKDVEKkeinqpgtvfaynsddeIFKDPSFL-IQEAFYNMNTVIIYGLEDyfcNLIEKAIDYSNKGQKRKTLVNSMLWG 1071
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1032 FALRMDILMNIVTFVV-ALLVTLSFSSISASSKGLsLSYIIQLSGLLQVCVRTGTETQAKFTsaeLLREYILTCVPEHTH 1110
Cdd:PTZ00265 1072 FSQSAQLFINSFAYWFgSFLIRRGTILVDDFMKSL-FTFLFTGSYAGKLMSLKGDSENAKLS---FEKYYPLIIRKSNID 1147
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1111 PFKVG--TCPKDWPSRGEITFKDYRMRY--RDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL--------- 1177
Cdd:PTZ00265 1148 VRDNGgiRIKNKNDIKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhi 1226
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1178 ---------------------------------------------VEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPV 1212
Cdd:PTZ00265 1227 vfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPM 1306
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 LFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEA 1290
Cdd:PTZ00265 1307 LFNMSIYENIK-FGKEdaTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEA 1385
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 52138554 1291 TASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLNCDLVLVMEN 1336
Cdd:PTZ00265 1386 TSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
491-692 |
1.38e-31 |
|
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: 131.70 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHGN 557
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAdlkqwdretfgkhIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:TIGR01842 408 VAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 637 hVGKHVFEECIKKT-LKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:TIGR01842 488 -EGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
496-713 |
1.63e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVNGP--------LAYVSQQA---WIFHGNVRENIL 563
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGpN-GAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FGekynhqRYQHTVHVCGLQKD--------LNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAV 634
Cdd:COG1121 100 MG------RYGRRGLFRRPSRAdreavdeaLERV---GLEDLADRPIGeLSGGQQQRVLLARALAQDPDLLLLDEPFAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 635 DAHvGKHVFEECIKKtLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEkGTHKELMEErgryaKLIHNLRGLQFKDP 711
Cdd:COG1121 171 DAA-TEEALYELLRE-LRreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTP-----ENLSRAYGGPVALL 242
|
..
gi 52138554 712 EH 713
Cdd:COG1121 243 AH 244
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1129-1338 |
4.14e-31 |
|
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: 121.81 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1129 FKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIP 1208
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1209 QDP--VLFVGTVR----YNLDPLGSHTDEM---LWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALL 1279
Cdd:cd03225 82 QNPddQFFGPTVEeevaFGLENLGLPEEEIeerVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1280 RNSKIILLDEATASMDSKTDTLVQSTIKEaFKSC--TVLTIAHRLNTVLN-CDLVLVMENGK 1338
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
491-680 |
4.16e-31 |
|
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: 130.25 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV------------AVNGP-LAYVSQQAWIFHGN 557
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGRhIGYLPQDVELFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENI-LFGEkynhqryqHT------------VHvcglqkDL-NSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQ 623
Cdd:COG4618 422 IAENIaRFGD--------ADpekvvaaaklagVH------EMiLRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 624 LYLLDDPLSAVDAhVGKHVFEECIKKtLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:COG4618 488 LVVLDEPNSNLDD-EGEAALAAAIRA-LKarGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1130-1362 |
4.90e-31 |
|
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: 122.99 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1130 KDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQ 1209
Cdd:COG1124 9 VSYGQGGRRVP--VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1210 DPVLFV---GTVRYNLD-PLGSH----TDEMLWHVLERTFMRDTIM-KLPEKLqaevtengenfSVGERQLLCMARALLR 1280
Cdd:COG1124 87 DPYASLhprHTVDRILAePLRIHglpdREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1281 NSKIILLDEATASMdsktDTLVQSTI-------KEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKP 1352
Cdd:COG1124 156 EPELLLLDEPTSAL----DVSVQAEIlnllkdlREERGL-TYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|.
gi 52138554 1353 DSAFA-MLLAA 1362
Cdd:COG1124 231 KHPYTrELLAA 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1127-1348 |
5.53e-31 |
|
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: 122.29 E-value: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICT--VGLED 1199
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQDPVLFVGTVRYNLDpLGshtdemLWHVLERTfmRDTIMKLPEK------LQAEVTE--NGENFSVGERQL 1271
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YG------LRLHGIKL--KEELDERVEEalrkaaLWDEVKDrlHALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1272 LCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVL 1348
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
494-680 |
9.68e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.69 E-value: 9.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRE 560
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkPLsampppewrrqvAYVPQEPALWGGTVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYNHQRYQHTvHVCGLQKDLNsLPYGDLteigERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvG 639
Cdd:COG4619 93 NLPFPFQLRERKFDRE-RALELLERLG-LPPDIL----DKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-N 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 640 KHVFEECIKKTL--KGKTVVLVTH-QLQFLESCDEVILLEDGEI 680
Cdd:COG4619 166 TRRVEELLREYLaeEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
496-692 |
1.23e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 118.63 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAwIFHGN--VREN 561
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEP-ALYPDltVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILF-------GEKYNHQRYQHTVHVCGLQKDLNSLpygdlteIGergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 634
Cdd:COG1131 94 LRFfarlyglPRKEARERIDELLELFGLTDAADRK-------VG----TLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 635 DAhVGKHVFEECIKKtLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 692
Cdd:COG1131 163 DP-EARRELWELLRE-LAaeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
496-680 |
1.23e-29 |
|
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: 118.34 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRENI 562
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkPIsqyehkylhskvSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKH 641
Cdd:cd03248 109 AYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQ 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 52138554 642 VFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1124-1352 |
1.58e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.60 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1124 RGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTK 1203
Cdd:PRK10789 311 RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1204 LTMIPQDPVLFVGTVRYNLdPLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRN 1281
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNI-ALGrpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1282 SKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 1352
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1127-1364 |
2.05e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 124.63 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK 1203
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1204 LTMIPQDPvlfvgtvRYNLDPL--GSHTDEMLW-HVLERTFMRDTIMKLPEK--LQAEVTENGENFSVGERQLLCMARAL 1278
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVtvGDQIAEALEnLGLSRAEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1279 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIE-------FDKPEVL 1348
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEdgppeeiLAAPQAL 237
|
250
....*....|....*.
gi 52138554 1349 AEKPDSAFAMLLAAEV 1364
Cdd:COG1123 238 AAVPRLGAARGRAAPA 253
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
494-680 |
2.24e-29 |
|
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: 115.57 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGplayvsQQAWIFHGNVRENIlfgekynhqry 573
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRI----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 574 qhtvhvcGLQKDLNSLpYGDLTeiGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKK-TLK 652
Cdd:cd03230 76 -------GYLPEEPSL-YENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElKKE 144
|
170 180
....*....|....*....|....*....
gi 52138554 653 GKTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:cd03230 145 GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
494-692 |
2.91e-29 |
|
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: 117.84 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWI-FHGNVR 559
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrDLaslsrrelarriAYVPQEPPApFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGekynhqRYQHTVHVCGLQKD--------LNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:COG1120 94 ELVALG------RYPHLGLFGRPSAEdreaveeaLERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 631 LSAVDAHvgkHVFE--ECIKK--TLKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:COG1120 165 TSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1127-1365 |
3.12e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.55 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDP-VLFVG-TVR---------YNLDPlgSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMA 1275
Cdd:PRK13632 88 IFQNPdNQFIGaTVEddiafglenKKVPP--KKMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1276 RALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP-EVLAEKP 1352
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPkEILNNKE 234
|
250 260
....*....|....*....|
gi 52138554 1353 -------DSAFAMLLAAEVG 1365
Cdd:PRK13632 235 ilekakiDSPFIYKLSKKLK 254
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
491-677 |
4.16e-28 |
|
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: 113.72 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------PLAYVSQQAWIF-HGNVREN 561
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDALLpWLTVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGEKYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 634
Cdd:cd03293 94 VALGLELQGvpkaearERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 52138554 635 DAHVGKHVFEEcIKKTLK--GKTVVLVTHQLqflescDEVILLED 677
Cdd:cd03293 163 DALTREQLQEE-LLDIWRetGKTVLLVTHDI------DEAVFLAD 200
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
794-1077 |
5.62e-28 |
|
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: 115.05 E-value: 5.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 794 LVLCLFFLMMGS--SAFSTWWLGIWLDrgsqvvcasqnnktACNVDQTLQDTKHHMYQLVYIASMVSVLMFGIIKGFTFT 871
Cdd:pfam00664 1 LILAILLAILSGaiSPAFPLVLGRILD--------------VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 872 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 951
Cdd:pfam00664 67 HTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 952 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 1031
Cdd:pfam00664 147 LLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 52138554 1032 FALRMDILMNIVTFVVALLVTLSFSSISASSKGL--SLSYIIQLSGLL 1077
Cdd:pfam00664 227 SFGITQFIGYLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFGPL 274
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
496-695 |
7.24e-28 |
|
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: 113.80 E-value: 7.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQQAWIFHGN-------VRENI 562
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkePREARRQIGVLPDERglydrltVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 -LFGEKY------NHQRYQHTVHVCGLQKDLNslpygdlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:COG4555 96 rYFAELYglfdeeLKKRIEELIELLGLEEFLD-----------RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 636 AhVGKHVFEECIKKTLK-GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 695
Cdd:COG4555 165 V-MARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
496-701 |
8.24e-28 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 121.20 E-value: 8.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSS---LISALL----GQM--------QLQKGVVAvnGPLAYVSQQAWIFHGNVRE 560
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTiakLVAGLYqpwsGEIlfdgipreEIPREVLA--NSVAMVDQDIFLFEGTVRD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NI-LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:TIGR03796 572 NLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 640 KHVFEEcIKKtlKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 701
Cdd:TIGR03796 652 KIIDDN-LRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
496-680 |
1.64e-27 |
|
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: 110.38 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHGNVRENI 562
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LfgekynhqryqhtvhvcglqkdlnslpygdlteigergvnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDaHVGKHV 642
Cdd:cd03246 97 L-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERA 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 52138554 643 FEECIKKT-LKGKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:cd03246 135 LNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1127-1348 |
2.21e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 112.44 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVG-TV-------RYN-LDPLGSHTDE---MLWHVLERTfmrdtimKLPEKLQAEVTEngenFSVGERQLLCM 1274
Cdd:COG1120 80 VPQEPPAPFGlTVrelvalgRYPhLGLFGRPSAEdreAVEEALERT-------GLEHLADRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1275 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVL 1348
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPeEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
491-679 |
2.23e-27 |
|
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: 111.02 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW--------------IFH 555
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkDLTKLSLKELrrkvglvfqnpddqFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 GNVRENILFGEKyNHQRYQHTVhvcgLQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLArAVYANR-QLYLLDDPLSA 633
Cdd:cd03225 91 PTVEEEVAFGLE-NLGLPEEEI----EERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIA-GVLAMDpDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 52138554 634 VDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQFL-ESCDEVILLEDGE 679
Cdd:cd03225 165 LDPAGRRELLE--LLKKLKaeGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
494-689 |
2.23e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 111.82 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PL----AYVSQQAWIFHG- 556
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyRLrrrmGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENILFGEKYNHQRYQHTV--------HVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLD 628
Cdd:cd03261 93 TVFENVAFPLREHTRLSEEEIreivleklEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 629 DPLSAVDAhVGKHVFEECI---KKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 689
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
494-679 |
3.60e-27 |
|
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: 108.87 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWifhgnvRENILfgekYNHQr 572
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEEL------RRRIG----YVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 573 yqhtvhvcglqkdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLK 652
Cdd:cd00267 81 -------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE 129
|
170 180
....*....|....*....|....*...
gi 52138554 653 GKTVVLVTHQLQFLE-SCDEVILLEDGE 679
Cdd:cd00267 130 GRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1143-1338 |
4.05e-27 |
|
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: 109.20 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG--LEDLRTKLTMIPQDPVLFVG-TVR 1219
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 YNLdplgshtdemlwhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTD 1299
Cdd:cd03229 95 ENI--------------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 52138554 1300 TLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGK 1338
Cdd:cd03229 137 REVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
494-680 |
4.19e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.45 E-value: 4.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQqawifhgnvre 560
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 nilfgekynhqryqhtvhvcglqkdlnSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52138554 640 KHVFEECIK-KTLKGKTVVLVTHQL-QFLESCDEVILLEDGEI 680
Cdd:cd03214 134 IELLELLRRlARERGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
496-701 |
4.83e-27 |
|
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: 118.91 E-value: 4.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-------------AVNGPLAYVSQQAWIFHGNVRENI 562
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqdlagldvqAVRRQLGVVLQNGRLMSGSIFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV 642
Cdd:TIGR03797 548 AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIV 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 643 FEECikKTLKGkTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 701
Cdd:TIGR03797 628 SESL--ERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
131-412 |
1.23e-26 |
|
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: 111.49 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 131 ILCIVMAALGPTVLiHQILQHITSISSGHIgIGICLCLALFTTEFTKVLFWA-LAWAINyRTAIRLKVALSTLIFENLLS 209
Cdd:cd18598 7 LLADVLGFAGPLLL-NKLVEFLEDSSEPLS-DGYLYALGLVLSSLLGALLSShYNFQMN-KVSLKVRAALVTAVYRKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 210 FKT--LTHISAGEVLNILSSDS-------YSLFEAALfcpLPATIPIlmvvcavyAFFIL----GSTALVGISVYLIFIP 276
Cdd:cd18598 84 VRSssLSKFSTGEIVNLMSTDAdrivnfcPSFHDLWS---LPLQIIV--------ALYLLyqqvGVAFLAGLVFALVLIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 277 IQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIVST 356
Cdd:cd18598 153 INKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 357 IAIVSTFTCHIFLKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18598 233 LISILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
496-677 |
1.84e-26 |
|
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: 108.34 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQQAWIFHGN-------VRENI 562
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHADglkpeltVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LF-----GEKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 637
Cdd:COG4133 97 RFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 52138554 638 vGKHVFEECIKKTL-KGKTVVLVTHQLQFLESCdEVILLED 677
Cdd:COG4133 166 -GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-RVLDLGD 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
496-699 |
6.50e-26 |
|
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: 114.53 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQ---AWI---------FHGNVRENI 562
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqDIRDVTQAslrAAIgivpqdtvlFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFG-------EKYNHQRYQHtvhvcgLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:COG5265 453 AYGrpdaseeEVEAAARAAQ------IHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 636 AHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 699
Cdd:COG5265 527 SRT-----ERAIQAALrevaRGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
496-693 |
8.13e-26 |
|
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: 107.42 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQ-----------QawIFHGNV 558
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRkvglvfqnpddQ--LFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLArAVYANR-QLYLLDDP 630
Cdd:COG1122 94 EEDVAFGpenlglpREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIA-GVLAMEpEVLVLDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 631 LSAVDAHvGKHVFEECIKK-TLKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:COG1122 162 TAGLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1127-1353 |
9.17e-26 |
|
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: 107.20 E-value: 9.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 1203
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1204 LTMIPQDPVLFVG-TVRYNLD-PLGSHTDEMLWHVLERTFM-------RDTIMKLPEKLqaevtengenfSVGERQLLCM 1274
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTRLSEEEIREIVLEkleavglRGAEDLYPAEL-----------SGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1275 ARALLRNSKIILLDEATASMDSKTDTLVQSTI---KEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAE 1350
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIrslKKELG-LTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
...
gi 52138554 1351 KPD 1353
Cdd:cd03261 227 SDD 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
499-680 |
9.53e-26 |
|
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: 106.61 E-value: 9.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVrKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL-----------------AYVSQQAWIF-HGNVRE 560
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYnHQRYQHTVHVcglQKDLNSLpygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:cd03297 95 NLAFGLKR-KRNREDRISV---DELLDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 640 KHVFEEC--IKKTLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:cd03297 168 LQLLPELkqIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1140-1338 |
1.19e-25 |
|
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: 106.01 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1140 TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIdevdICTVGLedlrtkltmIPQDPVLFVGTVR 1219
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV----PGSIAY---------VSQEPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 YNLdpLGSHT--DEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 1297
Cdd:cd03250 84 ENI--LFGKPfdEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52138554 1298 T-DTLVQSTIKEAFKSC-TVLTIAHRLNTVLNCDLVLVMENGK 1338
Cdd:cd03250 162 VgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
375-663 |
2.56e-25 |
|
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: 112.07 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 375 APVAFSVI-----AMFNVMkfsiAILPFSVKAVAEASVSLRRMKKILIAKSPPSYITQPEDPDtilllanatltweqein 449
Cdd:TIGR02868 269 APVTLAVLvllplAAFEAF----AALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGA----------------- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 450 rkSDPPKAQIQKRHVfkkqrpelyseqsrsdqgvaSPEWQSGSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLG 529
Cdd:TIGR02868 328 --VGLGKPTLELRDL--------------------SAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 530 QMQLQKGVVAVNGP-------------LAYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLT 595
Cdd:TIGR02868 384 LLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLArPDATDEELWAALERVGLADWLRALPDGLDT 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 596 EIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQL 663
Cdd:TIGR02868 464 VLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1119-1352 |
3.45e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 113.97 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1119 KDWPSRGEITFKDYRMRY--RDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-DEVDICTV 1195
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYdtRKDVEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1196 GLEDLRTKLTMIPQDPVLFVGTVRYNL-------------------------------------------DPLGSHTDEM 1232
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedgndsqenknkrnscrakcagdlnDMSNTTDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1233 LWH---------------VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 1297
Cdd:PTZ00265 534 LIEmrknyqtikdsevvdVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1298 TDTLVQSTIK--EAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 1352
Cdd:PTZ00265 614 SEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
491-684 |
3.56e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.93 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP------------LAYVSQQAWIFHGNV 558
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENIlfgekynhqryqhtvhvcglqkdlnslpygdlteiGERgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHV 638
Cdd:cd03247 92 RNNL-----------------------------------GRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52138554 639 GKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKG 684
Cdd:cd03247 134 ERQLLS-LIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
487-680 |
5.08e-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: 104.49 E-value: 5.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 487 EWQSGSPKS-VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW----------IF 554
Cdd:cd03255 9 TYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtDISKLSEKELaafrrrhigfVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 -------HGNVRENILFGEKY-------NHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYA 620
Cdd:cd03255 89 qsfnllpDLTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYP-----------SELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 621 NRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMEL-LRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1130-1340 |
6.03e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 103.28 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1130 KDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQ 1209
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1210 dpvlfvgtvryNLDPLGshtdemLWHVLERTFMRdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDE 1289
Cdd:cd03214 81 -----------ALELLG------LAHLADRPFNE--------------------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1290 ATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVI 1340
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1127-1346 |
1.52e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 1277
Cdd:PRK13635 86 VFQNPdNQFVGAtvqddVAFGLENIGVPREEMVERVdqaLRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1278 LLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPE 1346
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1127-1353 |
1.97e-24 |
|
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: 103.52 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 1203
Cdd:COG1127 6 IEVRNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1204 LTMIPQDPVLFVG-TVRYNLD-PLGSHTD-------EMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGerqllcM 1274
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfPLREHTDlseaeirELVLEKLELVGLPGAADKMPSEL-----------SGG------M 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1275 ------ARALLRNSKIILLDEATASMD----SKTDTLVQsTIKEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 1343
Cdd:COG1127 147 rkrvalARALALDPEILLYDEPTAGLDpitsAVIDELIR-ELRDELG-LTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
250
....*....|
gi 52138554 1344 KPEVLAEKPD 1353
Cdd:COG1127 225 TPEELLASDD 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
491-678 |
2.15e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.02 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------PLAYVSQQA----WIfhgNV 558
Cdd:COG1116 21 GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQEPallpWL---TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:COG1116 98 LDNVALGlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 632 SAVDAHVGKHVFEECIK---KTlkGKTVVLVTHQLQ---FLesCDEVILLEDG 678
Cdd:COG1116 167 GALDALTRERLQDELLRlwqET--GKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
495-685 |
2.31e-24 |
|
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: 102.49 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVREN 561
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 IlfgEKYNHQRyqhtvhvcglQKDLnslpYGDLtEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgKH 641
Cdd:cd03369 102 L---DPFDEYS----------DEEI----YGAL-RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 642 VFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 685
Cdd:cd03369 163 LIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
496-680 |
2.31e-24 |
|
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: 102.60 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENIL 563
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDYALFpHLTVAENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FGEKYNHQRYQHTVhvcglQKDLNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV 642
Cdd:cd03259 95 FGLKLRGVPKAEIR-----ARVRELLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 52138554 643 FEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 680
Cdd:cd03259 170 REE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1127-1341 |
2.67e-24 |
|
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: 103.04 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIIIDEVDICTV---GLEDL 1200
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1201 RTKLTMIPQDPVLFVG-TVRYNLD-PL------GSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLL 1272
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1273 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElgLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
497-700 |
4.62e-24 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 108.82 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENIL 563
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGidintvtreslrkSIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV 642
Cdd:TIGR01192 431 LGrEGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARV 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 643 fEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 700
Cdd:TIGR01192 511 -KNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
497-632 |
6.18e-24 |
|
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: 99.26 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIF-HGNVRENI 562
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 563 LFGEkyNHQRYQHTVHVCGLQKDLNSLPYGDL--TEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 632
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1127-1343 |
6.89e-24 |
|
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: 101.06 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdlRTKLTM 1206
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLF-----VGTVRYNLDPLGSHTDEMLWHVLERTFMrdtiMKLPEKLQAEVTEngenFSVGERQLLCMARALLRN 1281
Cdd:cd03259 77 VFQDYALFphltvAENIAFGLKLRGVPKAEIRARVRELLEL----VGLEGLLNRYPHE----LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1282 SKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 1343
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1127-1345 |
1.50e-23 |
|
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: 101.11 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 1203
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1204 LTMIPQDpvlfvgtvrYNLDP------------LGSHTdemLWHVLERTFMRDTIMK---------LPEKLQAEVTEnge 1262
Cdd:cd03256 80 IGMIFQQ---------FNLIErlsvlenvlsgrLGRRS---TWRSLFGLFPKEEKQRalaalervgLLDKAYQRADQ--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1263 nFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVL-NCDLVLVMENGKV 1339
Cdd:cd03256 145 -LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAReYADRIVGLKDGRI 223
|
....*.
gi 52138554 1340 IeFDKP 1345
Cdd:cd03256 224 V-FDGP 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
494-679 |
1.50e-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: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG---------------PLAYVSQQAWIF-HGN 557
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFpHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILFGekynhqryqhtvhvcglqkdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 637
Cdd:cd03229 93 VLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52138554 638 VGKHVFEECikKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGE 679
Cdd:cd03229 135 TRREVRALL--KSLQaqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
496-691 |
1.51e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 103.69 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAWIF-HGNVRENI 562
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlpprerRVGFVFQHYALFpHMTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFG-------EKYNHQRYQH---TVHvcglqkdlnslpygdLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:COG1118 97 AFGlrvrppsKAEIRARVEElleLVQ---------------LEGLADRYPSqLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 632 SAVDAHVGKHVfEECIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 691
Cdd:COG1118 162 GALDAKVRKEL-RRWLRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
497-701 |
1.92e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.58 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENIL 563
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhvgkhV 642
Cdd:PRK13657 431 VGrPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV-----E 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 643 FEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 701
Cdd:PRK13657 506 TEAKVKAALdelmKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1127-1340 |
2.04e-23 |
|
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: 99.89 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTvGLEDLRTKLTM 1206
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVG-TVRYNLD---PLGSHTDEMLWHVLERTFmrdTIMKLPEKLQAEVTengeNFSVGERQLLCMARALLRNS 1282
Cdd:cd03263 80 CPQFDALFDElTVREHLRfyaRLKGLPKSEIKEEVELLL---RVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1283 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 1340
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
494-696 |
2.88e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 106.34 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRE 560
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrPLsslshsvlrqgvAMVQQDPVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgk 640
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-- 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 641 hvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRY 696
Cdd:PRK10790 512 ---EQAIQQALaavrEHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
496-680 |
6.07e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.96 E-value: 6.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA----------------YVSQqawiFHG-- 556
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqDISslserelarlrrrhigFVFQ----FFNll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 ---NVRENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYL 626
Cdd:COG1136 99 pelTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 627 LDDPLSAVDAHVGKHVFE---ECIKKTlkGKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLEllrELNREL--GTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1127-1350 |
1.36e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 98.24 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvglEDLRTKLTM 1206
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQD-------PVL---FVGTVRYN----LDPLGSHTDEMLWHVLERT----FMRDTIMKLpeklqaevtengenfSVGE 1268
Cdd:COG1121 80 VPQRaevdwdfPITvrdVVLMGRYGrrglFRRPSRADREAVDEALERVgledLADRPIGEL---------------SGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1269 RQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMeNGKVIEFDKP- 1345
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPe 223
|
....*
gi 52138554 1346 EVLAE 1350
Cdd:COG1121 224 EVLTP 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1143-1350 |
1.80e-22 |
|
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: 97.50 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPVLFVG-TVRY 1220
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1221 NLDpLGSHT------DEMLWHVLERtFMRdtimkLPEKLQAEvtenGENFSVGERQLLCMARALLRNSKIILLDEATASM 1294
Cdd:cd03224 95 NLL-LGAYArrrakrKARLERVYEL-FPR-----LKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1295 DSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAE 1350
Cdd:cd03224 164 APKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
496-692 |
2.33e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 100.17 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENIL 563
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppekrNVGMVFQDYALFpHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FG---EKYN----HQRYQHTVHVCGLqkdlnslpygdlTEIGERGVN-LSGGQRQRISLARAVyANR-QLYLLDDPLSAV 634
Cdd:COG3842 100 FGlrmRGVPkaeiRARVAELLELVGL------------EGLADRYPHqLSGGQQQRVALARAL-APEpRVLLLDEPLSAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 635 DAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:COG3842 167 DAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
496-691 |
2.86e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 97.57 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWiFHGNVRenILFGEKYN--HQRy 573
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRRRVQ--MVFQDPYAslHPR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 574 qHTV--------HVCGLqkdlnslpygdlTEIGERGVN------------------LSGGQRQRISLARAVYANRQLYLL 627
Cdd:COG1124 96 -HTVdrilaeplRIHGL------------PDREERIAElleqvglppsfldryphqLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 628 DDPLSAVDAHVGKHV---FEEcIKKTlKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 691
Cdd:COG1124 163 DEPTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1143-1341 |
2.88e-22 |
|
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: 99.36 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTVGLEDLRT----KLTMIPQD----- 1210
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1211 -PVLfvgTVRYNL-DPLGSHTD-----------EMlwhvLERTFMRDtimklPEKL------QaevtengenFSVGERQL 1271
Cdd:COG0444 100 nPVM---TVGDQIaEPLRIHGGlskaeareraiEL----LERVGLPD-----PERRldryphE---------LSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1272 LCMARALLRNSKIILLDEATASMdsktDTLVQSTI-------KEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTAL----DVTIQAQIlnllkdlQRELG-LAILFITHDLGVVAEiADRVAVMYAGRIVE 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1127-1339 |
3.16e-22 |
|
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: 96.40 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYR--DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIIIDEVDICTVGLEDL--- 1200
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1201 -RTKLTMIPQD----PVLfvgTVRYNLD-PL------GSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGE 1268
Cdd:cd03255 80 rRRHIGFVFQSfnllPDL---TALENVElPLllagvpKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1269 RQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKV 1339
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1127-1354 |
3.99e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPV-LFVG-TVRYN----LDPLGSHTDEM---LWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 1277
Cdd:PRK13648 88 VFQNPDnQFVGsIVKYDvafgLENHAVPYDEMhrrVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1278 LLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDS 1354
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
491-684 |
5.08e-22 |
|
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: 96.42 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQ---------AWIF------ 554
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkDLLKLSRRlrkirrkeiQMVFqdpmss 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 -----------------HGNVRENilfgEKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARA 617
Cdd:cd03257 95 lnprmtigeqiaeplriHGKLSKK----EARKEAVLLLLVGVGLPEEVLNRYPHE-----------LSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 618 VYANRQLYLLDDPLSAVDAHVgkhvfEECIKKTLK------GKTVVLVTHQLQFL-ESCDEVILLEDGEICEKG 684
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSV-----QAQILDLLKklqeelGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
494-691 |
8.20e-22 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 95.82 E-value: 8.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWI---------FHG------- 556
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrrigmlFQGgalfdsl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENILFGEKynhqryQHT----------VHVC----GLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANR 622
Cdd:COG1127 98 TVFENVAFPLR------EHTdlseaeirelVLEKlelvGLPGAADKMP-------SE----LSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 623 QLYLLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 691
Cdd:COG1127 161 EILLYDEPTAGLDP-ITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
123-388 |
9.40e-22 |
|
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: 96.94 E-value: 9.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 123 VLMDVVANILCIVMAALGPtVLIHQILQHITSISSGH--IGIGICLCLALFTteftkVLFWALAWAINY---RTAIRLKV 197
Cdd:pfam00664 1 LILAILLAILSGAISPAFP-LVLGRILDVLLPDGDPEtqALNVYSLALLLLG-----LAQFILSFLQSYllnHTGERLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 198 ALSTLIFENLL--SFKTLTHISAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILG-STALVGISVYLIF 274
Cdd:pfam00664 75 RLRRKLFKKILrqPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGwKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 275 IPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQSGNSALAPIV 354
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 52138554 355 STIAIVSTFTCHIFL--KRKLTAPVAFSVIAMFNVM 388
Cdd:pfam00664 235 GYLSYALALWFGAYLviSGELSVGDLVAFLSLFAQL 270
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
493-689 |
1.09e-21 |
|
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: 95.33 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK-----GVVAVNG---------PLAY------VSQQAW 552
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGkdiydldvdVLELrrrvgmVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 553 IFHGNVRENILFGEKynhqryqhtVHVCGLQKDLNSLPYGDLTEIG--------ERGVNLSGGQRQRISLARAVYANRQL 624
Cdd:cd03260 92 PFPGSIYDNVAYGLR---------LHGIKLKEELDERVEEALRKAAlwdevkdrLHALGLSGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 625 YLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKEL 689
Cdd:cd03260 163 LLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1125-1321 |
1.48e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTPLVlDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIIIDEVDictvgledl 1200
Cdd:COG4178 361 GALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGKSTL----LRaiagLWPYGSGRIARPAGA--------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1201 rtKLTMIPQDPVLFVGTVR----YNLDPlGSHTDEMLWHVLERTFMRDtimkLPEKLQAEvtENGEN-FSVGERQLLCMA 1275
Cdd:COG4178 427 --RVLFLPQRPYLPLGTLReallYPATA-EAFSDAELREALEAVGLGH----LAERLDEE--ADWDQvLSLGEQQRLAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52138554 1276 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR 1321
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
496-692 |
1.55e-21 |
|
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: 94.81 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVSQQAWIFHG-NVRE 560
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglpPheraragIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYNHQRyqhtvhvcGLQKDLNSLpYGDLTEIGER----GVNLSGGQRQRISLARAVYANRQLYLLDDP---LSA 633
Cdd:cd03224 95 NLLLGAYARRRA--------KRKARLERV-YELFPRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 634 VdahVGKHVFeECIKKtLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:cd03224 166 K---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
792-1101 |
3.56e-21 |
|
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: 95.36 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 792 SFLVLCLFFLMMGSSAFSTWWLGIWLDRgsqvvcasqnnktacNVDQTLQDTkhHMYQLVYIASMVS--VLMFGIikGFT 869
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDD---------------PVNGPQEHG--QVYLSVLGALAILqgITVFQY--SMA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 870 FTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVL 949
Cdd:cd18559 62 VSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 950 VVLAgLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFnCAL 1029
Cdd:cd18559 142 VGIP-LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSI-VYL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1030 RWFALRMDILMNIVTFVVALLVTLSFSSISASSkGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 1101
Cdd:cd18559 220 RALAVRLWCVGPCIVLFASFFAYVSRHSLAGLV-ALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
497-691 |
4.32e-21 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 93.94 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLA-----------YVSQQAWIF-HGNVRENILF 564
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHYALFrHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 565 G-------EKYNHQRYQHTVHvcglqkdlNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:cd03296 98 GlrvkprsERPPEAEIRAKVH--------ELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 637 HVGKHvfeecIKKTLK------GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 691
Cdd:cd03296 170 KVRKE-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
496-689 |
5.05e-21 |
|
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: 93.41 E-value: 5.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG----------------PLAYVSQQAWIFHG-NV 558
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkarrRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:cd03258 100 FENVALpleiagvPKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 632 SAVDAHVGKHVFE--ECIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 689
Cdd:cd03258 169 SALDPETTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
488-680 |
5.35e-21 |
|
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: 92.70 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P----LAYVSQQAWIF-H 555
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlpPkdrdIAMVFQNYALYpH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 GNVRENILFGEKYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLD 628
Cdd:cd03301 87 MTVYDNIAFGLKLRKvpkdeidERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 629 DPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 680
Cdd:cd03301 156 EPLSNLDAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
493-680 |
5.40e-21 |
|
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: 92.98 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG---------------PLAYVSQQAWIF-HG 556
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENILFGEKYNHQR---------YQHTVHVcGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLL 627
Cdd:cd03262 92 TVLENITLAPIKVKGMskaeaeeraLELLEKV-GLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 52138554 628 DDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQF-LESCDEVILLEDGEI 680
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
483-680 |
5.50e-21 |
|
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: 92.23 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 483 VASPEWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ--KGVVAVNGP----------LAYVSQQ 550
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRpldkrsfrkiIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 551 AwIFHGN--VRENILFGEKYnhqryqhtvhvcglqkdlnslpygdlteigeRGvnLSGGQRQRISLARAVYANRQLYLLD 628
Cdd:cd03213 91 D-ILHPTltVRETLMFAAKL-------------------------------RG--LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 629 DPLSAVDAHVGKHVFeecikKTLK-----GKTVVLVTHQL--QFLESCDEVILLEDGEI 680
Cdd:cd03213 137 EPTSGLDSSSALQVM-----SLLRrladtGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1143-1364 |
5.91e-21 |
|
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: 93.55 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdlRTKLTMIPQDPVLFVG-TVRYN 1221
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1222 LDplgshtdemlWHVLERTFMRDTI----MKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 1295
Cdd:cd03299 92 IA----------YGLKKRKVDKKEIerkvLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1296 SKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSAF-AMLLAAEV 1364
Cdd:cd03299 162 VRTKEKLREELKKIRKEfgVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFvAEFLGFNN 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
497-692 |
9.57e-21 |
|
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: 93.86 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA----------WIF-------HGNV 558
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqDIAAMSRKElrelrrkkisMVFqsfallpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 632 SAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
496-715 |
1.74e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 96.90 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW---------IF---------HG 556
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkDLTKLSRRSLrelrrrvqmVFqdpysslnpRM 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENI-----LFGEKYNHQRYQHTVHV---CGLQKD-LNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLL 627
Cdd:COG1123 360 TVGDIIaeplrLHGLLSRAERRERVAELlerVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLIL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 628 DDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELmeergryaklihnl 703
Cdd:COG1123 429 DEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV-------------- 492
|
250
....*....|..
gi 52138554 704 rglqFKDPEHIY 715
Cdd:COG1123 493 ----FANPQHPY 500
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
491-690 |
2.98e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 91.59 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIF-HG 556
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENI-----LfgEKYNHQRYQHTVhvcglqKDLNSLPYGDLTEIGER-GVNLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:cd03295 91 TVEENIalvpkL--LKWPKEKIRERA------DELLALVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 631 LSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 690
Cdd:cd03295 163 FGALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1127-1348 |
3.04e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDN-TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLT 1205
Cdd:PRK13650 5 IEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1206 MIPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMAR 1276
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLENKGIPHEEMKERVneaLELVGMQDFKEREPARL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1277 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVL 1348
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1129-1340 |
3.55e-20 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 90.29 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1129 FKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdicTVGLEDLRTKLTMIP 1208
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-----GKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1209 QD-------PVL---FVGTVRYN----LDPLGSHTDEMLWHVLERTFMRDtimklpeKLQAEVTEngenFSVGERQLLCM 1274
Cdd:cd03235 75 QRrsidrdfPISvrdVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSE-------LADRQIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1275 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMeNGKVI 1340
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
490-689 |
3.84e-20 |
|
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: 90.64 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 490 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAWIFHG- 556
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENI-LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDlTEIGergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:cd03263 91 TVREHLrFYARLKGLPKSEIKEEVELLLRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 636 aHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 689
Cdd:cd03263 166 -PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
496-691 |
4.49e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.92 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSL---ISAL--LGQMQLQKGVVAVNGPLA----------YVSQQAWIF-HGNVR 559
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLeeITSGDLIVDGLKVNDPKVderlirqeagMVFQQFYLFpHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGekynhqryqhTVHVCGLQK-DLNSLPYGDLTEIG--ERG----VNLSGGQRQRISLARAVYANRQLYLLDDPLS 632
Cdd:PRK09493 96 ENVMFG----------PLRVRGASKeEAEKQARELLAKVGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 633 AVDAHVGKHVFEecIKKTL--KGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELME 691
Cdd:PRK09493 166 ALDPELRHEVLK--VMQDLaeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
499-680 |
5.06e-20 |
|
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: 93.63 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------------PLAYVSQQAWIF-HGNVRE 560
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYN--HQRYQHTVHVCglqkdlnslpygDLTEIG---ERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAV 634
Cdd:COG4148 97 NLLYGRKRAprAERRISFDEVV------------ELLGIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52138554 635 DAHVgKHvfeECIK--KTLKGKT---VVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:COG4148 165 DLAR-KA---EILPylERLRDELdipILYVSHSLDEVARlADHVVLLEQGRV 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1143-1340 |
5.30e-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: 88.25 E-value: 5.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQdpvlfvgtvryn 1221
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1222 ldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASMDSK-TDT 1300
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52138554 1301 LVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVI 1340
Cdd:cd03216 121 LFK-VIRR-LRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
462-701 |
7.10e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 7.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 462 RHVFKKQRpeLYSEQSRSDQGVASPEWQSGSP-KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV 540
Cdd:COG1134 8 ENVSKSYR--LYHEPSRSLKELLLRRRRTRREeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 541 NG----PLAYvsqqAWIFHGN--VRENILFG-------EKYNHQRYQHTVhvcglqkdlnslpygDLTEIGE------Rg 601
Cdd:COG1134 86 NGrvsaLLEL----GAGFHPEltGRENIYLNgrllglsRKEIDEKFDEIV---------------EFAELGDfidqpvK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 602 vNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvgkhvF-EECIKK----TLKGKTVVLVTHQLQFLES-CDEVILL 675
Cdd:COG1134 146 -TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA-----FqKKCLARirelRESGRTVIFVSHSMGAVRRlCDRAIWL 219
|
250 260
....*....|....*....|....*.
gi 52138554 676 EDGEICEKGTHKELMEergRYAKLIH 701
Cdd:COG1134 220 EKGRLVMDGDPEEVIA---AYEALLA 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
471-680 |
7.11e-20 |
|
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: 89.90 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 471 ELYSEQSRSDQGVASPEWQ-SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGplayvsQ 549
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 550 QAWI------FHGN--VRENILFG-------EKYNHQRYQHTVHVCGLQKDLNsLPYGdlteigergvNLSGGQRQRISL 614
Cdd:cd03220 85 VSSLlglgggFNPEltGRENIYLNgrllglsRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 615 ARAVYANRQLYLLDDPLSAVDAHvgkhvF-EECIKK----TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAA-----FqEKCQRRlrelLKQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
491-691 |
9.67e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 94.58 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLG---QMQLQKGVVAVNGP-------------LAYVSQQAW-- 552
Cdd:COG1123 16 GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMtq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 553 IFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLY 625
Cdd:COG1123 96 LNPVTVGDQIAEAlenlglsRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 626 LLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELME 691
Cdd:COG1123 165 IADEPTTALDVTTQAEILDL-LRELQRerGTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1144-1337 |
9.78e-20 |
|
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: 89.31 E-value: 9.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTK----LTMIPQDPVLFVGTVR 1219
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 YNLdPLGSHTDEMLWH-VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK- 1297
Cdd:cd03290 97 ENI-TFGSPFNKQRYKaVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 52138554 1298 TDTLVQSTIKEAFK--SCTVLTIAHRLNTVLNCDLVLVMENG 1337
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1144-1346 |
1.32e-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: 94.37 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPvlfvgtvrY 1220
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--------F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1221 N-LDP-----------LGSH--------TDEMLWHVLERTFM-RDTIMKLP-EklqaevtengenFSVGERQLLCMARAL 1278
Cdd:COG4172 373 GsLSPrmtvgqiiaegLRVHgpglsaaeRRARVAEALEEVGLdPAARHRYPhE------------FSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1279 LRNSKIILLDEATASMD-SktdtlVQSTIKEAFKSC------TVLTIAHRLNTV--LnCDLVLVMENGKVIE-------F 1342
Cdd:COG4172 441 ILEPKLLVLDEPTSALDvS-----VQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVEqgpteqvF 514
|
....
gi 52138554 1343 DKPE 1346
Cdd:COG4172 515 DAPQ 518
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1127-1340 |
1.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.15 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNT----PLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG-LEDLR 1201
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TKLTMIPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLL 1272
Cdd:PRK13633 85 NKAGMVFQNPdNQIVATiveedVAFGPENLGIPPEEIRERVdesLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1273 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLNCDLVLVMENGKVI 1340
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
189-412 |
2.01e-19 |
|
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: 90.35 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 189 YRTAIRLKVALSTLIFENLL----SFKTLThiSAGEVLNILSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTA 264
Cdd:cd18559 63 SIGGIFASRAVHLDLYHKALrspiSFFERT--PSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 265 LVGISVYLIFIPIQMFMAKLNSTFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEESFINTIHDIRKREKKLLEKAGYVQ 344
Cdd:cd18559 141 AVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLR 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 345 SGNSALAPIVSTIAIVSTFTCHIFL--KRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18559 221 ALAVRLWCVGPCIVLFASFFAYVSRhsLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
496-689 |
2.06e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P----LAYVSQQAWIF-HGNVRENIL 563
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlpPkdrnIAMVFQSYALYpHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FGEKYN-------HQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:COG3839 98 FPLKLRkvpkaeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 637 HVgKHVFEECIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:COG3839 167 KL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1127-1341 |
2.07e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.57 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLRTK 1203
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1204 LTMIPQD-PVLFVGTVRYNLD-PL---GSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMA 1275
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENVAlPLrvtGKSRKEIRRRVrevLDLVGLSDKAKALPHEL-----------SGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1276 RALLRNSKIILLDEATASMDSKTdtlvqST-IKEAFKS-----CTVLtIA-HRLNTVLNCDL-VLVMENGKVIE 1341
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPET-----SWeIMELLEEinrrgTTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1127-1351 |
2.10e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.29 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGLEDLRTKL 1204
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDP--VLFVGTV----RYNLDPLGSHTDEM---LWHVLERTFMrdtimklpEKLQAEVTengENFSVGERQLLCMA 1275
Cdd:PRK13636 85 GMVFQDPdnQLFSASVyqdvSFGAVNLKLPEDEVrkrVDNALKRTGI--------EHLKDKPT---HCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1276 RALLRNSKIILLDEATASMD----SKTDTLVQSTIKEAfkSCTVLTIAHRLNTV-LNCDLVLVMENGKVI-EFDKPEVLA 1349
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVpLYCDNVFVMKEGRVIlQGNPKEVFA 231
|
..
gi 52138554 1350 EK 1351
Cdd:PRK13636 232 EK 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
491-693 |
2.18e-19 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 88.78 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL----------AYVSQQAWIFHG---- 556
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrQLRRQIGMIFQQfnli 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 ---NVRENILFGekynhqR--YQHTVHVCglqkdLNSLPYGD-------LTEIG------ERGVNLSGGQRQRISLARAV 618
Cdd:cd03256 91 erlSVLENVLSG------RlgRRSTWRSL-----FGLFPKEEkqralaaLERVGlldkayQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 619 YANRQLYLLDDPLSAVD---AHVGKHVFEEcIKKTlKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:cd03256 160 MQQPKLILADEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1136-1350 |
2.21e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.11 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1136 YRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC--TVGLEDLRTKLTMIPQD 1210
Cdd:PRK13637 12 YMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1211 P--VLFVGTVR----YNLDPLGSHTDEMLWHVLERtfmrdtiMKLPeKLQAEVTENGENF--SVGERQLLCMARALLRNS 1282
Cdd:PRK13637 92 PeyQLFEETIEkdiaFGPINLGLSEEEIENRVKRA-------MNIV-GLDYEDYKDKSPFelSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1283 KIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 1350
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPrEVFKE 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
494-680 |
6.06e-19 |
|
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: 85.95 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG---------------- 556
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkPVTRRSPRDAIRAGiayvpedrkreglvld 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 -NVRENILfgekynhqryqhtvhvcglqkdLNSLpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:cd03215 93 lSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 52138554 636 ahVG--KHVFEECIKKTLKGKTVVLVTHQLQ-FLESCDEVILLEDGEI 680
Cdd:cd03215 137 --VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1143-1340 |
8.11e-19 |
|
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: 87.11 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEVDICTVGlEDLRTKLTMIP--QDPVLFVG 1216
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1217 -TVRYNLD----PLGSHTDEMLWHVLERTFMRDTIMKLPE--KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDE 1289
Cdd:cd03219 90 lTVLENVMvaaqARTGSGLLLARARREEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1290 ATASMDSK-TDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 1340
Cdd:cd03219 170 PAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
496-680 |
1.22e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 84.40 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHGnVRenilfgekynhqryq 574
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkEVSFASPRDARRAG-IA--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 575 hTVHvcglQkdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK-- 652
Cdd:cd03216 79 -MVY----Q--------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRaq 131
|
170 180
....*....|....*....|....*....
gi 52138554 653 GKTVVLVTHQLQ-FLESCDEVILLEDGEI 680
Cdd:cd03216 132 GVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1127-1340 |
1.23e-18 |
|
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: 86.27 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDN--TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdLRTKL 1204
Cdd:cd03266 2 ITADALTKRFRDVkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFVG-TVRYNLDPLGShtdemlWHVLERTFMRDTIMKLPEKLQAEVTEN--GENFSVGERQLLCMARALLRN 1281
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAG------LYGLKGDELTARLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1282 SKIILLDEATASMdsktDTLVQSTIKEAFKS-----CTVLTIAHRLNTVLN-CDLVLVMENGKVI 1340
Cdd:cd03266 155 PPVLLLDEPTTGL----DVMATRALREFIRQlralgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
499-693 |
1.31e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.35 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFG- 565
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppaerPVSMLFQENNLFpHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 566 ---EKYN---HQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD---- 635
Cdd:COG3840 97 rpgLKLTaeqRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 636 ---AHVGKHVFEEcikktlKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:COG3840 166 qemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1127-1356 |
1.37e-18 |
|
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: 86.59 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVlDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFvgtvrynldPlgsHtdemlWHVLERTFMRDTIMKLP-EKLQAEVTE-------NGENF--------SVGERQ 1270
Cdd:cd03295 80 VIQQIGLF---------P---H-----MTVEENIALVPKLLKWPkEKIRERADEllalvglDPAEFadryphelSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1271 LLCMARALLRNSKIILLDEATASMDSKTDTLVQS---TIKEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 1346
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEefkRLQQELGK-TIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPD 221
|
250
....*....|
gi 52138554 1347 VLAEKPDSAF 1356
Cdd:cd03295 222 EILRSPANDF 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1127-1321 |
1.44e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 84.51 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdictvgledlRTKLTM 1206
Cdd:cd03223 1 IELENLSLATPDGRVLLKD-LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVGTVRynldplgshtdEML---WhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSK 1283
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypW--------------------------DDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 52138554 1284 IILLDEATASMDSKTDTLVQSTIKEAFksCTVLTIAHR 1321
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1136-1366 |
1.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1136 YRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG-LEDLRTKLTMIPQDP-VL 1213
Cdd:PRK13644 11 YPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1214 FVG-TVRYNLdplgSHTDEMLwhVLERTFMRDTI-MKLPE-KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEA 1290
Cdd:PRK13644 90 FVGrTVEEDL----AFGPENL--CLPPIEIRKRVdRALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1291 TASMDSKTDTLVQSTIKEAF-KSCTVLTIAHRLNTVLNCDLVLVMENGKViefdkpeVLAEKPDSAFAMLLAAEVGL 1366
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKI-------VLEGEPENVLSDVSLQTLGL 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
496-692 |
1.50e-18 |
|
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: 86.14 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENIL 563
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphkrPVNTVFQNYALFpHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FG---EKYNHQRYQHTVHvcglqkdlNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:cd03300 95 FGlrlKKLPKAEIKERVA--------EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 640 KHVFEEC--IKKTLkGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:cd03300 167 KDMQLELkrLQKEL-GITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
495-700 |
1.67e-18 |
|
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: 87.22 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLgQMQLQKGVVAVNG------PL-------AYVSQQAWIFHGNVREN 561
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvPLqkwrkafGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGEKYNHQRYQHTVHVCGLQKDLNSLPyGDLT-EIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhvgk 640
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGLKSVIEQFP-GQLDfVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP---- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 641 hVFEECIKKTLK----GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 700
Cdd:cd03289 172 -ITYQVIRKTLKqafaDCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1127-1341 |
1.69e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.70 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRT-- 1202
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1203 -KLTMIPQdpvlfvgtvRYNLdpLGSHTdemlwhVLERTFMRDTIMKLP-EKLQAEVTENGE-------------NFSVG 1267
Cdd:PRK11153 82 rQIGMIFQ---------HFNL--LSSRT------VFDNVALPLELAGTPkAEIKARVTELLElvglsdkadrypaQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1268 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
496-691 |
1.82e-18 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 86.24 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P----LAYVSQQAWIF-HGNVRENIL 563
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlpPekrdISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FGEKYN-------HQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:cd03299 94 YGLKKRkvdkkeiERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 637 HVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 691
Cdd:cd03299 163 RTKEKLREE-LKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
496-682 |
1.84e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.87 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA---------------YVSQQAW-IFHGNV 558
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqDLSrlkrreipylrrrigVVFQDFRlLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENILFG---EKYNHQRYQHTVH-----VcGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVyANR-QLYLLDD 629
Cdd:COG2884 97 YENVALPlrvTGKSRKEIRRRVRevldlV-GLSDKAKALPH-----------ELSGGEQQRVAIARAL-VNRpELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 630 PLSAVDAHVGK---HVFEEcIKKTlkGKTVVLVTHQLQFLESCDE-VILLEDGEICE 682
Cdd:COG2884 164 PTGNLDPETSWeimELLEE-INRR--GTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
496-695 |
2.75e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 85.82 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL--------------AYVSQQAWIF-HGNVR 559
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGeDLtdskkdinklrrkvGMVFQQFNLFpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGekynhqryqhTVHVCGLQKDlnslpygDLTEIGER-----GV---------NLSGGQRQRISLARAVYANRQLY 625
Cdd:COG1126 96 ENVTLA----------PIKVKKMSKA-------EAEERAMEllervGLadkadaypaQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 626 LLDDPLSAVDAhvgkhvfeECIKKTLK--------GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELME----E 692
Cdd:COG1126 159 LFDEPTSALDP--------ELVGEVLDvmrdlakeGMTMVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFFEnpqhE 230
|
...
gi 52138554 693 RGR 695
Cdd:COG1126 231 RTR 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
493-680 |
2.78e-18 |
|
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: 85.02 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIF----HG-----NVRENI 562
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkPLDIAARNRIGYlpeeRGlypkmKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 L-FGE--KYNHQRYQHTVhvcglQKDLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhV 638
Cdd:cd03269 92 VyLAQlkGLKKEEARRRI-----DEWLERL---ELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-V 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 639 GKHVFEECIKKTL-KGKTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:cd03269 163 NVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1127-1352 |
3.71e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTVGLEDLRTK 1203
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1204 LTMIPQDP-VLFVGT-----VRYNLDPLGSHTDEML---WHVLERTFMRDTIMKLPeklqaevtengENFSVGERQLLCM 1274
Cdd:PRK13640 86 VGIVFQNPdNQFVGAtvgddVAFGLENRAVPRPEMIkivRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1275 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAF--KSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 1352
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
494-692 |
3.99e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.08 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVREN 561
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpaenrHVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFG---EKYNHQRYQHTVhvcglqkdLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 637
Cdd:PRK09452 107 VAFGlrmQKTPAAEITPRV--------MEALRMVQLEEFAQRKPhQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 638 VGKHVFEEcIK---KTLkGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:PRK09452 179 LRKQMQNE-LKalqRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
496-675 |
4.32e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--PLAYVSQQ---AWIFHGNVRENILFGekynh 570
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMG----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 571 qRYQHTvhvcGLQKDLN---------SLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGK 640
Cdd:NF040873 82 -RWARR----GLWRRLTrddraavddALERVGLADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 52138554 641 HVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILL 675
Cdd:NF040873 157 RIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
497-677 |
4.70e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.07 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ---KGVVAVNG------P-----LAYVSQQAWIF-HGNVREN 561
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGrrltalPaeqrrIGILFQDDLLFpHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFG--EKYNHQRYQHTVhvcglQKDLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH- 637
Cdd:COG4136 97 LAFAlpPTIGRAQRRARV-----EQALEEA---GLAGFADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAl 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52138554 638 ---VGKHVFEECIKKTLkgkTVVLVTHQLQFLESCDEVILLED 677
Cdd:COG4136 169 raqFREFVFEQIRQRGI---PALLVTHDEEDAPAAGRVLDLGN 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
500-690 |
5.35e-18 |
|
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: 87.47 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------------PLAYVSQQAWIF-HGNVREN 561
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGEK-----YNHQRYQHTVHVCGLQKDLnslpygdlteigERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:TIGR02142 96 LRYGMKrarpsERRISFERVIELLGIGHLL------------GRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 636 AHVGKHV--FEECIKKTLkGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 690
Cdd:TIGR02142 164 DPRKYEIlpYLERLHAEF-GIPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1127-1339 |
7.18e-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: 84.00 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICtvGLED-----LR 1201
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TKLTMIPQDPVLFVG-TVRYNL-------DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLC 1273
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVafalevtGVPPREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1274 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNC--DLVLVMENGKV 1339
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
494-690 |
1.12e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 84.40 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWI-FHGNVR 559
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrPLaawspwelarrrAVLPQHSSLaFPFTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGeKYNHQR-YQHTVHVCG--LQKdlnslpyGDLTEIGERGVN-LSGGQRQRISLARA-------VYANRQLYLLD 628
Cdd:COG4559 94 EVVALG-RAPHGSsAAQDRQIVReaLAL-------VGLAHLAGRSYQtLSGGEQQRVQLARVlaqlwepVDGGPRWLFLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 629 DPLSAVD-AHVgKHVFEecIKKTL--KGKTVVLVTHQL----QFlesCDEVILLEDGEICEKGTHKELM 690
Cdd:COG4559 166 EPTSALDlAHQ-HAVLR--LARQLarRGGGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
494-700 |
1.12e-17 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 84.58 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRE 560
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgK 640
Cdd:cd03288 114 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-E 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 641 HVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM-EERGRYAKLI 700
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
485-692 |
1.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 485 SPEWQSGSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------PLAYVSQQAWIFHGN 557
Cdd:PRK13644 8 SYSYPDGTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 ---------VRENILFGEKynhqryqhtvHVCGLQKDLNSLPYGDLTEIG------ERGVNLSGGQRQRISLARAVYANR 622
Cdd:PRK13644 86 petqfvgrtVEEDLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 623 QLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1143-1346 |
1.83e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 83.55 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEVDIctVGLE-DLRTKLTM-----IPQdpv 1212
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDI--TGLPpHRIARLGIartfqNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 LFVG-TVRYNLD-PLGSHTDEMLWHVLERTF--------MRDTIMKLPE--KLQAEVTENGENFSVGERQLLCMARALLR 1280
Cdd:COG0411 90 LFPElTVLENVLvAAHARLGRGLLAALLRLPrarreereARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1281 NSKIILLDEATASMDSK-TDTLVQsTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 1346
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEeTEELAE-LIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
848-1050 |
2.37e-17 |
|
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: 84.14 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 848 YQLVYIASMVSVLMFGIIKGFTFTNTTLMASSSLH------NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLP 921
Cdd:cd07346 35 LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRvvfdlrRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 922 FHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQEL-----KQVENISrspwfSHITSSIQGLG 996
Cdd:cd07346 115 SGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKAsrevrESLAELS-----AFLQESLSGIR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 997 VIHAYDKKDDCISKFKTLNDENSSHLLYfncALRWFAL---RMDILMNIVTFVVALL 1050
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLR---AARLSALfspLIGLLTALGTALVLLY 243
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1143-1353 |
2.62e-17 |
|
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: 82.72 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL-RTKLTMIPQDPVLFVG-TVRY 1220
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1221 NLDpLGSHT-------DEMLWHVLERtFMRdtimkLPEKLQAEvtenGENFSVGERQLLCMARALLRNSKIILLDEATAS 1293
Cdd:COG0410 98 NLL-LGAYArrdraevRADLERVYEL-FPR-----LKERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1294 mdsktdtLVQSTIKEafksctVLTIAHRLN----TVL----N-------CDLVLVMENGKVIEFDKPEVLAEKPD 1353
Cdd:COG0410 167 -------LAPLIVEE------IFEIIRRLNregvTILlveqNarfaleiADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1127-1339 |
3.59e-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: 81.81 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC--TVGLEDLRTKL 1204
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDpvlfvgtvrYNLDPlgsHTDemlwhVLErtfmrdTIMKLPEKLQ----AEVTENGENF---------------- 1264
Cdd:cd03262 79 GMVFQQ---------FNLFP---HLT-----VLE------NITLAPIKVKgmskAEAEERALELlekvgladkadaypaq 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1265 -SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKV 1339
Cdd:cd03262 136 lSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
494-682 |
3.90e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.93 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYV---SQQAW------IFHG-----NV 558
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqDLYQLdrkQRRAFrrdvqlVFQDspsavNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENI--LFGEKYNH----------QRYQHTVHVCGLQ-KDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLY 625
Cdd:TIGR02769 104 RMTVrqIIGEPLRHltsldeseqkARIAELLDMVGLRsEDADKLP-----------RQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 626 LLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICE 682
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKlQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
850-1051 |
4.22e-17 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 83.59 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 850 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhAE---- 925
Cdd:cd18544 45 LLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------NElfts 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 926 ---NFLQQFFMVVFILVIM-------AAVFPVVLVVLAGLAVIFLILLRIFHRGVQElkQVENISrspwfSHITSSIQGL 995
Cdd:cd18544 118 glvTLIGDLLLLIGILIAMfllnwrlALISLLVLPLLLLATYLFRKKSRKAYREVRE--KLSRLN-----AFLQESISGM 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 996 GVIHAYDKKDDCISKFKTLNDEnssHLLYFNCALRWFALRMDILMNIVTFVVALLV 1051
Cdd:cd18544 191 SVIQLFNREKREFEEFDEINQE---YRKANLKSIKLFALFRPLVELLSSLALALVL 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1127-1341 |
6.76e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.59 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLR 1201
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TKLTMIPQDpvlfvgtvrYNLdpLGSHTdemlwhV-------LErtfmrdtIMKLP-EKLQAEVTE---------NGENF 1264
Cdd:COG1135 82 RKIGMIFQH---------FNL--LSSRT------VaenvalpLE-------IAGVPkAEIRKRVAEllelvglsdKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1265 ----SVGERQLLCMARALLRNSKIILLDEATASMDSKT-----DTLVQstIKEAFKScTVLTIAHRLNTVLN-CDLVLVM 1334
Cdd:COG1135 138 psqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsilDLLKD--INRELGL-TIVLITHEMDVVRRiCDRVAVL 214
|
....*..
gi 52138554 1335 ENGKVIE 1341
Cdd:COG1135 215 ENGRIVE 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
496-662 |
6.78e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 6.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP----LAYVSQQAWIFHGN-------VRENILF 564
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLGHRNamkpaltVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 565 GEKYNHQRyQHTVHVC----GLQkDLNSLPYGdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGK 640
Cdd:PRK13539 97 WAAFLGGE-ELDIAAAleavGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AV 163
|
170 180
....*....|....*....|...
gi 52138554 641 HVFEECIKKTLK-GKTVVLVTHQ 662
Cdd:PRK13539 164 ALFAELIRAHLAqGGIVIAATHI 186
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
490-675 |
8.40e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.83 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 490 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL-------AYVSQQ----AWIfhgN 557
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvPVtgpgadrGVVFQKdallPWL---N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILFGEKYN-------HQRYQHTVHVCGLQkdlnslpygdltEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:COG4525 93 VLDNVAFGLRLRgvpkaerRARAEELLALVGLA------------DFARRRIwQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52138554 630 PLSAVDAHVGKHVFE---ECIKKTlkGKTVVLVTHQLQ---FLEScdEVILL 675
Cdd:COG4525 161 PFGALDALTREQMQElllDVWQRT--GKGVFLITHSVEealFLAT--RLVVM 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
496-708 |
1.02e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.59 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-----------LAYVSQQAWIF-HGNVRENIL 563
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHYALFrHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FGEKYNHQRYQHTVHVCGlQKDLNSLPYGDLTEIGER-GVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGK-- 640
Cdd:PRK10851 97 FGLTVLPRRERPNAAAIK-AKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKel 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 641 -----HVFEEcikktLKgKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL---------MEERGRYAKLIHNLRG 705
Cdd:PRK10851 176 rrwlrQLHEE-----LK-FTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepatrfvLEFMGEVNRLQGTIRG 249
|
...
gi 52138554 706 LQF 708
Cdd:PRK10851 250 GQF 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1143-1351 |
1.99e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVG-TVR-- 1219
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 --YNLDPLGSH------TDEMLwhvLERTFMRDTIMKLPEKLqaeVTEngenFSVGERQLLCMARALLRNSKIILLDEAT 1291
Cdd:PRK11231 97 vaYGRSPWLSLwgrlsaEDNAR---VNQAMEQTRINHLADRR---LTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1292 ASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAEK 1351
Cdd:PRK11231 167 TYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPeEVMTPG 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1126-1366 |
2.37e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1126 EITFKDYRMRYRDNTPLVLDGL---NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVG-----L 1197
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFERRALydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI-TAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1198 EDLRTKLTMIPQDP--VLFVGTVRYNL--DPLG---------SHTDEMLWHVlertfmrdtimKLPEKLqaeVTENGENF 1264
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEKDIcfGPMNfgvseedakQKAREMIELV-----------GLPEEL---LARSPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1265 SVGERQLLCMARALLRNSKIILLDEATASMDSKTdtlvQSTIKEAF------KSCTVLTIAHRLNTVLN-CDLVLVMENG 1337
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 52138554 1338 KVIE-------FDKPEVLAEK----PDSA-FAMLLAAEVGL 1366
Cdd:PRK13634 223 TVFLqgtpreiFADPDELEAIgldlPETVkFKRALEEKFGI 263
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1127-1346 |
2.43e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:PRK09536 4 IDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVL-FVGTVRY-----------NLDPLGShTDEMlwhVLERTFMRDTIMKLPEKlqaEVTEngenFSVGERQLLCM 1274
Cdd:PRK09536 82 VPQDTSLsFEFDVRQvvemgrtphrsRFDTWTE-TDRA---AVERAMERTGVAQFADR---PVTS----LSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1275 ARALLRNSKIILLDEATASMD----SKTDTLVQSTIKEAFkscTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 1346
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDinhqVRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPA 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
494-700 |
2.45e-16 |
|
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: 85.35 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLgQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRE 560
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIFSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGK 640
Cdd:TIGR01271 1311 NLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTL 1389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 641 HVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 700
Cdd:TIGR01271 1390 QIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
496-689 |
2.88e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV----NGPLAYVSQQAW------------------- 552
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITnpyskkiknfkelrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 553 --------IFHGNVRENILFG------EKYN-HQRYQHTVHVCGLQKD-LNSLPYGdlteigergvnLSGGQRQRISLAR 616
Cdd:PRK13631 121 vfqfpeyqLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 617 AVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1143-1341 |
3.07e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.50 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLRTKLTMIPQDPVLFVG--- 1216
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSISAVNprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1217 TVRY----------NLDPLG--SHTDEMLWHVlertFMRDTIM-KLPEKLqaevtengenfSVGERQLLCMARALLRNSK 1283
Cdd:PRK10419 107 TVREiireplrhllSLDKAErlARASEMLRAV----DLDDSVLdKRPPQL-----------SGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 1284 IILLDEATASMDSKTDTLVQSTIKE-------AFksctvLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKlqqqfgtAC-----LFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1143-1340 |
3.39e-16 |
|
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: 78.36 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIIIDEVDIctvGLEDLRTKLTMIPQDPVLFVG-TVR 1219
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 ynldplgshtdEMLWHVLErtfMRdtimklpeklqaevtengeNFSVGERQLLCMARALLRNSKIILLDEATASMDSKTD 1299
Cdd:cd03213 101 -----------ETLMFAAK---LR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 1300 TLVQSTIKE-AFKSCTVLTIAHRLNTVL--NCDLVLVMENGKVI 1340
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
512-692 |
4.77e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 81.00 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 512 ICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFGEKYNHQ-RYQHTVH 578
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvpphlrHINMVFQSYALFpHMTVEENVAFGLKMRKVpRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 579 VcglqkdLNSLPYGDLTEIGERG-VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECikKTLK---GK 654
Cdd:TIGR01187 81 V------LEALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL--KTIQeqlGI 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 52138554 655 TVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:TIGR01187 153 TFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
492-684 |
6.50e-16 |
|
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: 78.18 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 492 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAyVSQQAWIFHGN-------- 557
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkePAE-ARRRLGFVSDStglydrlt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYGDlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:cd03266 95 ARENLEyFAGLYGLKGDELTARLEELADRLGMEELLD-----RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 52138554 637 HVGKHVFEecIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 684
Cdd:cd03266 170 MATRALRE--FIRQLRalGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1143-1341 |
6.72e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVgLEDLRTKLTMIPQDPVLFVG-TVR 1219
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFRSP-RDAQAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 YNLdplgshtdeML------WHVLERTFMRDTIMKLPEKLQAEV--TENGENFSVGERQLLCMARALLRNSKIILLDEAT 1291
Cdd:COG1129 98 ENI---------FLgreprrGGLIDWRAMRRRARELLARLGLDIdpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1292 ASMDSK-TDTLVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:COG1129 169 ASLTEReVERLFR-IIRR-LKAqgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
488-680 |
7.37e-16 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 78.24 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA----------WIF-- 554
Cdd:COG4181 19 GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqDLFALDEDArarlrarhvgFVFqs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 -----HGNVRENI-----LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQL 624
Cdd:COG4181 99 fqllpTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 625 YLLDDPLSAVDAHVGKHV----FEecIKKTlKGKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:COG4181 168 LFADEPTGNLDAATGEQIidllFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
494-691 |
8.57e-16 |
|
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: 78.35 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------P--------LAYVSQQAWIFHG-NV 558
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklPmhkrarlgIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENIL-------FGEKYNHQRYQHTVHVCGLQKDLNSLpygdlteigerGVNLSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:cd03218 93 EENILavleirgLSKKEREEKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 632 SAVDAhvgKHVFE-ECIKKTLKGKTV-VLVT-HQL-QFLESCDEVILLEDGEICEKGTHKELME 691
Cdd:cd03218 162 AGVDP---IAVQDiQKIIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
496-690 |
8.93e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 8.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP--------------------------LAYVSQ 549
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlkvadknqlrllrtrLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 550 QAWIF-HGNVRENILfgekynhqryQHTVHVCGLQKDL---NSLPYGDLTEIGERG-----VNLSGGQRQRISLARAVYA 620
Cdd:PRK10619 100 HFNLWsHMTVLENVM----------EAPIQVLGLSKQEareRAVKYLAKVGIDERAqgkypVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 621 NRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 690
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1137-1308 |
9.36e-16 |
|
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: 77.52 E-value: 9.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1137 RDNTPLvLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTMIPQDPVLFVG 1216
Cdd:COG4133 12 RGERLL-FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1217 -TVRYNLDPL-----GSHTDEMLWHVLERtfmrdtiMKLPEKLQAEVtengENFSVGERQLLCMARALLRNSKIILLDEA 1290
Cdd:COG4133 90 lTVRENLRFWaalygLRADREAIDEALEA-------VGLAGLADLPV----RQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170
....*....|....*...
gi 52138554 1291 TASMDSKTDTLVQSTIKE 1308
Cdd:COG4133 159 FTALDAAGVALLAELIAA 176
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1135-1342 |
9.91e-16 |
|
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: 77.62 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNtpLVLDGLNLNIQSGQTvGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVGLEDLRTKLTMIPQDPVLF 1214
Cdd:cd03264 9 RYGKK--RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1215 VG-TVRYNLDPLG-------SHTDEMLWHVLERTFMRDtimKLPEKLQAevtengenFSVGERQLLCMARALLRNSKIIL 1286
Cdd:cd03264 85 PNfTVREFLDYIAwlkgipsKEVKARVDEVLELVNLGD---RAKKKIGS--------LSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1287 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV-LNCDLVLVMENGKVIEF 1342
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
494-678 |
1.08e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGV-----VAVNGPLA---YVSQQ----AWIfhgNVREN 561
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgKPVEGPGAergVVFQNegllPWR---NVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGEKY----NHQRyqhtvhvcgLQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:PRK11248 91 VAFGLQLagveKMQR---------LEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 52138554 637 HVGKHVFEECIK---KTlkGKTVVLVTHQLQ---FLEScdEVILLEDG 678
Cdd:PRK11248 162 FTREQMQTLLLKlwqET--GKQVLLITHDIEeavFMAT--ELVLLSPG 205
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
494-692 |
1.09e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.20 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQawifhgN--- 557
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQE------Nhin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 ----VRENILFGekynhqRYQHT---------VHVcglqkDlNSLPYGDLTEIGERGVN-LSGGQRQRISLArAVYANRQ 623
Cdd:COG4604 88 srltVRELVAFG------RFPYSkgrltaedrEII-----D-EAIAYLDLEDLADRYLDeLSGGQRQRAFIA-MVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 624 LY-LLDDPLSAVDAhvgKHVFEecIKKTLK------GKTVVLVTHQLQFlESC--DEVILLEDGEICEKGTHKELMEE 692
Cdd:COG4604 155 DYvLLDEPLNNLDM---KHSVQ--MMKLLRrladelGKTVVIVLHDINF-ASCyaDHIVAMKDGRVVAQGTPEEIITP 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
494-693 |
1.32e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.13 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHG-NVR 559
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGEK-YNH------QRYQHTVHVcGLQKDlnslpygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:PRK11231 95 ELVAYGRSpWLSlwgrlsAEDNARVNQ-AMEQT-------RINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 632 SAVDAHvgkHVFEecIKKTL-----KGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:PRK11231 167 TYLDIN---HQVE--LMRLMrelntQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
496-691 |
1.64e-15 |
|
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: 77.33 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVSQQAWIFHG-NVRE 560
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpPhriarlgIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGekynhqryqhtvhvCGLQKDLNSLPyGDLTEI-------GER----GVNLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:COG0410 98 NLLLG--------------AYARRDRAEVR-ADLERVyelfprlKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 630 P---LSAVdahVGKHVFeECIKKtLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELME 691
Cdd:COG0410 163 PslgLAPL---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
488-676 |
1.67e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGspKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP----------LAYVSQQA---WIF 554
Cdd:PRK15056 16 WRNG--HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 HGNVRENILFGeKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSA 633
Cdd:PRK15056 94 PVLVEDVVMMG-RYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 634 VDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLE 676
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTVMVK 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1127-1341 |
1.71e-15 |
|
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: 77.13 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTP--LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGledlrTKL 1204
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFvgtvrynldPlgshtdemlWhvleRTfMRDTIMkLPEKLQ----AEVTENGENF---------------- 1264
Cdd:cd03293 76 GYVFQQDALL---------P---------W----LT-VLDNVA-LGLELQgvpkAEARERAEELlelvglsgfenayphq 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1265 -SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLN-TVLNCDLVLVMEN--GK 1338
Cdd:cd03293 132 lSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGR 211
|
...
gi 52138554 1339 VIE 1341
Cdd:cd03293 212 IVA 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1144-1353 |
2.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDP-VLFVGT----- 1217
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGAtvedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1218 VRYNLDPLGSHTDEMLWHVLERTF---MRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASM 1294
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLavnMLDFKTREPARL-----------SGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1295 DSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP-EVLAEKPD 1353
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPsELFATSED 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
496-662 |
2.24e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.24 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA-----YVSQQAWIFHGN-------VRENI 562
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtPLAeqrdePHENILYLGHLPglkpelsALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFgekYN--HQRYQHTVHvcglqkdlNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvG 639
Cdd:TIGR01189 95 HF---WAaiHGGAQRTIE--------DALAAVGLTGFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-G 162
|
170 180
....*....|....*....|....
gi 52138554 640 KHVFEECIKKTL-KGKTVVLVTHQ 662
Cdd:TIGR01189 163 VALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1144-1350 |
2.34e-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: 80.62 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII----DEVDICTVGLeDLRTKLT----MIPQDPVLFv 1215
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigILHQEYDLY- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1216 gTVRYNLDPLgshTDEMLWHVLERTFMRDTIMKL-----PEKLQAEVTEN-GENFSVGERQLLCMARALLRNSKIILLDE 1289
Cdd:TIGR03269 378 -PHRTVLDNL---TEAIGLELPDELARMKAVITLkmvgfDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1290 ATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 1350
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPeEIVEE 518
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
488-675 |
2.51e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.68 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSPKsVLHNISFVVRKGKVLGICGNVGSGKS-------SLISALLGQMQLQKGVVAVNGPLAY---VS---QQAWIF 554
Cdd:PRK10247 15 YLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKStllkivaSLISPTSGTLLFEGEDISTLKPEIYrqqVSycaQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 HGNVRENILFGEKYNHQRYQHTVHVCGLQKdlnslpYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSA 633
Cdd:PRK10247 94 GDTVYDNLIFPWQIRNQQPDPAIFLDDLER------FALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 634 VDAHvGKHVFEECIKK--TLKGKTVVLVTHQLQFLESCDEVILL 675
Cdd:PRK10247 168 LDES-NKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-691 |
2.62e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.75 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGpLAYVSQQAW--------IFHG--------NVRE 560
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmVFQNpdnqfvgaTVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKyNHQ--------RYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLS 632
Cdd:PRK13635 102 DVAFGLE-NIGvpreemveRVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 633 AVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 691
Cdd:PRK13635 170 MLDPRGRREVLE--TVRQLKeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
850-1017 |
2.63e-15 |
|
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: 78.21 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 850 LVYIASMVsvlmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlpfhaeNFLQ 929
Cdd:cd18547 53 GLYLLSAL----FSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNIS--------QALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 930 Q--------FFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLRIFHRgVQEL--KQVENISRspWFSHITSSIQGLGVI 998
Cdd:cd18547 121 QsltqlissILTIVGTLIMMLYIsPLLTLIVLVTVPLSLLVTKFIAKR-SQKYfrKQQKALGE--LNGYIEEMISGQKVV 197
|
170
....*....|....*....
gi 52138554 999 HAYDKKDDCISKFKTLNDE 1017
Cdd:cd18547 198 KAFNREEEAIEEFDEINEE 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1127-1340 |
3.69e-15 |
|
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: 75.99 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDnTPLVLDglnLNIQSGQTVGIVGRTGSGKSSLG--MALFRLvePASGTIIIDEVDICTvgLEDLRTKL 1204
Cdd:cd03298 1 VRLDKIRFSYGE-QPMHFD---LTFAQGEITAIVGPSGSGKSTLLnlIAGFET--PQSGRVLINGVDVTA--APPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQDPVLFVG-TVRYNLD----P---LGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMAR 1276
Cdd:cd03298 73 SMLFQENNLFAHlTVEQNVGlglsPglkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1277 ALLRNSKIILLDEATASMD----SKTDTLVQSTIKEafKSCTVLTIAHRLNTVLNC-DLVLVMENGKVI 1340
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
494-682 |
4.43e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW-IFHGNVRenILFGEKYNHQ 571
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGePLAKLNRAQRkAFRRDIQ--MVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 572 RYQHTV---------HVCGLQK-----------DLNSLPYGDLTEigeRGVNLSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:PRK10419 103 NPRKTVreiireplrHLLSLDKaerlarasemlRAVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 632 SAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGEICE 682
Cdd:PRK10419 180 SNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1130-1337 |
5.27e-15 |
|
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: 75.93 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1130 KDYRMRYRDNTPL-VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID----EVDICTVG---LEDLR 1201
Cdd:COG4778 12 KTFTLHLQGGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TK--------LTMIPQdpvlfVGTVRYNLDPLgshtdemlwhvLERTFMRD----------TIMKLPEKL--QAEVTeng 1261
Cdd:COG4778 92 RRtigyvsqfLRVIPR-----VSALDVVAEPL-----------LERGVDREearararellARLNLPERLwdLPPAT--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1262 enFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAfKS--CTVLTIAHRLNTVLN-CDLVLVMENG 1337
Cdd:COG4778 153 --FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KArgTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
494-695 |
5.43e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.33 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL------------LGQMQL--------QKGVV-AVNGPLAYVSQQAW 552
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIdtarslsqQKGLIrQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 553 IF-HGNVRENILFG--------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQ 623
Cdd:PRK11264 96 LFpHRTVLENIIEGpvivkgepKEEATARARELLAKVGLAGKETSYPR-----------RLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 624 LYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELM----EERGR 695
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFadpqQPRTR 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
884-1289 |
5.51e-15 |
|
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: 79.84 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 884 RVFNKIVRSPMSFFDTTPTGRLMNRFSKDMD---ELDVRLPFhaenFLQQFFMVVFILVIMA----AVFPVVLVVLAGLA 956
Cdd:COG4615 86 RLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE----LLQSVALVLGCLAYLAwlspPLFLLTLVLLGLGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 957 VIFLILLRIFHRGVQELKQVENIsrspWFSHITSSIQG---LGvIHAyDKKDD--------CISKFKtlnDENSSHLLYF 1025
Cdd:COG4615 162 AGYRLLVRRARRHLRRAREAEDR----LFKHFRALLEGfkeLK-LNR-RRRRAffdedlqpTAERYR---DLRIRADTIF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1026 NCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSkgLSLSYIIQ-LSGLL---------QVCVRTGTETQAKFTSAE 1095
Cdd:COG4615 233 ALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFV--LVLLFLRGpLSQLVgalptlsraNVALRKIEELELALAAAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1096 llreyiltcvpEHTHPFKVGTCPKDWpsrGEITFKDYRMRYR---DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGM 1172
Cdd:COG4615 311 -----------PAAADAAAPPAPADF---QTLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1173 ALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFvgtvRYNLDPLGSHTDEMLWHVLERtfmrdtiMKLPEK 1252
Cdd:COG4615 377 LLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLER-------LELDHK 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 52138554 1253 LQAevtENGE----NFSVGERQLLCMARALLRNSKIILLDE 1289
Cdd:COG4615 446 VSV---EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1125-1356 |
6.15e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.81 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSL-----GmalfrLVEPASGTIIIDEVDIctvglED 1199
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV-----TD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTK---LTMIPQDPVLFVG-TVRYNLD-PL------GSHTDEMLWHVLErtfmrdtIMKLPEKLQAEVTEngenFSVGE 1268
Cdd:COG3839 70 LPPKdrnIAMVFQSYALYPHmTVYENIAfPLklrkvpKAEIDRRVREAAE-------LLGLEDLLDRKPKQ----LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1269 RQLLCMARALLRNSKIILLDEATASMDSKtdtL-VQ--STIKE---AFKSCTV---------LTIAHRlntvlncdlVLV 1333
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAK---LrVEmrAEIKRlhrRLGTTTIyvthdqveaMTLADR---------IAV 206
|
250 260
....*....|....*....|...
gi 52138554 1334 MENGKVIEFDKPEVLAEKPDSAF 1356
Cdd:COG3839 207 MNDGRIQQVGTPEELYDRPANLF 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1130-1353 |
6.75e-15 |
|
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: 75.66 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1130 KDYRMRYrdntplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvgledlrTKLTM--- 1206
Cdd:cd03218 8 KRYGKRK------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---------TKLPMhkr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 -------IPQDPVLFVG-TVRYNLDPlgshtdemlwhVLErtfmrdtIMKLPEKLQAEVTE--------------NGENF 1264
Cdd:cd03218 73 arlgigyLPQEASIFRKlTVEENILA-----------VLE-------IRGLSKKEREEKLEelleefhithlrksKASSL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1265 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 1342
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAE 214
|
250
....*....|.
gi 52138554 1343 DKPEVLAEKPD 1353
Cdd:cd03218 215 GTPEEIAANEL 225
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1143-1353 |
7.89e-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: 76.43 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQDPVLFVGTVRYNL 1222
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1223 dPLGSHTDEMLW-HVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDtl 1301
Cdd:cd03291 119 -IFGVSYDEYRYkSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE-- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1302 vqstiKEAFKSC--------TVLTIAHRLNTVLNCDLVLVMENGKVIEFDK-PEVLAEKPD 1353
Cdd:cd03291 196 -----KEIFESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTfSELQSLRPD 251
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
494-692 |
9.07e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG------------NVRE 560
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvPVPARARLARARIGvvpqfdnldlefTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NIL-FGekynhqRY--QHTVHVCGLQKDLnsLPYGDL-TEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:PRK13536 134 NLLvFG------RYfgMSTREIEAVIPSL--LEFARLeSKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 637 HvGKHVFEECIKKTL-KGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 692
Cdd:PRK13536 206 H-ARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1143-1340 |
9.15e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.89 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvgledlrTKLT------MIP---QDPVL 1213
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---------TKLPeykrakYIGrvfQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1214 fvGT-----VRYNL---------DPLGshtdemlWHVL--ERTFMRDTI----MKLPEKLQAEVtengENFSVGERQLLC 1273
Cdd:COG1101 92 --GTapsmtIEENLalayrrgkrRGLR-------RGLTkkRRELFRELLatlgLGLENRLDTKV----GLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1274 MARALLRNSKIILLDEATASMDSKTDTLV----QSTIKEafKSCTVLTIAHRLNTVLNC-DLVLVMENGKVI 1340
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEE--NNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
494-679 |
9.47e-15 |
|
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: 72.87 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV--NGPLAYVSQqawifhgnvrenilfgekynhq 571
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 572 ryqhtvhvcglqkdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKtL 651
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEEALKE-Y 116
|
170 180
....*....|....*....|....*....
gi 52138554 652 KGkTVVLVTHQLQFLES-CDEVILLEDGE 679
Cdd:cd03221 117 PG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1136-1334 |
9.72e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.14 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1136 YRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFV 1215
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1216 GTVRYNLdplgshtdEMLWHV----LERTFMRDTIMK--LPEKLqaeVTENGENFSVGERQLLcmarALLRN----SKII 1285
Cdd:PRK10247 95 DTVYDNL--------IFPWQIrnqqPDPAIFLDDLERfaLPDTI---LTKNIAELSGGEKQRI----SLIRNlqfmPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1286 LLDEATASMDSKTDTLVQSTIKEAF--KSCTVLTIAHRLNTVLNCDLVLVM 1334
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
488-717 |
9.78e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 76.36 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------------PLAYVS 548
Cdd:PRK13646 12 YQKGTPyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 549 Q--QAWIFHGNVRENILFGEKynhqRYQHTVhvcglqKDLNSLPYGDLTEIG-ERGV------NLSGGQRQRISLARAVY 619
Cdd:PRK13646 92 QfpESQLFEDTVEREIIFGPK----NFKMNL------DEVKNYAHRLLMDLGfSRDVmsqspfQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 620 ANRQLYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRY 696
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
250 260
....*....|....*....|....
gi 52138554 697 AKL---IHNLRGLQfKDPEHIYNV 717
Cdd:PRK13646 241 ADWhigLPEIVQLQ-YDFEQKYQT 263
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
504-684 |
1.07e-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: 74.45 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 504 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFGE----K 567
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFaHLTVEQNVGLGLspglK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 568 YNHQRyQHTVHVC----GLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD----AHVG 639
Cdd:cd03298 101 LTAED-RQAIEVAlarvGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52138554 640 KHVFEECIKktlKGKTVVLVTHQLQFLESCDE-VILLEDGEICEKG 684
Cdd:cd03298 169 DLVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1124-1341 |
1.08e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.33 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1124 RGEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICTVGLE 1198
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1199 DLRTKLTMIPQDPvlfvgtvrynlDPLGSHTdemLWHVLERTFMRDTIMKLPEKLQAEVTENGE---------------- 1262
Cdd:PRK14247 79 ELRRRVQMVFQIP-----------NPIPNLS---IFENVALGLKLNRLVKSKKELQERVRWALEkaqlwdevkdrldapa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1263 -NFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAH------RLNtvlncDLVLVME 1335
Cdd:PRK14247 145 gKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLY 219
|
....*.
gi 52138554 1336 NGKVIE 1341
Cdd:PRK14247 220 KGQIVE 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
494-685 |
1.41e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.19 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWI-FHGNVR 559
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrPLadwspaelarrrAVLPQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGekynhqRYQHTvhvcGLQKDLNSLPYG-----DLTEIGERGV-NLSGGQRQRISLARA------VYANRQLYLL 627
Cdd:PRK13548 95 EVVAMG------RAPHG----LSRAEDDALVAAalaqvDLAHLAGRDYpQLSGGEQQRVQLARVlaqlwePDGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 628 DDPLSAVD-AHvGKHVFEecIKKTL---KGKTVVLVTHQL----QFlesCDEVILLEDGEICEKGT 685
Cdd:PRK13548 165 DEPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1130-1346 |
1.47e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.69 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1130 KDYRMRYR--DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTV---GLEDLR 1201
Cdd:PRK09473 16 KDLRVTFStpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLpekELNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 T-KLTMIPQDPVLfvgtvryNLDPLgSHTDEMLWHVL-------------ERTFMRDTImKLPEKLQaEVTENGENFSVG 1267
Cdd:PRK09473 96 AeQISMIFQDPMT-------SLNPY-MRVGEQLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARK-RMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1268 ERQLLCMARALLRNSKIILLDEATASMdsktDTLVQSTI-------KEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKV 1339
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTAL----DVTVQAQImtllnelKREFNT-AIIMITHDLGVVAGiCDKVLVMYAGRT 240
|
....*..
gi 52138554 1340 IEFDKPE 1346
Cdd:PRK09473 241 MEYGNAR 247
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
480-680 |
1.52e-14 |
|
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: 74.61 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 480 DQGVASPEWqsGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK---GVVAVNG-PL---------AY 546
Cdd:cd03234 8 DVGLKAKNW--NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGqPRkpdqfqkcvAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 547 VSQQ-AWIFHGNVRENILF------GEKYNHQRYQHTVHVCGLqKDLNSLPYGdlteiGERGVNLSGGQRQRISLARAVY 619
Cdd:cd03234 86 VRQDdILLPGLTVRETLTYtailrlPRKSSDAIRKKRVEDVLL-RDLALTRIG-----GNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 620 ANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ-----LQFLescDEVILLEDGEI 680
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
837-1017 |
1.59e-14 |
|
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: 76.01 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 837 DQTLQDTKHHMYQLVYI------ASMVSVLMFGIIKGFTftNTTLMA--SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNR 908
Cdd:cd18563 28 DVLIQLGPGGNTSLLLLlvlglaGAYVLSALLGILRGRL--LARLGEriTADLRRDLYEHLQRLSLSFFDKRQTGSLMSR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 909 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIM---------AAVFPVVLVVLaGLAVIFLILLRIFHRgvqelkqvenI 979
Cdd:cd18563 106 VTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLfslnwklalLVLIPVPLVVW-GSYFFWKKIRRLFHR----------Q 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 52138554 980 SRSpWF---SHITSSIQGLGVIHAYDKKDDCISKFKTLNDE 1017
Cdd:cd18563 175 WRR-WSrlnSVLNDTLPGIRVVKAFGQEKREIKRFDEANQE 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1148-1352 |
1.76e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1148 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR----TKLTMIPQDPVLF-----VGTV 1218
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMphmtvLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1219 RYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD 1295
Cdd:PRK10070 128 AFGMELAGinaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1296 SKTDTLVQSTIK--EAFKSCTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKP 1352
Cdd:PRK10070 197 PLIRTEMQDELVklQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
499-689 |
1.77e-14 |
|
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: 73.94 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAWIFHG-NVRENI-LF 564
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 565 GEKYNHQRYQHTvhvcglQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF 643
Cdd:cd03265 98 ARLYGVPGAERR------ERIDELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 52138554 644 EEcIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 689
Cdd:cd03265 172 EY-IEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1148-1356 |
2.18e-14 |
|
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: 74.99 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1148 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL----RTKLTMIPQDPVLF-----VGTV 1218
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLphrtvLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1219 RYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD 1295
Cdd:cd03294 124 AFGLEVQGvprAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 1296 SKTDTLVQSTI----KEAFKscTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKPDSAF 1356
Cdd:cd03294 193 PLIRREMQDELlrlqAELQK--TIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
501-680 |
2.31e-14 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 73.74 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 501 SFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFG--- 565
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqshtglapyqrPVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 566 -EKYNHQRYQHTVHVC---GLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 641
Cdd:TIGR01277 98 gLKLNAEQQEKVVDAAqqvGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52138554 642 VFeeCIKKTL---KGKTVVLVTHQLQFL-ESCDEVILLEDGEI 680
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDArAIASQIAVVSQGKI 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
496-685 |
2.80e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.88 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGqmqLQK---GVVAVNG-PLAYVSQQAW---------IF-HGN---- 557
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsGSVLVDGvDLTALSERELraarrkigmIFqHFNllss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 --VRENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLD 628
Cdd:COG1135 97 rtVAENVALpleiagvPKAEIRKRVAELLELVGLSDKADAYP-----------SQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 629 DPLSAVDAHVGKHVFE---EcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 685
Cdd:COG1135 166 EATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1127-1348 |
2.87e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.82 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 1199
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQDP--VLFVGTV-----------RYNLDPLGSHTDEMLwhvLERTFMRDTIMKLPEKLqaevtengenfSV 1266
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVereiifgpknfKMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQM-----------SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1267 GERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 1343
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQT 228
|
....*
gi 52138554 1344 KPEVL 1348
Cdd:PRK13646 229 SPKEL 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1127-1353 |
2.95e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLV---LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC----TVGLED 1199
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQDP--VLFVGTV----RYNLDPLGSHTDE-----MLWhvLERTFMRDTIM-KLPEKLqaevtengenfSVG 1267
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVlkdvEFGPKNFGFSEDEakekaLKW--LKKVGLSEDLIsKSPFEL-----------SGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1268 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 1345
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGhTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
....*...
gi 52138554 1346 EVLAEKPD 1353
Cdd:PRK13641 230 KEIFSDKE 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1140-1353 |
3.01e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 78.41 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1140 TPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQDPVLFVGTVR 1219
Cdd:TIGR01271 439 TP-VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 YNLdPLGSHTDEMLW-HVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKT 1298
Cdd:TIGR01271 505 DNI-IFGLSYDEYRYtSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1299 DtlvqstiKEAFKSC--------TVLTIAHRLNTVLNCDLVLVMENGKVIEFDK-PEVLAEKPD 1353
Cdd:TIGR01271 584 E-------KEIFESClcklmsnkTRILVTSKLEHLKKADKILLLHEGVCYFYGTfSELQAKRPD 640
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
495-684 |
3.78e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWI-FHGNVRE 560
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGekynhqRYQHTVHVCGLQKD-----LNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAV 634
Cdd:PRK09536 97 VVEMG------RTPHRSRFDTWTETdraavERAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 52138554 635 DAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 684
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
496-685 |
5.17e-14 |
|
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: 73.24 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVSQQAWIFHG-NVRE 560
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglpPheiarlgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGV------NLSGGQRQRISLARAVYANRQLYLLDDP---L 631
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLadrpagELSYGQQRRLEIARALATDPKLLLLDEPaagL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 632 SAVDAHVGKHVFEEcIKKtlKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 685
Cdd:cd03219 175 NPEETEELAELIRE-LRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1154-1364 |
6.26e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1154 GQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPVLFVG---TVRYN-LDPLG 1226
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYASLDprqTVGDSiMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1227 SH--------TDEMLWhVLERTFMRdtimklPEKLQAEVTEngenFSVGERQLLCMARALLRNSKIILLDEATASMDSKT 1298
Cdd:PRK10261 430 VHgllpgkaaAARVAW-LLERVGLL------PEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1299 ---------DTLVQSTIKEAFKS---CTVLTIAHRlntvlncdlVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 1364
Cdd:PRK10261 499 rgqiinlllDLQRDFGIAYLFIShdmAVVERISHR---------VAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1126-1358 |
7.80e-14 |
|
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: 72.76 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1126 EITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLT 1205
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1206 MipQDPVLFVG-TVRYNL------DPLGSHTDEMLwhvlertfMRDTIMKLPEKLQAEVTENG--ENFSVGERQLLCMAR 1276
Cdd:cd03296 80 F--QHYALFRHmTVFDNVafglrvKPRSERPPEAE--------IRAKVHELLKLVQLDWLADRypAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1277 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTI--AHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 1353
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
....*
gi 52138554 1354 SAFAM 1358
Cdd:cd03296 230 SPFVY 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
547-700 |
8.35e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 547 VSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLY 625
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 626 LLDDPLSAVDAHVgkhvfEECIKKTL------KGKTVVLVTHQLQFLESCDEVILLEDGE-----ICEKGTHKELME-ER 693
Cdd:PTZ00265 1381 LLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQD 1455
|
....*..
gi 52138554 694 GRYAKLI 700
Cdd:PTZ00265 1456 GVYKKYV 1462
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
494-680 |
9.24e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.79 E-value: 9.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKG-VVAVNGPLAYVS-------QQA----WifhGNVREN 561
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGeLLAGTAPLAEARedtrlmfQDArllpW---KKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGEKYN-HQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGK 640
Cdd:PRK11247 102 VGLGLKGQwRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52138554 641 HVFEECIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEI 680
Cdd:PRK11247 170 IEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1145-1341 |
9.88e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.97 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1145 DGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII---DEVDICTVGLEDLRTKLTMIPQDPVLfvgtvryN 1221
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDPLA-------S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1222 LDP---LGSHTDEMLwhvleRTFM----RDTIMklpEKLQAEVTENG----------ENFSVGERQLLCMARALLRNSKI 1284
Cdd:PRK15079 111 LNPrmtIGEIIAEPL-----RTYHpklsRQEVK---DRVKAMMLKVGllpnlinrypHEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1285 ILLDEATASMD----SKTDTLVQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK15079 183 IICDEPVSALDvsiqAQVVNLLQQLQREMGLS--LIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1131-1349 |
1.02e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1131 DYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII--DEVDICTVGLEDLRTKLTMIP 1208
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1209 QDP---VLFV---GTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAevtengenFSVGERQLLCMARALLRNS 1282
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1283 KIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLA 1349
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPgEVFA 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
494-691 |
1.07e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG------------NVRE 560
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGePVPSRARHARQRVGvvpqfdnldpdfTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NIL-FGEKYNHQRYQHTVHVCGLqkdlnsLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHv 638
Cdd:PRK13537 100 NLLvFGRYFGLSAAAARALVPPL------LEFAKLENKADAKVgELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 639 GKHVFEECIKKTL-KGKTVVLVTHqlqFLES----CDEVILLEDGEICEKGTHKELME 691
Cdd:PRK13537 173 ARHLMWERLRSLLaRGKTILLTTH---FMEEaerlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
497-680 |
1.10e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 71.67 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA----------------WIFHGNVR 559
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLS 632
Cdd:cd03292 97 ENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 52138554 633 AVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDE-VILLEDGEI 680
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
793-1053 |
1.14e-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: 73.23 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 793 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQvvcasqnnktacnvdqtlqdtKHHMYQLVYIASMVsVLMFgIIKG-FTFT 871
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIFV---------------------EKDLEALLLVPLAI-IGLF-LLRGlASYL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 872 NTTLMASSSLH------NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVF 945
Cdd:cd18552 59 QTYLMAYVGQRvvrdlrNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 946 PV-VLVVLAGLAVIFLILLRI------FHRGVQElkQVENISrspwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEN 1018
Cdd:cd18552 139 WKlTLIALVVLPLAALPIRRIgkrlrkISRRSQE--SMGDLT-----SVLQETLSGIRVVKAFGAEDYEIKRFRKANERL 211
|
250 260 270
....*....|....*....|....*....|....*
gi 52138554 1019 sshllyfncalRWFALRMDILMNIVTFVVALLVTL 1053
Cdd:cd18552 212 -----------RRLSMKIARARALSSPLMELLGAI 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
493-684 |
1.14e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAW---------IFHG------- 556
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLlpvrhriqvVFQDpnsslnp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 --NVRENILFGEKYNH------QRYQHTVHVcglqkdlnslpygdLTEIG-------ERGVNLSGGQRQRISLARAVYAN 621
Cdd:PRK15134 378 rlNVLQIIEEGLRVHQptlsaaQREQQVIAV--------------MEEVGldpetrhRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 622 RQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILLEDGEICEKG 684
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILA--LLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
499-715 |
1.27e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.10 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFGE 566
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshvppyqrPINMMFQSYALFpHMTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 567 KYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDahvg 639
Cdd:PRK11607 117 KQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 640 khvfeecikKTLKGKTvvlvthQLQFLEscdevILLEDGEICEKGTH--KELMEERGRYAklIHNlRG--LQFKDPEHIY 715
Cdd:PRK11607 182 ---------KKLRDRM------QLEVVD-----ILERVGVTCVMVTHdqEEAMTMAGRIA--IMN-RGkfVQIGEPEEIY 238
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
494-662 |
1.72e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.60 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA-----YVSQQAWIFHGN-------VRE 560
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgPLDfqrdsIARGLLYLGHAPgikttlsVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NIlfgekynhqRYQHTVHvcGLQKDLNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:cd03231 93 NL---------RFWHADH--SDEQVEEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|...
gi 52138554 640 KHVFEECIKKTLKGKTVVLVTHQ 662
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
496-680 |
1.74e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA------------WIFHG------ 556
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqPMSKLSSAAkaelrnqklgfiYQFHHllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 ---NVRENILFGEKYN---HQRYQHTVHVCGLQKDLNslpygdlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:PRK11629 104 aleNVAMPLLIGKKKPaeiNSRALEMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 52138554 631 LSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
492-692 |
1.76e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.53 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 492 SPKSVLHNISFVVRKGKVLGICGNVGSGKSS---LISALLGQMQLQKGVVAVNGpLAYVSQQAW--------IFH----- 555
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdirekvgiVFQnpdnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 ---GNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:PRK13640 97 fvgATVGDDVAFGlENRAVPRPEMIKIVRDVLADVGMLDYID-----SEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 632 SAVDAHvGKHVFEECIKKTLKGK--TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:PRK13640 172 SMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1127-1350 |
1.97e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 1206
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQ----DPVLfvgTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTEngenFSVGERQLLCMARALLRNS 1282
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1283 KIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAH------RLntvlnCDLVLVMENGKVIEFDKPEVLAE 1350
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
488-680 |
2.48e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.76 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSG-SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG---------PLAYVSQQ--AWIFH 555
Cdd:PRK10535 14 YPSGeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatldadALAQLRREhfGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 gnvRENILfgekyNHQRYQHTVHV----CGLQKD---------LNSLPYGDltEIGERGVNLSGGQRQRISLARAVYANR 622
Cdd:PRK10535 94 ---RYHLL-----SHLTAAQNVEVpavyAGLERKqrllraqelLQRLGLED--RVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 623 QLYLLDDPLSAVDAHVGKHVFeeCIKKTL--KGKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVM--AILHQLrdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
494-691 |
2.66e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.74 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISaLLGQMQ-LQKGVVAVNG-PL------------AYVSQQAWIFHG-NV 558
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAqPLeswsskafarkvAYLPQQLPAAEGmTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENILFGeKY------------NHQRYQHTVHVCGLqkdlnslpygdlTEIGERGVN-LSGGQRQRISLARAVYANRQLY 625
Cdd:PRK10575 103 RELVAIG-RYpwhgalgrfgaaDREKVEEAISLVGL------------KPLAHRLVDsLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 626 LLDDPLSAVD-AHvgkHVFEECIKKTL---KGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 691
Cdd:PRK10575 170 LLDEPTSALDiAH---QVDVLALVHRLsqeRGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
501-690 |
2.77e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 501 SFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFG--- 565
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsrrPVSMLFQENNLFsHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 566 ----EKYNHQRYQHTVHVCGLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD----AH 637
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 52138554 638 VGKHVFEECIKKTLkgkTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 690
Cdd:PRK10771 168 MLTLVSQVCQERQL---TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
491-703 |
2.96e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------------PLAYVSQ 549
Cdd:PRK13641 15 GTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 550 QAWIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDL-NSLPYgdlteigergvNLSGGQRQRISLARAVYAN 621
Cdd:PRK13641 95 EAQLFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDLiSKSPF-----------ELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 622 RQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKli 700
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKK-- 241
|
...
gi 52138554 701 HNL 703
Cdd:PRK13641 242 HYL 244
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1107-1341 |
3.40e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1107 EHTHPFKVGTCPKDWPsrgEITFKDYRMRYRDNTpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTII 1186
Cdd:PRK10522 306 PYKAEFPRPQAFPDWQ---TLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1187 IDEVDICTVGLEDLRTKLTMIPQDPVLFvgtvRYNLDPLGSHTDEML---WhvLERtfmrdtiMKLPEKLQaevTENGE- 1262
Cdd:PRK10522 382 LDGKPVTAEQPEDYRKLFSAVFTDFHLF----DQLLGPEGKPANPALvekW--LER-------LKMAHKLE---LEDGRi 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1263 ---NFSVGERQLLCMARALLRNSKIILLDEATASMDSK------TDTLVQstIKEAFKscTVLTIAHRLNTVLNCDLVLV 1333
Cdd:PRK10522 446 snlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPL--LQEMGK--TIFAISHDDHYFIHADRLLE 521
|
....*...
gi 52138554 1334 MENGKVIE 1341
Cdd:PRK10522 522 MRNGQLSE 529
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
494-689 |
3.85e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.93 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL----LGQMQLQkGVVAVNG-PL---------AYVsQQAWIFHGN-- 557
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGS-GSVLLNGmPIdakemraisAYV-QQDDLFIPTlt 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILF----------GEKYNHQRYQHTVHVCGLQKDLNslpygdlTEIGERGV--NLSGGQRQRISLARAVYANRQLY 625
Cdd:TIGR00955 116 VREHLMFqahlrmprrvTKKEKRERVDEVLQALGLRKCAN-------TRIGVPGRvkGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 626 LLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1143-1348 |
5.08e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVL-FVGTVR-- 1219
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 --YNLDPLGS---HTDEMLWHVLERTfmrdtimklpeklqaEVTENGENF----SVGERQLLCMARALLRNS------KI 1284
Cdd:PRK13548 97 vaMGRAPHGLsraEDDALVAAALAQV---------------DLAHLAGRDypqlSGGEQQRVQLARVLAQLWepdgppRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1285 ILLDEATASMDSKTdtlvQSTIKEAFKSCT------VLTIAHRLN-TVLNCDLVLVMENGKVIEFDKP-EVL 1348
Cdd:PRK13548 162 LLLDEPTSALDLAH----QHHVLRLARQLAherglaVIVVLHDLNlAARYADRIVLLHQGRLVADGTPaEVL 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1127-1357 |
6.15e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.05 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKltM 1206
Cdd:COG3842 6 LELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG--M 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLF-----VGTVRYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 1278
Cdd:COG3842 82 VFQDYALFphltvAENVAFGLRMRGvpkAEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1279 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC---TV---------LTIAHRlntvlncdlVLVMENGKVIEFDKPE 1346
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELgitFIyvthdqeeaLALADR---------IAVMNDGRIEQVGTPE 221
|
250
....*....|.
gi 52138554 1347 VLAEKPDSAFA 1357
Cdd:COG3842 222 EIYERPATRFV 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1143-1351 |
6.37e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGL-EDLRTKLTMIPQDPVLFVGTVRYN 1221
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1222 ldplgshtdeMLWHVLErtfMRDTIMKLPEKLQA-EVTEN----------GENFSVGERQLLCMARALLRNSKIILLDEA 1290
Cdd:PRK10895 98 ----------NLMAVLQ---IRDDLSAEQREDRAnELMEEfhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1291 TASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAEK 1351
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPtEILQDE 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
498-669 |
6.58e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 498 HNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL-----AYVSQQAWIFHGN-------VRENILF 564
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGePIrrqrdEYHQDLLYLGHQPgikteltALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 565 gekynhqrYQHtVHVCGLQKDLNSLpygdLTEIGERGV------NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHv 638
Cdd:PRK13538 98 --------YQR-LHGPGDDEALWEA----LAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ- 163
|
170 180 190
....*....|....*....|....*....|..
gi 52138554 639 GKHVFEECIKKTL-KGKTVVLVTHQLQFLESC 669
Cdd:PRK13538 164 GVARLEALLAQHAeQGGMVILTTHQDLPVASD 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1135-1363 |
6.58e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL-----VEPASGTIIIDEVDICTVGLEDLR----TKLT 1205
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1206 MIPQDPVLfvgtvryNLDPLgsHTDE-MLWHVL------ERTFMRDTIMKLPEKL---QA--EVTENGENFSVGERQLLC 1273
Cdd:PRK15134 96 MIFQEPMV-------SLNPL--HTLEkQLYEVLslhrgmRREAARGEILNCLDRVgirQAakRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1274 MARALLRNSKIILLDEATASMdsktDTLVQSTIKEAFK------SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 1346
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTAL----DVSVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....*...
gi 52138554 1347 VLAEKPDSAFA-MLLAAE 1363
Cdd:PRK15134 243 TLFSAPTHPYTqKLLNSE 260
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
495-682 |
7.32e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA----------WIFHG------- 556
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqPLHQMDEEAraklrakhvgFVFQSfmliptl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENI-----LFGEKYNHQRYQ--HTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:PRK10584 104 NALENVelpalLRGESSRQSRNGakALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 52138554 630 PLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLESCDEVILLEDGEICE 682
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1127-1344 |
7.96e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.80 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYrdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL--VEP---ASGTIIIDEVDIC-----TVg 1196
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYsprtdTV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1197 leDLRTKLTMIPQDPVLFVGT----VRYNLDPLGSHTDEMLWHVLERTFMRDTIMklpEKLQAEVTENGENFSVGERQLL 1272
Cdd:PRK14239 83 --DLRKEIGMVFQQPNPFPMSiyenVVYGLRLKGIKDKQVLDEAVEKSLKGASIW---DEVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1273 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 1344
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1144-1350 |
8.67e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLgM-ALFRLVEPASGTIIID--EVDI--------CTVGledlrtkltMIPQDPV 1212
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDgkPVRIrsprdaiaLGIG---------MVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 LF-VGTVRYNLDpLGshTDEMLWHVLERTFMRDTIMKLPEK------LQAEVtengENFSVGERQLLCMARALLRNSKII 1285
Cdd:COG3845 91 LVpNLTVAENIV-LG--LEPTKGGRLDRKAARARIRELSERygldvdPDAKV----EDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1286 LLDEATASM-DSKTDTLVQsTIKEaFKS--CTVLTIAHRLNTVL-NCDLVLVMENGKVI-EFDKPEV----LAE 1350
Cdd:COG3845 164 ILDEPTAVLtPQEADELFE-ILRR-LAAegKSIIFITHKLREVMaIADRVTVLRRGKVVgTVDTAETseeeLAE 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
497-693 |
8.79e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------QMQLQKGVVAVNGPLA-----YVSQQAWIFHG----- 556
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirkSRANTGYIFQQfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 --NVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYgdLTEIG------ERGVNLSGGQRQRISLARAVYANRQLYLLD 628
Cdd:PRK09984 100 rlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 629 DPLSAVDAHVGKHVFEEC--IKKTlKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:PRK09984 178 EPIASLDPESARIVMDTLrdINQN-DGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
496-686 |
1.09e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISAL-------LGQMQL------------QKGVVAVNGPLAYVSQQ--AWIf 554
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIagnhfdfsktpsDKAIRELRRNVGMVFQQynLWP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 HGNVRENILfgekynhqryQHTVHVCGLQKD---------LNSLpygDLTEIGER-GVNLSGGQRQRISLARAVYANRQL 624
Cdd:PRK11124 96 HLTVQQNLI----------EAPCRVLGLSKDqalaraeklLERL---RLKPYADRfPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 625 YLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTH 686
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVS--IIRELAetGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDA 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1143-1341 |
1.78e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPvlfvgtvR 1219
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 YNLDP-----------LGSHTDEMlwHVLERTFMRDTIMKL----PEKLQAEVTEngenFSVGERQLLCMARALLRNSKI 1284
Cdd:PRK15134 373 SSLNPrlnvlqiieegLRVHQPTL--SAAQREQQVIAVMEEvgldPETRHRYPAE----FSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1285 ILLDEATASMDsKTdtlVQSTIKEAFKS------CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK15134 447 IILDEPTSSLD-KT---VQAQILALLKSlqqkhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1143-1343 |
2.18e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEvdictvgledlRTKLTMIPQDPVLFVG-- 1216
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILagelEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1217 ---TVRYNLDPLGSHTDEMLwHVLERTFMRDTIMKLPEKLQAEVTENGE--------------------------NFSVG 1267
Cdd:COG0488 78 vldTVLDGDAELRALEAELE-ELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1268 ERQLLCMARALLRNSKIILLDEATASMDSKT-----DTLVQSTikeafksCTVLTIAH-R--LNTVlnCDLVLVMENGKV 1339
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNYP-------GTVLVVSHdRyfLDRV--ATRILELDRGKL 227
|
....
gi 52138554 1340 IEFD 1343
Cdd:COG0488 228 TLYP 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-689 |
2.26e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAY-------------------VSQQAWIF 554
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiklrkevgmVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 -HGNVRENILFGEKYNHQRYQHTVHVCgLQKDLNSLpyGDLTEIGER----GVNLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:PRK14246 103 pHLSIYDNIAYPLKSHGIKEKREIKKI-VEECLRKV--GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 630 PLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQ-LQFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:PRK14246 180 PTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
509-680 |
2.44e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 509 VLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL-----------------AYVSQQAWIF-HGNVRENILFG-EKYN 569
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLFpHYKVRGNLRYGmAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 570 HQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV--FEECI 647
Cdd:PRK11144 106 VAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELlpYLERL 174
|
170 180 190
....*....|....*....|....*....|....
gi 52138554 648 KKTLKgKTVVLVTHQLQ-FLESCDEVILLEDGEI 680
Cdd:PRK11144 175 AREIN-IPILYVSHSLDeILRLADRVVVLEQGKV 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1143-1341 |
2.47e-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: 67.17 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPVLFVGtvr 1219
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 ynldplgshtdemlwhVLERTFMRDTimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIILLDEatasMDSKTD 1299
Cdd:cd03217 92 ----------------VKNADFLRYV---------------NEGFSGGEKKRNEILQLLLLEPDLAILDE----PDSGLD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 52138554 1300 TLVQSTIKEAFKS-----CTVLTIAH--RLNTVLNCDLVLVMENGKVIE 1341
Cdd:cd03217 137 IDALRLVAEVINKlreegKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
836-1050 |
3.10e-12 |
|
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: 69.00 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 836 VDQTLQDTKHHMyqLVYIASMVsvLMFGIIKG-FTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 908
Cdd:cd18542 26 IDSVIGGGLREL--LWLLALLI--LGVALLRGvFRYLQGYLAEKASqkvaydLRNDLYDHLQRLSFSFHDKARTGDLMSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 909 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLrIFHRGVQelKQVENISRSpwFSH 987
Cdd:cd18542 102 CTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSInWKLTLISLAIIPFIALFSY-VFFKKVR--PAFEEIREQ--EGE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 988 ITSSIQ----GLGVIHAYDKKDDCISKFKTLNDEnsshllYFNCALR-------WFALrMDILMNIVTFVVALL 1050
Cdd:cd18542 177 LNTVLQenltGVRVVKAFAREDYEIEKFDKENEE------YRDLNIKlakllakYWPL-MDFLSGLQIVLVLWV 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1144-1337 |
3.13e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDLRTKLT------MIPQD-PVLFVG 1216
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-----YNKLDHKLAaqlgigIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1217 TVRYNLdPLGSHTDEMLW--HVLERTFMRD--TIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATA 1292
Cdd:PRK09700 96 TVLENL-YIGRHLTKKVCgvNIIDWREMRVraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 52138554 1293 SM-DSKTDTL--VQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENG 1337
Cdd:PRK09700 175 SLtNKEVDYLflIMNQLRKEGTA--IVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1127-1341 |
3.28e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDI-CTVGLEDLRTKLT 1205
Cdd:PRK11264 4 IEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1206 MIPQDpvlfVGTV--RYNLDPLGShtdeMLWHVLE-----RTFMRDTIMKLPEKLQAEVTENGEN------FSVGERQLL 1272
Cdd:PRK11264 82 QLRQH----VGFVfqNFNLFPHRT----VLENIIEgpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1273 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1127-1356 |
3.65e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 67.80 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGtiiiDEVDIC-----TVGLEDLR 1201
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFgerrgGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TKL---------TMIPQDPVL------FVGTV-RYNldplgSHTDEM------------LWHVLERTFmrdtimklpekl 1253
Cdd:COG1119 78 KRIglvspalqlRFPRDETVLdvvlsgFFDSIgLYR-----EPTDEQrerarellellgLAHLADRPF------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1254 qaevtengENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNC-DL 1330
Cdd:COG1119 141 --------GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTH 212
|
250 260
....*....|....*....|....*..
gi 52138554 1331 VLVMENGKVIEF-DKPEVLAEKPDSAF 1356
Cdd:COG1119 213 VLLLKDGRVVAAgPKEEVLTSENLSEA 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-680 |
3.86e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVnGP---LAYVSQQAWIFHGN--VRENIlfgeky 568
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQHQEELDPDktVLDEL------ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 569 nhQRY---QHTVHVCGLQKDLNsLPYGD-LTEIGergvNLSGGQRQRISLARAVYANRQLYLLDDP-----LSAVDAhvg 639
Cdd:COG0488 401 --RDGapgGTEQEVRGYLGRFL-FSGDDaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA--- 470
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 52138554 640 khvFEECIKkTLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:COG0488 471 ---LEEALD-DFPG-TVLLVSHDRYFLDRvATRILEFEDGGV 507
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
488-711 |
4.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.51 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV----------NGPLAYVSQQAWI-- 553
Cdd:PRK13634 12 YQYKTPfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkkNKKLKPLRKKVGIvf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 -------FHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKD-LNSLPYgdlteigergvNLSGGQRQRISLARAV 618
Cdd:PRK13634 92 qfpehqlFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEElLARSPF-----------ELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 619 YANRQLYLLDDPLSAVDAHvGKH----VFEECIKKtlKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKEL---- 689
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPK-GRKemmeMFYKLHKE--KGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPREIfadp 237
|
250 260 270
....*....|....*....|....*....|.
gi 52138554 690 --MEERG-------RYAKLIHNLRGLQFKDP 711
Cdd:PRK13634 238 deLEAIGldlpetvKFKRALEEKFGISFPKP 268
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
497-684 |
4.56e-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: 66.83 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVL------------GICGNVGSGKSSLISALLGQMQLQKGVVAVNGP------------LAYVSQQaw 552
Cdd:cd03264 3 LENLTKRYGKKRALdgvsltlgpgmyGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 553 iFhgNVRENILFGEKYNHQRYQHTVH-------VCGLQKDLNslpygdLTEIGERGVN-LSGGQRQRISLARAVYANRQL 624
Cdd:cd03264 81 -F--GVYPNFTVREFLDYIAWLKGIPskevkarVDEVLELVN------LGDRAKKKIGsLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 625 YLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 684
Cdd:cd03264 152 LIVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
488-692 |
5.14e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVnGPLAYVSQ---------------- 549
Cdd:PRK13643 11 YQPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTskqkeikpvrkkvgvv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 550 ----QAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPygdlTEIGERG-VNLSGGQRQRISLARAVYANRQL 624
Cdd:PRK13643 90 fqfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLA----DEFWEKSpFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 625 YLLDDPLSAVD--AHVGKHVFEECIKKTlkGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:PRK13643 166 LVLDEPTAGLDpkARIEMMQLFESIHQS--GQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
844-1018 |
5.35e-12 |
|
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: 68.26 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 844 KHHMYQLVYIASMVSVLMFgIIKGFTFTNTTLMAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD 917
Cdd:cd18545 33 NGDLSGLLIIALLFLALNL-VNWVASRLRIYLMAKvgqrilYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 918 VRLPFHAENFLQQFFMVVFILVIMAAVFPVV-LVVLAGLAVIFLILLRIFHRgVQELKQVENISRSPWFSHITSSIQGLG 996
Cdd:cd18545 112 DLLSNGLINLIPDLLTLVGIVIIMFSLNVRLaLVTLAVLPLLVLVVFLLRRR-ARKAWQRVRKKISNLNAYLHESISGIR 190
|
170 180
....*....|....*....|..
gi 52138554 997 VIHAYDKKDDCISKFKTLNDEN 1018
Cdd:cd18545 191 VIQSFAREDENEEIFDELNREN 212
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
836-1051 |
5.94e-12 |
|
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: 68.21 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 836 VDqTLQDTKHHMYQLVYIASMVSVLMFGIIKGFTFTNTTLMASS-----SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFS 910
Cdd:cd18541 26 ID-ALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASrrieyDLRNDLFAHLLTLSPSFYQKNRTGDLMARAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 911 KDMDEldVR--LPFHAENFLQQFFMVVFILVIMAAVFP----VVLVVLAGLAVIFLILLRIFHRG---VQELkqvenisr 981
Cdd:cd18541 105 NDLNA--VRmaLGPGILYLVDALFLGVLVLVMMFTISPkltlIALLPLPLLALLVYRLGKKIHKRfrkVQEA-------- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 982 spwFSHITSSIQ----GLGVIHAYDKKDDCISKFKTLNDEnsshllYFNCALRWFALR--MDILMNIVTFVVALLV 1051
Cdd:cd18541 175 ---FSDLSDRVQesfsGIRVIKAFVQEEAEIERFDKLNEE------YVEKNLRLARVDalFFPLIGLLIGLSFLIV 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1127-1351 |
6.57e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.84 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDP--VLFVGTV-------RYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 1277
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 1278 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIA-HRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1130-1346 |
6.67e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1130 KDYRMRYRDNTpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGLEDLRTKLTMI 1207
Cdd:PRK13639 5 RDLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgePIKYDKKSLLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1208 PQDP--VLFVGTVRYNL--DP--LGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 1278
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVafGPlnLGLSKEEVEKRVkeaLKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1279 LRNSKIILLDEATASMD----SKTDTLVQSTIKEAFkscTVLTIAHRLNTV-LNCDLVLVMENGKVIEFDKPE 1346
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKEGI---TIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPK 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
496-690 |
7.08e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 67.56 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA------WIFHG-----NVRENIl 563
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhKLEYGDYKYrckhirMIFQDpntslNPRLNI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 fGE------KYN--------HQRYQHTVHVCGLqkdlnslpYGDLTEIGERgvNLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:COG4167 107 -GQileeplRLNtdltaeerEERIFATLRLVGL--------LPEHANFYPH--MLSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 630 PLSAVDAHVGKhvfeECIKKTLK-----GKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 690
Cdd:COG4167 176 ALAALDMSVRS----QIINLMLElqeklGISYIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVF 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
496-662 |
7.29e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.84 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV--NGPLAYVSQQAWIFHGNVRENILF---GEKYNH 570
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 571 QRYQHTVHVCGLQkDLNslpyGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKT 650
Cdd:COG4178 458 AELREALEAVGLG-HLA----ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREE 531
|
170
....*....|..
gi 52138554 651 LKGKTVVLVTHQ 662
Cdd:COG4178 532 LPGTTVISVGHR 543
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
494-691 |
7.60e-12 |
|
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: 69.45 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ--KGVVAVN----------GPLAYVSQQA---------- 551
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIYHvalcekcgyvERPSKVGEPCpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 552 ----WIFHGNVRENIlfgEKYNHQRYQHTVHVCG----LQKDLNSLP---YG------------DLTEIGER----GVNL 604
Cdd:TIGR03269 93 evdfWNLSDKLRRRI---RKRIAIMLQRTFALYGddtvLDNVLEALEeigYEgkeavgravdliEMVQLSHRithiARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 605 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEECIKKtlKGKTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVIEDlSDKAIWLENGEI 247
|
250
....*....|.
gi 52138554 681 CEKGTHKELME 691
Cdd:TIGR03269 248 KEEGTPDEVVA 258
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
494-693 |
8.10e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVS----QQAWIFH 555
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvrirsPrdairagIAYVPedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 GNVRENILFGekyNHQRYQH---------TVHVCGLQKDLNSLPYGDLTEIGergvNLSGGQRQRISLARAVYANRQLYL 626
Cdd:COG1129 345 LSIRENITLA---SLDRLSRgglldrrreRALAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 627 LDDPLSAVDahVG-KHVFEECIKK-TLKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:COG1129 418 LDEPTRGID--VGaKAEIYRLIRElAAEGKAVIVISSELPeLLGLSDRILVMREGRIVGELDREEATEEA 485
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1125-1341 |
8.18e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV------DICTVGLE 1198
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1199 DLRTKLTMIPQDPVLFVGTVRYN--LDPLGSHTDEMLWHVleRTFMRDTIMK--LPEKLQAEVTENGENFSVGERQLLCM 1274
Cdd:PRK14246 87 KLRKEVGMVFQQPNPFPHLSIYDniAYPLKSHGIKEKREI--KKIVEECLRKvgLWKEVYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1275 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
489-685 |
8.62e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.29 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 489 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG---------PLAYVSQQ-AWIF-HGN 557
Cdd:PRK11153 13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalsekELRKARRQiGMIFqHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 ------VRENILF-----GEKYNH--QRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQL 624
Cdd:PRK11153 93 llssrtVFDNVALplelaGTPKAEikARVTELLELVGLSDKADRYP-----------AQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 625 YLLDDPLSAVDAHVGKHVFE--ECIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 685
Cdd:PRK11153 162 LLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1144-1341 |
1.08e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC---TVGLEDLRTKLTMIPQDPvlfVG---- 1216
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP---YGslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1217 --TVRYNL-DPLGSHTDemlwhvLERTFMRDTIMKLPEK--LQAEVTENGEN-FSVGERQLLCMARALLRNSKIILLDEA 1290
Cdd:PRK11308 108 rkKVGQILeEPLLINTS------LSAAERREKALAMMAKvgLRPEHYDRYPHmFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1291 TasmdSKTDTLVQSTI-------KEAFKSCTVLtIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK11308 182 V----SALDVSVQAQVlnlmmdlQQELGLSYVF-ISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
848-1051 |
1.21e-11 |
|
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: 67.20 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 848 YQLVYIASMVSVLMFgiIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENF 927
Cdd:cd18557 40 LILLAIYLLQSVFTF--VRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 928 LQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQEL-KQV-ENISRSPwfSHITSSIQGLGVIHAYDKKD 1005
Cdd:cd18557 118 LRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLsKEVqDALAKAG--QVAEESLSNIRTVRSFSAEE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52138554 1006 DCISKFKTLNDEnsSHLLYFNCAlRWFALRMDIlMNIVTFVVALLV 1051
Cdd:cd18557 196 KEIRRYSEALDR--SYRLARKKA-LANALFQGI-TSLLIYLSLLLV 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
496-680 |
1.23e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG--------------NVR 559
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGeN-GAGKSTLMKILSGVYQPDSGEILLDGePVRFRSPRDAQAAGiaiihqelnlvpnlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGE------KYNHQR-YQHTVHVC---GLQKDLNslpygdlTEIGErgvnLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:COG1129 98 ENIFLGReprrggLIDWRAmRRRARELLarlGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 52138554 630 PLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEI 680
Cdd:COG1129 167 PTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGRL 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1127-1339 |
1.41e-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: 65.35 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDlrTKLTM 1206
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDpvlfvgtvrYNLDPLGSHTDEMLWHVLERTFMRDTI----------MKLPEKLQAEVTEngenFSVGERQLLCMAR 1276
Cdd:cd03301 77 VFQN---------YALYPHMTVYDNIAFGLKLRKVPKDEIdervrevaelLQIEHLLDRKPKQ----LSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1277 ALLRNSKIILLDEATASMDSKTDTLVQSTIK---EAFKSCTV---------LTIAHRlntvlncdlVLVMENGKV 1339
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKrlqQRLGTTTIyvthdqveaMTMADR---------IAVMNDGQI 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1144-1340 |
1.45e-11 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 65.39 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQ---SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDLRTKLTMIPQD---------- 1210
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV-----LFDSRKKINLPPQQrkiglvfqqy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1211 ---PVLfvgTVRYNLdplgshtdEMLWHVLERTFMRDTIMKLPEKLQAEVTENG--ENFSVGERQLLCMARALLRNSKII 1285
Cdd:cd03297 85 alfPHL---NVRENL--------AFGLKRKRNREDRISVDELLDLLGLDHLLNRypAQLSGGEKQRVALARALAAQPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1286 LLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTV-LNCDLVLVMENGKVI 1340
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1143-1341 |
1.57e-11 |
|
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: 65.53 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlED----LRTKLtmipqdpvlfVGTV 1218
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDararLRARH----------VGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1219 RYNLDPLGSHTdeMLWHV---LERTFMRDtimklPEKLQAEVTEN---GENF-------SVGERQLLCMARALLRNSKII 1285
Cdd:COG4181 96 FQSFQLLPTLT--ALENVmlpLELAGRRD-----ARARARALLERvglGHRLdhypaqlSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1286 LLDEATASMDSKTDTLVQS---TIKEAFKSCTVLT-----IAHRlntvlnCDLVLVMENGKVIE 1341
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDllfELNRERGTTLVLVthdpaLAAR------CDRVLRLRAGRLVE 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
497-678 |
1.58e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG--------------NVREN 561
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGekynhqryqHTVHVCGL--QKDLNSLPYGDLTEIGE------RGVNLSGGQRQRISLARAVYANRQLYLLDDPLSA 633
Cdd:PRK11288 100 LYLG---------QLPHKGGIvnRRLLNYEAREQLEHLGVdidpdtPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 52138554 634 VDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDG 678
Cdd:PRK11288 171 LSAREIEQLFR--VIRELRaeGRVILYVSHRMeEIFALCDAITVFKDG 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1135-1289 |
1.63e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.82 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIIIDEVDIctvgledlrTKLTM---- 1206
Cdd:COG1137 12 SYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDI---------THLPMhkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 ------IPQDPVLFVG-TVRYNLdplgshtdeMLwhVLERTFM-RDTIMKLPEKLQAE-----VTEN-GENFSVGERQLL 1272
Cdd:COG1137 77 rlgigyLPQEASIFRKlTVEDNI---------LA--VLELRKLsKKEREERLEELLEEfgithLRKSkAYSLSGGERRRV 145
|
170
....*....|....*..
gi 52138554 1273 CMARALLRNSKIILLDE 1289
Cdd:COG1137 146 EIARALATNPKFILLDE 162
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
494-662 |
1.68e-11 |
|
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: 64.10 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV--AVNGPLAYVSQQAWIFHGNVRENILFgekynhq 571
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmPEGEDLLFLPQRPYLPLGTLREQLIY------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 572 ryqhtvhvcglqkdlnslPYGDlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECikkTL 651
Cdd:cd03223 87 ------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KE 136
|
170
....*....|.
gi 52138554 652 KGKTVVLVTHQ 662
Cdd:cd03223 137 LGITVISVGHR 147
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1127-1339 |
1.73e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.24 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdicTVGLEDLRTKLTM 1206
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLF--------VGtvrynLDPLGSHTDEMLwHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 1278
Cdd:PRK11247 86 MFQDARLLpwkkvidnVG-----LGLKGQWRDAAL-QALAAVGLADRANEWPAAL-----------SGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1279 LRNSKIILLDEATASMDSKTDTLVQSTI-----KEAFkscTVLTIAHRLN-TVLNCDLVLVMENGKV 1339
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1135-1356 |
1.85e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.44 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIID--EV--------DICtvgledl 1200
Cdd:PRK11432 15 RFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDgeDVthrsiqqrDIC------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1201 rtkltMIPQDPVLF----VG-TVRYNLDPLGSHTDEMLWHVLERTFMRDtimklpekLQAEVTENGENFSVGERQLLCMA 1275
Cdd:PRK11432 82 -----MVFQSYALFphmsLGeNVGYGLKMLGVPKEERKQRVKEALELVD--------LAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1276 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKP 1352
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQP 228
|
....
gi 52138554 1353 DSAF 1356
Cdd:PRK11432 229 ASRF 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1144-1363 |
1.90e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK--------LTMIPQDPV 1212
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHgtyEGEIIFEGEELQASNIRDTERAgiaiihqeLALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 L---FVGTV-----RYNLDPLGSHTDEMLWHVlertfmrdtimklpeKLQAEVTENGENFSVGERQLLCMARALLRNSKI 1284
Cdd:PRK13549 100 LeniFLGNEitpggIMDYDAMYLRAQKLLAQL---------------KLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1285 ILLDEATASM-DSKTDTLVqsTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEkpDSAFAMLL 1360
Cdd:PRK13549 165 LILDEPTASLtESETAVLL--DIIRDLKAhgIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTE--DDIITMMV 240
|
...
gi 52138554 1361 AAE 1363
Cdd:PRK13549 241 GRE 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1127-1351 |
1.93e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 1206
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQ-DPVLFVGTVRYNLDPLGSH-------TDEMLWHVLErtFMRdtimkLPEKLQAEVTEngenFSVGERQLLCMARAL 1278
Cdd:PRK13536 119 VPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLE--FAR-----LESKADARVSD----LSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1279 LRNSKIILLDEATASMDSKTDTLVQSTIKEAF-KSCTVLTIAH------RLntvlnCDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1127-1356 |
2.03e-11 |
|
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: 65.34 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctVGLEDLRTKLTM 1206
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFvgtvrynldplgSHTDemlwhVLERTFMRDTIMKLPEK-LQAEVTE-----NGENF--------SVGERQLL 1272
Cdd:cd03300 77 VFQNYALF------------PHLT-----VFENIAFGLRLKKLPKAeIKERVAEaldlvQLEGYanrkpsqlSGGQQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1273 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLA 1349
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIY 219
|
....*..
gi 52138554 1350 EKPDSAF 1356
Cdd:cd03300 220 EEPANRF 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1112-1340 |
2.19e-11 |
|
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: 64.98 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1112 FKVGTCPKDWpsrgeitfkdyrmryrDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIIID 1188
Cdd:cd03234 7 WDVGLKAKNW----------------NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1189 EVDictvgledlRTKLTM------IPQDPVLFVG-TVR-----YNLDPLGSHTDEmlwhvlERTFMRDTIMKLpekLQAE 1256
Cdd:cd03234 71 GQP---------RKPDQFqkcvayVRQDDILLPGlTVRetltyTAILRLPRKSSD------AIRKKRVEDVLL---RDLA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1257 VTENG----ENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAH--RLNTVLNCD 1329
Cdd:cd03234 133 LTRIGgnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFD 212
|
250
....*....|.
gi 52138554 1330 LVLVMENGKVI 1340
Cdd:cd03234 213 RILLLSSGEIV 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1143-1363 |
2.23e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.17 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP----ASGTIIIDEVDICTVGLEDLRT----KLTMIPQDPVlf 1214
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1215 vgTvryNLDPLgsHTDE------MLWH--------------VLERTFMRDtimklPEK-LQAEVTEngenFSVGERQLLC 1273
Cdd:COG4172 103 --T---SLNPL--HTIGkqiaevLRLHrglsgaaararaleLLERVGIPD-----PERrLDAYPHQ----LSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1274 MARALLRNSKIILLDEATasmdskT--DTLVQSTIKEAFKSCT------VLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 1344
Cdd:COG4172 167 IAMALANEPDLLIADEPT------TalDVTVQAQILDLLKDLQrelgmaLLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
250 260
....*....|....*....|
gi 52138554 1345 PEVLAEKPDSAFA-MLLAAE 1363
Cdd:COG4172 241 TAELFAAPQHPYTrKLLAAE 260
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
497-691 |
2.48e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.79 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGqMQLQKGVVAVNG-PLAYVSQQAW---------IF---HG------N 557
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrmqvVFqdpFGslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRE------NILFGEKYNHQRYQHTVHVcglqkdlnslpygdLTEIG-----------ErgvnLSGGQRQRISLARAVYA 620
Cdd:COG4172 381 VGQiiaeglRVHGPGLSAAERRARVAEA--------------LEEVGldpaarhryphE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 621 NRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 691
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1127-1354 |
3.17e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC--TVGLEDLRTKL 1204
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1205 TMIPQdpvlfvgtvRYNLDP-LGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEV--TENGENF----SVGERQLLCMARA 1277
Cdd:PRK09493 80 GMVFQ---------QFYLFPhLTALENVMFGPLRVRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1278 LLRNSKIILLDEATASMDSKTD----TLVQSTIKEAFKSCTV---LTIAHRLNTVLncdlvLVMENGKVIEFDKPEVLAE 1350
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGMTMVIVtheIGFAEKVASRL-----IFIDKGRIAEDGDPQVLIK 225
|
....
gi 52138554 1351 KPDS 1354
Cdd:PRK09493 226 NPPS 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
496-695 |
3.20e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.90 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWifhG------------NVRENI 562
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGePLDPEDRRRI---GylpeerglypkmKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 L-FGE-KynhqryqhtvhvcGLQKD---------LNSLpygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:COG4152 93 VyLARlK-------------GLSKAeakrradewLERL---GLGDRANKKVeELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 631 LSAVDAhVGKHVFEECIK-KTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 695
Cdd:COG4152 157 FSGLDP-VNVELLKDVIReLAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
485-690 |
3.38e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 485 SPEWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQ---LQKGVVAVNGPLA--------YVSQQAWI 553
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKPTkqilkrtgFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 F-HGNVRENILFgekynhqryqhtvhvCGLQKDLNSLPYGDLTEIGE---------------------RGVnlSGGQRQR 611
Cdd:PLN03211 152 YpHLTVRETLVF---------------CSLLRLPKSLTKQEKILVAEsviselgltkcentiignsfiRGI--SGGERKR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 612 ISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCLFFGKGSDA 294
|
.
gi 52138554 690 M 690
Cdd:PLN03211 295 M 295
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1143-1341 |
3.55e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.04 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-----------DEVDICtvgleDLRTKLTMIPQD- 1210
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIR-----ELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1211 ---PVLfvgTVRYNL--DP---LGshtdemlwhvLERTFMRDTIMKLPEKLQaeVTENGENF----SVGERQLLCMARAL 1278
Cdd:PRK11124 92 nlwPHL---TVQQNLieAPcrvLG----------LSKDQALARAEKLLERLR--LKPYADRFplhlSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1279 LRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
497-710 |
3.88e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.64 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAY--------------VSQQA--WIFHGNVR 559
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkPIDYsrkglmklresvgmVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLS 632
Cdd:PRK13636 102 QDVSFGavnlklpEDEVRKRVDNALKRTGIEHLKDKPTHC-----------LSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 633 AVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQFLE-SCDEVILLEDGEICEKGTHKELMEERG-------RYAKLIHN 702
Cdd:PRK13636 171 GLDP-MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEmlrkvnlRLPRIGHL 249
|
....*...
gi 52138554 703 LRGLQFKD 710
Cdd:PRK13636 250 MEILKEKD 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
494-691 |
4.09e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.67 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------P--------LAYVSQQAWIFHG-NV 558
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlPmhkrarlgIGYLPQEASIFRKlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENIL----FGEKYNHQRyqhtvhvcglQKDLNSLpygdLTEIG------ERGVNLSGGQRQRISLARAVYANRQLYLLD 628
Cdd:COG1137 96 EDNILavleLRKLSKKER----------EERLEEL----LEEFGithlrkSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 629 DPLSAVD--AhvgkhVFEecIKK---TLKGKTV-VLVT-HQLQ-FLESCDEVILLEDGEICEKGTHKELME 691
Cdd:COG1137 162 EPFAGVDpiA-----VAD--IQKiirHLKERGIgVLITdHNVReTLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
496-689 |
4.14e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.28 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-----------LAYVSQQAWIF-HGNVRENIL 563
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFpHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 564 FGEKynhqryqhtvhVCGLQKD------LNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 636
Cdd:PRK11432 101 YGLK-----------MLGVPKEerkqrvKEALELVDLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 637 HVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:PRK11432 170 NLRRSMREK-IRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
497-691 |
4.17e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.16 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLayVSQQAWifhGNVREN--ILFGEKYNhQRYQ 574
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA--ITDDNF---EKLRKHigIVFQNPDN-QFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 575 HTVH---VCGLQKdlNSLPYGDLTEIGERGVN--------------LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 637
Cdd:PRK13648 99 SIVKydvAFGLEN--HAVPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 638 VGKHVFEECIK-KTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 691
Cdd:PRK13648 177 ARQNLLDLVRKvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
490-699 |
4.31e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.01 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 490 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQQAWIFHGN------ 557
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIGIIFQNpdnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 ---VRENILFG---EKYNHQRYQ----HTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLL 627
Cdd:PRK13632 98 gatVEDDIAFGlenKKVPPKKMKdiidDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 628 DDPLSAVDAHvGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM--EERGRYAKL 699
Cdd:PRK13632 167 DESTSMLDPK-GKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILnnKEILEKAKI 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1127-1325 |
6.40e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYrdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICT-------VGLED 1199
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNqniyerrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQDPVLF----VGTVRYNLDPLGSHTDEMLWHVLERTfMRDTimKLPEKLQAEVTENGENFSVGERQLLCMA 1275
Cdd:PRK14258 86 LRRQVSMVHPKPNLFpmsvYDNVAYGVKIVGWRPKLEIDDIVESA-LKDA--DLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1276 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAF--KSCTVLTIAHRLNTV 1325
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
494-664 |
6.47e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.29 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL-----L-------GQMQL------QKGV--VAVNGPLAYVSQQAWI 553
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLipgarveGEILLdgediyDPDVdvVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 FHGNVRENILFGEKYNHQRyqhtvhvcglqkdlnslPYGDLTEIGER------------------GVNLSGGQRQRISLA 615
Cdd:COG1117 104 FPKSIYDNVAYGLRLHGIK-----------------SKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 52138554 616 RAVYANRQLYLLDDPLSAVD----AHVgkhvfEECIKKtLKGK-TVVLVTHQLQ 664
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpistAKI-----EELILE-LKKDyTIVIVTHNMQ 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1143-1349 |
6.61e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVdictvgledLRTKLT----------MIPQDPV 1212
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN---------PCARLTpakahqlgiyLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 LFVG-TVRYN-LDPLGSHTDEMlwhvlertfmrdtimklpEKLQAEVTENGENFS---------VGERQLLCMARALLRN 1281
Cdd:PRK15439 97 LFPNlSVKENiLFGLPKRQASM------------------QKMKQLLAALGCQLDldssagsleVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 1282 SKIILLDEATASMD-SKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI------EFDKPEVLA 1349
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIAlsgktaDLSTDDIIQ 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
497-689 |
8.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.64 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------------------PLAYVSQQAWIFHG 556
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrlrkeiGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPygdlTEIGERG-VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP----EDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 636 AHvGKHVFEECIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:PRK13645 183 PK-GEEDFINLFERLNKeyKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
501-690 |
8.77e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.83 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 501 SFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------------PLAYVSQQ-AWIFHGNVRENI 562
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFGEKY-------NHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 635
Cdd:PRK10070 128 AFGMELaginaeeRREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 636 AHVGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELM 690
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1112-1343 |
8.85e-11 |
|
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: 63.32 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1112 FKVGTCPKDWPSRGEITFKDYRMRYRdntpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDE-- 1189
Cdd:cd03220 10 YPTYKGGSSSLKKLGILGRKGEVGEF----WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1190 ---VDIcTVGLEDlrtKLTMIpqDPVLFVGTVrYNLDPlgshtDEMlwhvleRTFMRDTIM--KLPEKLQAEVtengENF 1264
Cdd:cd03220 86 sslLGL-GGGFNP---ELTGR--ENIYLNGRL-LGLSR-----KEI------DEKIDEIIEfsELGDFIDLPV----KTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1265 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEF 1342
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
.
gi 52138554 1343 D 1343
Cdd:cd03220 224 G 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
491-724 |
9.89e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------PLAYVSQQAWI------- 553
Cdd:PRK13637 15 GTPfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRKKVGLvfqypey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 --FHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDlnslPYGDLTEIgergvNLSGGQRQRISLARAVYANRQL 624
Cdd:PRK13637 95 qlFEETIEKDIAFGpinlglsEEEIENRVKRAMNIVGLDYE----DYKDKSPF-----ELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 625 YLLDDPLSAVDAHVGKHVFEEcIKKTLKGK--TVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGRYAK--- 698
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNK-IKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKEVETLESigl 244
|
250 260 270
....*....|....*....|....*....|....*
gi 52138554 699 -------LIHNLRGLQFKDPEHIYNV--AMVETLK 724
Cdd:PRK13637 245 avpqvtyLVRKLRKKGFNIPDDIFTIeeAKEEILK 279
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
494-692 |
1.02e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.54 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQM--QLQKGVVAVNGplayvsqqawifhgnvrENILFGEKYNHQ 571
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 572 R------YQHTVHVCGLqKDLNSLpygdlteigeRGVN--LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF 643
Cdd:cd03217 76 RlgiflaFQYPPEIPGV-KNADFL----------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52138554 644 EEcIKKTL-KGKTVVLVTHQLQFLESC--DEVILLEDGEICEKGThKELMEE 692
Cdd:cd03217 145 EV-INKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGD-KELALE 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1127-1343 |
1.18e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRL----VEPASGTIIIDEvdictvgledlRT 1202
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKLGE-----------TV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1203 KLTMIPQDpvlfvgtvRYNLDPlgshtDEMLWHVLERTFMRDTIMKL----------PEKLQAEVtengENFSVGERQLL 1272
Cdd:COG0488 379 KIGYFDQH--------QEELDP-----DKTVLDELRDGAPGGTEQEVrgylgrflfsGDDAFKPV----GVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1273 CMARALLRNSKIILLDEAT-----ASMDSKTDTLvqstikEAFKScTVLTIAH-R--LNTVlnCDLVLVMENGKVIEFD 1343
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTnhldiETLEALEEAL------DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1142-1308 |
1.24e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1142 LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvGLEDLRTKLTMI-PQD---PVLfvgT 1217
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1218 VRYNL----DPLGSHtDEMLWHVLERTFMRDtIMKLPEKlqaevtengeNFSVGERQLLCMARALLRNSKIILLDEATAS 1293
Cdd:PRK13539 90 VAENLefwaAFLGGE-ELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....*
gi 52138554 1294 MDSKTDTLVQSTIKE 1308
Cdd:PRK13539 158 LDAAAVALFAELIRA 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1143-1357 |
1.39e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVglEDLRTKLTMIPQDPVLFVG-TVRYN 1221
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1222 L-----------DPLGSHTDEMLWHVlertFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEA 1290
Cdd:PRK11607 112 IafglkqdklpkAEIASRVNEMLGLV----HMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1291 TASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSAFA 1357
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1127-1351 |
1.40e-10 |
|
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: 65.59 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLV---EPASGTIIIdEVDIC-TVGLEDLRT 1202
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRIIY-HVALCeKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1203 KL---------TMIPQDpVLFVG---TVRYNLDplgshtdEMLWHVLERTF-------MRDTIMK-LPE----------- 1251
Cdd:TIGR03269 77 KVgepcpvcggTLEPEE-VDFWNlsdKLRRRIR-------KRIAIMLQRTFalygddtVLDNVLEaLEEigyegkeavgr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1252 --------KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTV-LTIAHRL 1322
Cdd:TIGR03269 149 avdliemvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|.
gi 52138554 1323 NTVLN--CDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:TIGR03269 229 PEVIEdlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1130-1349 |
1.57e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1130 KDYRMR---YRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 1206
Cdd:PRK15112 12 KTFRYRtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPV-----------LFVGTVRYNLDPLGSHTDEMLWHVLERTFMR-DTIMKLPEKLqaevtengenfSVGERQLLCM 1274
Cdd:PRK15112 92 IFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHML-----------APGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 1275 ARALLRNSKIILLDEATASMD-SKTDTLVQSTIK-EAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF-DKPEVLA 1349
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERgSTADVLA 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
492-689 |
1.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 492 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP---------------LAYVSQQAWIFHG 556
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:PRK13652 95 TVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 630 PLSAVDAHVGKHV--FEECIKKTLkGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKEL 689
Cdd:PRK13652 164 PTAGLDPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1123-1355 |
1.86e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.06 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1123 SRGEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV------- 1195
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1196 ------GLEDLRTKLTMIPQdpvlfvgtvRYNldpLGSHTdEMLWHVLE---------RTFMRDTIMKLPEKLQAEVTEN 1260
Cdd:PRK10619 80 kvadknQLRLLRTRLTMVFQ---------HFN---LWSHM-TVLENVMEapiqvlglsKQEARERAVKYLAKVGIDERAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1261 GE---NFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNC-DLVLVME 1335
Cdd:PRK10619 147 GKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLH 226
|
250 260
....*....|....*....|
gi 52138554 1336 NGKVIEFDKPEVLAEKPDSA 1355
Cdd:PRK10619 227 QGKIEEEGAPEQLFGNPQSP 246
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
494-692 |
1.90e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PL--------AYVSQQAWIFHgnvR 559
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllPLhararrgiGYLPQEASIFR---R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENIlfgekynhqrYQHTVHVCGLQKDLNSLPYGD-LTEIGER----------GVNLSGGQRQRISLARAVYANRQLYLLD 628
Cdd:PRK10895 93 LSV----------YDNLMAVLQIRDDLSAEQREDrANELMEEfhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 629 DPLSAVDAhvgKHVFEecIKKTLK-----GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:PRK10895 163 EPFAGVDP---ISVID--IKRIIEhlrdsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
497-731 |
1.98e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.88 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLI------SALLGQMQLQKGV--------------VAVNGPLAYVSQQAWIFHG 556
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGKVtfhgknlyapdvdpVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENILFGEKYNhqryqhtvhvcGLQKDLNSLPYGDLTE----------IGERGVNLSGGQRQRISLARAVYANRQLYL 626
Cdd:PRK14243 106 SIYDNIAYGARIN-----------GYKGDMDELVERSLRQaalwdevkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 627 LDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGthkelmeerGRYAKLIhnlrgl 706
Cdd:PRK14243 175 MDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG---------GRYGYLV------ 238
|
250 260
....*....|....*....|....*
gi 52138554 707 QFKDPEHIYNvamvetlkeSPAQRD 731
Cdd:PRK14243 239 EFDRTEKIFN---------SPQQQA 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
499-692 |
2.03e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------PL-------AYV--SQQAWIFHGN--VRE 560
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprsPLdavkkgmAYIteSRRDNGFFPNfsIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKYNHQRYQHTVhvcGL------------QKDLNSLPYGDLTE-IGErgvnLSGGQRQRISLARAVYANRQLYLL 627
Cdd:PRK09700 361 NMAISRSLKDGGYKGAM---GLfhevdeqrtaenQRELLALKCHSVNQnITE----LSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 628 DDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRDDMSE 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
497-679 |
2.12e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------------QMQLQ-------KGVVAVNGPLAYVSQQAwi 553
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASnirdterAGIVIIHQELTLVPELS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 fhgnVRENILFGEKYNHQ----RYQHTVHVC-------GLQKDLNSLPYGDLteigergvnlSGGQRQRISLARAVYANR 622
Cdd:TIGR02633 95 ----VAENIFLGNEITLPggrmAYNAMYLRAknllrelQLDADNVTRPVGDY----------GGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 623 QLYLLDDPLSAVDAHVGKHVFEecIKKTLKGKTV--VLVTHQLQFLES-CDEVILLEDGE 679
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
497-726 |
2.46e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWI---------------FHGNVREN 561
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 634
Cdd:PRK13647 101 VAFGpvnmgldKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 635 DAHVGKHVFEECIKKTLKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKG-----THKELMEERGRYAKLIHNLrglqF 708
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVAQI----F 245
|
250
....*....|....*...
gi 52138554 709 KDPEHIYNVAMVETLKES 726
Cdd:PRK13647 246 EDLPELGQSKLPLTVKEA 263
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1127-1345 |
2.85e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.84 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 1199
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQDP--VLFVGTV----RYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKlqaevteNGENFSVGERQLLC 1273
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVlkdvAFGPQNFGVSQEEAEALAREKLALVGISESLFEK-------NPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1274 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 1345
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
499-692 |
2.96e-10 |
|
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: 64.44 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVN-----------GP---------LAYVSQQAWIF-HGN 557
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPdgrgrakryIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENIL------FGEKYNHQRYQHTVHVCGLQKD-----LNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYL 626
Cdd:TIGR03269 382 VLDNLTeaigleLPDELARMKAVITLKMVGFDEEkaeeiLDKYPD-----------ELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 627 LDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:TIGR03269 451 LDEPTGTMDP-ITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-680 |
3.25e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL--AYVSQQAWIF-HGNVRENIL--FGEKY 568
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQEPPLDdDLTVLDTVLdgDAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 569 NHQRYQHTVHVCGLQKDLNSLPYGDL-TEIGERGV--------------------------NLSGGQRQRISLARAVYAN 621
Cdd:COG0488 91 ALEAELEELEAKLAEPDEDLERLAELqEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 622 RQLYLLDDP-----LSAVDAhvgkhvFEECIKKtLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:COG0488 171 PDLLLLDEPtnhldLESIEW------LEEFLKN-YPG-TVLVVSHDRYFLDRvATRILELDRGKL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1143-1350 |
3.62e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.02 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdiCTVGledlrtkltmipqdPVLFVGTvryNL 1222
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN----GRVS--------------ALLELGA---GF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1223 DPlgSHTdemlwhVLERTFMRDTIMKLP-----EKLQ--AEVTENGE-------NFSVGERQLLCMARALLRNSKIILLD 1288
Cdd:COG1134 100 HP--ELT------GRENIYLNGRLLGLSrkeidEKFDeiVEFAELGDfidqpvkTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1289 EATASMDS----KTDTLVQSTIKEAfksCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 1350
Cdd:COG1134 172 EVLAVGDAafqkKCLARIRELRESG---RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPeEVIAA 236
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
853-961 |
4.02e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 62.56 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 853 IASMVSVLmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFF 932
Cdd:cd18572 44 LLSVLSGL-FSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLV 122
|
90 100 110
....*....|....*....|....*....|
gi 52138554 933 MVVFILVIMAAV-FPVVLVVLAGLAVIFLI 961
Cdd:cd18572 123 QLVGGLAFMFSLsWRLTLLAFITVPVIALI 152
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1141-1366 |
4.28e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1141 PLVlDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA----SGTIIIDEVdicTVGLEDLRTKLT-MIPQDPvlfv 1215
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALRGRKIaTIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1216 gtvRYNLDPLgsHTdeMLWHVLERTFMR---DTIMKLPEKLQAEVTENGE--------NFSVGERQLLCMARALLRNSKI 1284
Cdd:PRK10418 89 ---RSAFNPL--HT--MHTHARETCLALgkpADDATLTAALEAVGLENAArvlklypfEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1285 ILLDEATASMDSktdtLVQSTIKEAFKSCT------VLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKPDSAFA 1357
Cdd:PRK10418 162 IIADEPTTDLDV----VAQARILDLLESIVqkralgMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
250
....*....|
gi 52138554 1358 -MLLAAEVGL 1366
Cdd:PRK10418 238 rSLVSAHLAL 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1144-1340 |
5.08e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTvGLEDLRTKLTMIPQDPVLFVG-TVRY 1220
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkEIDFKS-SKEALENGISMVHQELNLVLQrSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1221 NLdPLGSHTDEMLWhVLERTFMRDTImKLPEKLQAEV--TENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK- 1297
Cdd:PRK10982 93 NM-WLGRYPTKGMF-VDQDKMYRDTK-AIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKe 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 1298 TDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 1340
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1127-1353 |
5.29e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICTVGLE--D 1199
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMK---LPEKLQAEVTENGENFSVGERQLLCMAR 1276
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKkaaLWDEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1277 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR-LNTVLNCDLVLVMENGKVIEFDKPEVLAEKPD 1353
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1127-1366 |
5.44e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.06 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPLV---LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 1199
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQDP--VLFVGT----VRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVtengenfSVGERQLLC 1273
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETvlkdVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFEL-------SGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1274 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 1351
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
250
....*....|....*
gi 52138554 1352 PDsafaMLLAAEVGL 1366
Cdd:PRK13643 235 VD----FLKAHELGV 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
494-689 |
5.63e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.33 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL--LGQMQLQ---KGVVAVNGPLAY---------------VSQQAWI 553
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYsprtdtvdlrkeigmVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 FHGNVRENILFGEKYNHQRYQHTVHVcGLQKDLNSLPYGDltEIGER----GVNLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:PRK14239 98 FPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 630 PLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 689
Cdd:PRK14239 175 PTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
880-1018 |
6.03e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 62.12 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 880 SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAV-FPVVLVVLAGLAVI 958
Cdd:cd18546 73 DLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLdPRLALVALAALPPL 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 959 FlILLRIFHRGVQEL--KQVENISRSpwFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEN 1018
Cdd:cd18546 153 A-LATRWFRRRSSRAyrRARERIAAV--NADLQETLAGIRVVQAFRRERRNAERFAELSDDY 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1147-1364 |
6.70e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1147 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI-------------IIDEVDICTVGLEDLR-TKLTMIPQDPV 1212
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgADMAMIFQEPM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 LFVGTVRynldPLGSHTDEMLwhVLERTFMRDTIM----------KLPEKlQAEVTENGENFSVGERQLLCMARALLRNS 1282
Cdd:PRK10261 115 TSLNPVF----TVGEQIAESI--RLHQGASREEAMveakrmldqvRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1283 KIILLDEATASMdsktDTLVQSTIKEAFK------SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSA 1355
Cdd:PRK10261 188 AVLIADEPTTAL----DVTIQAQILQLIKvlqkemSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAPQHP 263
|
....*....
gi 52138554 1356 FAMLLAAEV 1364
Cdd:PRK10261 264 YTRALLAAV 272
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
494-685 |
8.39e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL--AYVSQQAWI-------------FHGNV 558
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYLdttlpltvnrflrLRPGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 R-ENILFGEKynhqRYQHT-VHVCGLQKdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD- 635
Cdd:PRK09544 97 KkEDILPALK----RVQAGhLIDAPMQK-------------------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDv 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52138554 636 -AHVGKHVFEECIKKTLkGKTVVLVTHQLQF-LESCDEVILLeDGEICEKGT 685
Cdd:PRK09544 154 nGQVALYDLIDQLRREL-DCAVLMVSHDLHLvMAKTDEVLCL-NHHICCSGT 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1143-1340 |
1.04e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.82 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL----RTKLTMIPQdpvlfvgtv 1218
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQ--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1219 RYNLDP--LGSHTDEM--LWHVLERTFMRDTIMKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATA 1292
Cdd:PRK10535 94 RYHLLShlTAAQNVEVpaVYAGLERKQRLLRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 52138554 1293 SMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVI 1340
Cdd:PRK10535 174 ALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-696 |
1.26e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLI-----------------SALLGQMQL--QKGVVAVNGPLAYVSQQAWIF 554
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmndkvsgyrysgDVLLGGRSIfnYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 HGNVRENILFGEKynhqryqhtVHVCGLQKDLNSLPYGDLTEIG----------ERGVNLSGGQRQRISLARAVYANRQL 624
Cdd:PRK14271 114 PMSIMDNVLAGVR---------AHKLVPRKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 625 YLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELME-----ERGRY 696
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSspkhaETARY 261
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
495-689 |
1.30e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAY-------VSQQAWI---------FHGN 557
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYdkkslleVRKTVGIvfqnpddqlFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:PRK13639 96 VEEDVAFGplnlglsKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 631 LSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 689
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
497-690 |
1.37e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG-----------------NV 558
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhEVVTRSPQDGLANGivyisedrkrdglvlgmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENI---------LFGEKYNHQRYQHTVhvcglqKDLNSL-----PYGDLTeIGergvNLSGGQRQRISLARAVYANRQL 624
Cdd:PRK10762 348 KENMsltalryfsRAGGSLKHADEQQAV------SDFIRLfniktPSMEQA-IG----LLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 625 YLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEIC-----EKGTHKELM 690
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRISgeftrEQATQEKLM 488
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
494-690 |
1.61e-09 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 60.10 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGK---VLGicGNvGSGKSSLISALLGQM-QLQKGVVAVNG-------------PLAYVS---QQAWI 553
Cdd:COG1119 16 KTILDDISWTVKPGEhwaILG--PN-GAGKSTLLSLITGDLpPTYGNDVRLFGerrggedvwelrkRIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 FHGNVRENIL---FG-----EKYN---HQRYQHTVHVCGLQkDLNSLPYGDLteigergvnlSGGQRQRISLARAVYANR 622
Cdd:COG1119 93 RDETVLDVVLsgfFDsiglyREPTdeqRERARELLELLGLA-HLADRPFGTL----------SQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 623 QLYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 690
Cdd:COG1119 162 ELLILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1148-1322 |
1.62e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.60 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1148 NLNIQSGQTVGIVGRTGSGKSSLG--MALFrlVEPASGTIIIDEVDiCTVGLEDLRtKLTMIPQDPVLFVG-TVRYN--- 1221
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLnlIAGF--LTPASGSLTLNGQD-HTTTPPSRR-PVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1222 -LDP---LGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD-- 1295
Cdd:PRK10771 95 gLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180
....*....|....*....|....*....
gi 52138554 1296 --SKTDTLVQSTIKEafKSCTVLTIAHRL 1322
Cdd:PRK10771 164 lrQEMLTLVSQVCQE--RQLTLLMVSHSL 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
497-679 |
1.79e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------------QMQL-------QKGVVAVNGPLAYVSQQAwi 553
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifegeELQAsnirdteRAGIAIIHQELALVKELS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 fhgnVRENILFGEK--------YN--HQRYQHTVHvcGLQKDLNslPYgdlTEIGergvNLSGGQRQRISLARAVYANRQ 623
Cdd:PRK13549 99 ----VLENIFLGNEitpggimdYDamYLRAQKLLA--QLKLDIN--PA---TPVG----NLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 624 LYLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGE 679
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLD--IIRDLKahGIACIYISHKLnEVKAISDTICVIRDGR 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
489-723 |
1.86e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.49 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 489 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------PLAYVSQQAWIFHGN---- 557
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeeNLWDIRNKAGMVFQNpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 -----VRENILFG-------------------EKYNHQRYQ-HTVHVcglqkdlnslpygdlteigergvnLSGGQRQRI 612
Cdd:PRK13633 98 ivatiVEEDVAFGpenlgippeeirervdeslKKVGMYEYRrHAPHL------------------------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 613 SLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKE-- 688
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEif 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 52138554 689 ----LMEERG----RYAKLIHNLRGLQFKDPEHIYNV-AMVETL 723
Cdd:PRK13633 233 keveMMKKIGldvpQVTELAYELKKEGVDIPSDILTIdEMVNEL 276
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
496-680 |
1.87e-09 |
|
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: 60.05 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVSQQAWIFHG-NVR 559
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGpN-GAGKTTLFNLITGFYRPTSGRILFDGrditglpPhriarlgIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGekynhqryQHTVHVCGLQKDLNSLPYG------------------DLTEI-GERGVNLSGGQRQRISLARAVYA 620
Cdd:COG0411 98 ENVLVA--------AHARLGRGLLAALLRLPRArreereareraeellervGLADRaDEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 621 NRQLYLLDDPLSAVdAHVGKHVFEECIKK--TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:COG0411 170 EPKLLLLDEPAAGL-NPEETEELAELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1119-1348 |
2.15e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1119 KDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLE 1198
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1199 DLRTKLTMIPQD-PVLFVGTVRyNLDPLGSHTdemlWH-VLERTFMRDTimklpEKLQAEVTENG---------ENFSVG 1267
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVR-ELVAIGRYP----WHgALGRFGAADR-----EKVEEAISLVGlkplahrlvDSLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1268 ERQLLCMARALLRNSKIILLDEATASMD--SKTDT--LVQSTIKEafKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 1342
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDiaHQVDVlaLVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229
|
....*.
gi 52138554 1343 DKPEVL 1348
Cdd:PRK10575 230 GTPAEL 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
479-680 |
2.28e-09 |
|
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: 59.27 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 479 SDQGVASPEWQSgspKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIfhgnV 558
Cdd:cd03267 22 SLKSLFKRKYRE---VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL----R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 559 RENILFGekynhQRYQ-----HTVHVCGLQKDLNSLPYG-------------DLTEIGERGV-NLSGGQRQRISLARAVY 619
Cdd:cd03267 95 RIGVVFG-----QKTQlwwdlPVIDSFYLLAAIYDLPPArfkkrldelsellDLEELLDTPVrQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 620 ANRQLYLLDDPLSAVDAhVGKHVFEECIKK--TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 680
Cdd:cd03267 170 HEPEILFLDEPTIGLDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1144-1364 |
2.64e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.38 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK--------LTMIPQDPV 1212
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHgtwDGEIYWSGSPLKASNIRDTERAgiviihqeLTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 L---FVGTvryNLDPLGSHTDEMLWHVLERTFMRDtiMKLPEklqAEVTENGENFSVGERQLLCMARALLRNSKIILLDE 1289
Cdd:TIGR02633 96 AeniFLGN---EITLPGGRMAYNAMYLRAKNLLRE--LQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1290 ATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEkpDSAFAMLLAAEV 1364
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSE--DDIITMMVGREI 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1143-1355 |
3.01e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVgtvRYNL 1222
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQ---RPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1223 DPLgSHTDEMLWHVLERTFM-----------RDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEAT 1291
Cdd:PRK14271 113 FPM-SIMDNVLAGVRAHKLVprkefrgvaqaRLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1292 ASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSA 1355
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1143-1348 |
3.12e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.12 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC---TVGLedLRTKLTMIPQDPVLFVG-TV 1218
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqTAKI--MREAVAIVPEGRRVFSRmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1219 RYNLDPLGSHTDEMLWHV-LERTFmrdtimKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 1297
Cdd:PRK11614 98 EENLAMGGFFAERDQFQErIKWVY------ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1298 TDTLVQSTIKEAF-KSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVL 1348
Cdd:PRK11614 172 IIQQIFDTIEQLReQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1140-1339 |
3.25e-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: 57.83 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1140 TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPV---LFV 1215
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1216 G-TVRYNLDpLGSHtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASM 1294
Cdd:cd03215 92 DlSVAENIA-LSSL-----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 52138554 1295 DSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 1339
Cdd:cd03215 136 DVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1150-1307 |
4.92e-09 |
|
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: 58.57 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1150 NIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdictvgLEDLRTKLTMIPQDpvlFVGTVRynlDPLGSHT 1229
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE--------LDTVSYKPQYIKAD---YEGTVR---DLLSSIT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1230 DEMLWHvlerTFMRDTIMKlPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIK 1307
Cdd:cd03237 87 KDFYTH----PYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
497-689 |
4.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.97 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLaYVSQQAW--------IFH--------GNVRE 560
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVWdirhkigmVFQnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFG---EKYNHQ----RYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSA 633
Cdd:PRK13650 102 DVAFGlenKGIPHEemkeRVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 634 VDAHvGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:PRK13650 171 LDPE-GRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
555-689 |
5.37e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.66 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 555 HGNVRENILFGEKYN-------HQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLL 627
Cdd:PRK11000 89 HLSVAENMSFGLKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 628 DDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 689
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIE-ISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
496-692 |
5.98e-09 |
|
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: 59.30 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLG---QMQLQKGVVAVNG-PLAYVSQQAW----------IFHG----- 556
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGeDLLKLSEKELrkirgreiqmIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 N--------VRENILFGEKYNH-QRYQHTVHV---CGL---QKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYAN 621
Cdd:COG0444 100 NpvmtvgdqIAEPLRIHGGLSKaEARERAIELlerVGLpdpERRLDRYPH-----------ELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 622 RQLYLLDDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELMEE 692
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAQIlnlLKD-LQREL-GLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1144-1339 |
6.37e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALfrlvepaSGTIIIDEVDICTVGL------------EDLRTKLT----MI 1207
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIELlgrtvqregrlaRDIRKSRAntgyIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1208 PQDPVLFVGTVRYNLdPLGSHTDEMLWHVLERTFMRdtiMKLPEKLQAeVTENG---------ENFSVGERQLLCMARAL 1278
Cdd:PRK09984 93 QQFNLVNRLSVLENV-LIGALGSTPFWRTCFSWFTR---EQKQRALQA-LTRVGmvhfahqrvSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1279 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKV 1339
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1142-1364 |
6.60e-09 |
|
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: 59.34 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1142 LVLDGLNLNIQ-----SGQTVgIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDlRTKLTMIP-------- 1208
Cdd:COG4148 9 LRRGGFTLDVDftlpgRGVTA-LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV-----LQD-SARGIFLPphrrrigy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1209 --QDPVLFVG-TVRYNLD------PLGSHTDEM--------LWHVLERTfmrdtimklPEKLqaevtengenfSVGERQL 1271
Cdd:COG4148 82 vfQEARLFPHlSVRGNLLygrkraPRAERRISFdevvellgIGHLLDRR---------PATL-----------SGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1272 LCMARALLRNSKIILLDEATASMD--SKTDTL--VQSTIKEAfkSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP- 1345
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDlaRKAEILpyLERLRDEL--DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLa 219
|
250
....*....|....*....
gi 52138554 1346 EVLAEKPDSAFAMLLAAEV 1364
Cdd:COG4148 220 EVLSRPDLLPLAGGEEAGS 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1125-1345 |
7.05e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1125 GEITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVGL---- 1197
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI-PANLkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1198 --EDLRTKLTMIPQDP--VLFVGTVRYNL--DP--LGSHTDEMLWHVLERTfmrdTIMKLPEKLqaeVTENGENFSVGER 1269
Cdd:PRK13645 84 evKRLRKEIGLVFQFPeyQLFQETIEKDIafGPvnLGENKQEAYKKVPELL----KLVQLPEDY---VKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1270 QLLCMARALLRNSKIILLDEATASMDSKTD----TLVQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 1344
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLFERLNKEYKKR--IIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
.
gi 52138554 1345 P 1345
Cdd:PRK13645 235 P 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1144-1340 |
7.35e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII--DEV------DICTVGLEDLRTKLTMIPQDPV--- 1212
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVtfngpkSSQEAGIGIIHQELNLIPQLTIaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 LFVGtvRYNLDPLGShtdeMLWHVlertfMRDTIMKLPEKLQAEVTEN---GEnFSVGERQLLCMARALLRNSKIILLDE 1289
Cdd:PRK10762 100 IFLG--REFVNRFGR----IDWKK-----MYAEADKLLARLNLRFSSDklvGE-LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 1290 ATasmDSKTDTLVQS---TIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 1340
Cdd:PRK10762 168 PT---DALTDTETESlfrVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
496-662 |
9.47e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 59.76 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV--NGPLAYVSQQAWIFHGNVRENILFGEKYNHQRY 573
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 574 QhtvhvcGL-QKDLNS-LPYGDLTEIGERGVN----------LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 641
Cdd:TIGR00954 547 R------GLsDKDLEQiLDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY 620
|
170 180
....*....|....*....|.
gi 52138554 642 VFEECIKktlKGKTVVLVTHQ 662
Cdd:TIGR00954 621 MYRLCRE---FGITLFSVSHR 638
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
494-680 |
1.12e-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: 56.50 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMqlqKGVVAVNGPLAYVSQQAWIFHGNVRENILF-GEKYNHQR 572
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNGIPYKEFAEKYPGEIIYvSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 573 Y---QHTVH-VCGLQKDLNSlpygdlteigeRGVnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHvFEECIK 648
Cdd:cd03233 97 TltvRETLDfALRCKGNEFV-----------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE-ILKCIR 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 52138554 649 ---KTLKGKTVVLVTHQLQFLESC-DEVILLEDGEI 680
Cdd:cd03233 163 tmaDVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQ 198
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
603-691 |
1.21e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 603 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQ-LQFLESCDEVILLEDGEIC 681
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
90
....*....|
gi 52138554 682 EKGTHKELME 691
Cdd:PRK14267 228 EVGPTRKVFE 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
496-690 |
1.23e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.20 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------------PLAYVSQQAWIF-HGNVRE 560
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 NILFGEKY-NHQRYQHTV-HVCGLQKDLnslpygdLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHV 638
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIkWVYELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 639 GKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELM 690
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
496-693 |
1.54e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.79 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLI---SALL----GQMQ-----------------------LQ-------KGVV 538
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtGTIEwifkdeknkkktkekekvleklvIQktrfkkiKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 539 AVNGPLAYVSQQA--WIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKD-LNSLPYgdlteigergvNLSGGQ 608
Cdd:PRK13651 102 EIRRRVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGLDESyLQRSPF-----------ELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 609 RQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKG-TH 686
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTY 250
|
....*..
gi 52138554 687 KELMEER 693
Cdd:PRK13651 251 DILSDNK 257
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
496-662 |
1.83e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP------LAYVSQQAWIFHGN-------VRENI 562
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVGHRSginpyltLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 LFGEKYNHQRYQHTvHVCGLQK--DLNSLPYGdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGK 640
Cdd:PRK13540 96 LYDIHFSPGAVGIT-ELCRLFSleHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 52138554 641 HVFEECIKKTLKGKTVVLVTHQ 662
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
487-725 |
2.41e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 487 EWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPlAYVSQQAW--------IFH--- 555
Cdd:PRK13642 13 KYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrkigmVFQnpd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 -----GNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDlteigERGVNLSGGQRQRISLARAVYANRQLYLLDD 629
Cdd:PRK13642 92 nqfvgATVEDDVAFGmENQGIPREEMIKRVDEALLAVNMLDFKT-----REPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 630 PLSAVDAhVGKHVFEECIKKtLKGK---TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL------MEERGR----Y 696
Cdd:PRK13642 167 STSMLDP-TGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELfatsedMVEIGLdvpfS 244
|
250 260 270
....*....|....*....|....*....|
gi 52138554 697 AKLIHNLRGLQFKDPE-HIYNVAMVETLKE 725
Cdd:PRK13642 245 SNLMKDLRKNGFDLPEkYLSEDELVELLAD 274
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1144-1341 |
2.45e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV--------DICTVGLEDLRTKLTMIPQdpvlfv 1215
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttAALAAGVAIIYQELHLVPE------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1216 GTVRYNLdplgshtdeMLWH-------VLERTFMRDTIMKLpEKLQAEVTENG--ENFSVGERQLLCMARALLRNSKIIL 1286
Cdd:PRK11288 94 MTVAENL---------YLGQlphkggiVNRRLLNYEAREQL-EHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1287 LDEATASMDSKTDTLVQSTIKEAFKSCTV-LTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRViLYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1127-1338 |
2.82e-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: 53.99 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdictvgledlRTKLTM 1206
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQdpvlfvgtvrynldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIIL 1286
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1287 LDEATASMDSKTDTLVQSTIKEaFKsCTVLTIAH-R--LNTVlnCDLVLVMENGK 1338
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-YP-GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1142-1353 |
2.83e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1142 LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFR---LVEP--ASGTIIIDEVDICTVGLE--DLRTKLTMIPQDPVLF 1214
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1215 VGTVRYNL------DPLGSHTDEMLWHVLERTFMRDTImklPEKLQaevtENGENFSVGERQLLCMARALLRNSKIILLD 1288
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEV---KDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1289 EATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV---------LNCDLVLV-MENGKVIEFDKPEVLAEKPD 1353
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAarvsdmtafFNVELTEGgGRYGYLVEFDRTEKIFNSPQ 251
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1136-1345 |
2.87e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1136 YRDNTP---LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV----DICTVG------------ 1196
Cdd:PRK13631 31 FDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdKKNNHElitnpyskkikn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1197 LEDLRTKLTMIPQDP--VLFVGTVRYNL--DP--LGSHTDE---MLWHVLERTFMRDTIMKlpeklqaevtENGENFSVG 1267
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDImfGPvaLGVKKSEakkLAKFYLNKMGLDDSYLE----------RSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1268 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 1345
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
494-707 |
3.55e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.15 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP--LAYVSQQAWIFHGNVREN------ILFG 565
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNattpgdITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 566 EKYNHQRYQHTVHVCGLQKD-----LNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 639
Cdd:PRK10253 100 ELVARGRYPHQPLFTRWRKEdeeavTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 640 KHVFE--ECIKKTlKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEergryAKLIHNLRGLQ 707
Cdd:PRK10253 180 IDLLEllSELNRE-KGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT-----AELIERIYGLR 244
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1143-1353 |
3.83e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIidevdictvgledlrtkltmipQDPVLFVGTVrynl 1222
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------------------RNGKLRIGYV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1223 dPLGSHTDEMLWHVLERtFMR-------DTIMKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATAS 1293
Cdd:PRK09544 73 -PQKLYLDTTLPLTVNR-FLRlrpgtkkEDILPALKRVQAGhlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 1294 MDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVL-NCDLVLVMeNGKVIEFDKPEVLAEKPD 1353
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1122-1321 |
4.71e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1122 PSRGEITFKDYRMRYrDNTPLV-------LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdict 1194
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1195 vgledlRTKLTMIPQDPVLFVGTVR----YnldPLGShtDEMLwhvlERTFMRDTIMKLPEKLQAE--VTENG------- 1261
Cdd:TIGR00954 514 ------KGKLFYVPQRPYMTLGTLRdqiiY---PDSS--EDMK----RRGLSDKDLEQILDNVQLThiLEREGgwsavqd 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1262 --ENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAfkSCTVLTIAHR 1321
Cdd:TIGR00954 579 wmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
500-694 |
5.04e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGqMQLQKGVVAVNG-PL------------AYVSQQAwifhgnvreNILFGE 566
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGqPLeawsaaelarhrAYLSQQQ---------TPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 567 KYNH--QRYQHT-VHVCGLQKDLN----SLPYGDLTEigeRGVN-LSGGQRQRISLA-------RAVYANRQLYLLDDPL 631
Cdd:PRK03695 85 PVFQylTLHQPDkTRTEAVASALNevaeALGLDDKLG---RSVNqLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 632 SAVDahVGKHVFEECIKKTL--KGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERG 694
Cdd:PRK03695 162 NSLD--VAQQAALDRLLSELcqQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
499-693 |
5.12e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ-KGVVAVNG-PLAYVSQQAWIFHG--NVRENilfgekynhQRYQ 574
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkPVDIRNPAQAIRAGiaMVPED---------RKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 575 HTVHVCGLQKD-----LNSLPY-GDLTEIGERGV--------------------NLSGGQRQRISLARAVYANRQLYLLD 628
Cdd:TIGR02633 349 GIVPILGVGKNitlsvLKSFCFkMRIDAAAELQIigsaiqrlkvktaspflpigRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 629 DPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
489-678 |
5.69e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 489 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------PLAY------VSQQ-AWI 553
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhKLAAqlgigiIYQElSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 FHGNVRENILFGE--------------KYNHQRYQHTVHVCGLQKDLNslpygdlteigERGVNLSGGQRQRISLARAVY 619
Cdd:PRK09700 93 DELTVLENLYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 620 ANRQLYLLDDPLSAVDAHVGKHVFeeCIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDG 678
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLF--LIMNQLRkeGTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
880-982 |
6.19e-08 |
|
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: 55.90 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 880 SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPV-VLVVLAGLAVI 958
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVlTLVTLAVVPLA 149
|
90 100
....*....|....*....|....
gi 52138554 959 FLILLRIfhrgvqeLKQVENISRS 982
Cdd:cd18551 150 FLIILPL-------GRRIRKASKR 166
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
492-684 |
6.93e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.09 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 492 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQmqLQKGVVAVNGPLAY--VSQQAWIFHGNVRENILFGEK-- 567
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI--LPAGVRQTAGRVLLdgKPVAPCALRGRKIATIMQNPRsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 568 YN--HQRYQHTVHVC---GLQKDLNSLPYGdLTEIG----ERGVNL-----SGGQRQRISLARAVYANRQLYLLDDPLSA 633
Cdd:PRK10418 92 FNplHTMHTHARETClalGKPADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 52138554 634 VDAHVGKHVFE--ECIKKTlKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKG 684
Cdd:PRK10418 171 LDVVAQARILDllESIVQK-RALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
497-698 |
7.62e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIfHGNVR--ENI-LFGekynhqry 573
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGL-NGQLTgiENIeLKG-------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 574 qhtvHVCGLQKDL------NSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSavdahVGKHVF-EE 645
Cdd:PRK13545 111 ----LMMGLTKEKikeiipEIIEFADIGKFIYQPVkTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQTFtKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 646 CIKK----TLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGRYAK 698
Cdd:PRK13545 182 CLDKmnefKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-663 |
8.13e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALlGQMQLQKGVVAVNGPLAYVSQQAW--------------------- 552
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYerrvnlnrlrrqvsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 553 IFHGNVRENILFGEKYNHQRYQhtVHVCGLQKdlNSLPYGDL-----TEIGERGVNLSGGQRQRISLARAVYANRQLYLL 627
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVGWRPK--LEIDDIVE--SALKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 52138554 628 DDPLSAVDAHVGKHVFEECIKKTLKGK-TVVLVTHQL 663
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
499-690 |
9.09e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL-----AYVSQQA-WIFHG-----NVRENI---- 562
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhPLhfgdySYRSQRIrMIFQDpstslNPRQRIsqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 563 ---------LFGEKYNHQRYQhTVHVCGLQKD-LNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLS 632
Cdd:PRK15112 111 dfplrlntdLEPEQREKQIIE-TLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 633 AVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELM 690
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
488-680 |
1.05e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAY-------------VSQQAWI 553
Cdd:PRK15439 18 SKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnPCARltpakahqlgiylVPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 554 FHG-NVRENILFG---EKYNHQRYQHTVHVCGLQKDLNSlPYGDLtEIGErgvnlsggqRQRISLARAVYANRQLYLLDD 629
Cdd:PRK15439 98 FPNlSVKENILFGlpkRQASMQKMKQLLAALGCQLDLDS-SAGSL-EVAD---------RQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 630 PLSAVDAHVGKHVFEEcIKKTL-KGKTVVLVTHQL-QFLESCDEVILLEDGEI 680
Cdd:PRK15439 167 PTASLTPAETERLFSR-IRELLaQGVGIVFISHKLpEIRQLADRISVMRDGTI 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1143-1347 |
1.14e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGlEDLRTKLTMIPQD-------PVL 1213
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRIRSPR-DAIRAGIAYVPEDrkgeglvLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1214 fvgTVRYN-----LDPLGSHTdeMLWHVLERTFMRDTIMKL---PEKLQAEVTengeNFSVGERQLLCMARALLRNSKII 1285
Cdd:COG1129 346 ---SIRENitlasLDRLSRGG--LLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1286 LLDEATASMD--SKTDtlVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMENGKVI-EFDKPEV 1347
Cdd:COG1129 417 ILDEPTRGIDvgAKAE--IYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
504-679 |
1.36e-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: 54.34 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 504 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-LAYVSQQAWI-FHGNVREnILFG---EKYNHQRYQHTVh 578
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYIKAdYEGTVRD-LLSSitkDFYTHPYFKTEI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 579 vcglqkdLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikkt 650
Cdd:cd03237 100 -------AKPL---QIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaSKVIRRFAEN----- 164
|
170 180
....*....|....*....|....*....
gi 52138554 651 lKGKTVVLVTHQLQFLESCDEVILLEDGE 679
Cdd:cd03237 165 -NEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
490-677 |
1.41e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 490 SGSPKSVLHNISFVvrKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAWIFHG- 556
Cdd:TIGR01257 941 SGRPAVDRLNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 NVRENILFGEKYNHQRYQHTvhvcglQKDLNSLpygdLTEIG------ERGVNLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEA------QLEMEAM----LEDTGlhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 52138554 631 LSAVDAHVGKHVFEECIKKTlKGKTVVLVTHQLqflescDEVILLED 677
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHM------DEADLLGD 1128
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
846-1001 |
1.46e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 54.88 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 846 HMYQLVYIASMVsVLMFGIIKGFTFTNTTLM---ASSSLHN-RV--FNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVR 919
Cdd:cd18565 49 PRGQLWLLGGLT-VAAFLLESLFQYLSGVLWrrfAQRVQHDlRTdtYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 920 LPFHAENFLQQFFMVVFILVIMA------AVFPVVLV-VLAGLAVIFLILLRIFHRGVQElkQVENISrspwfSHITSSI 992
Cdd:cd18565 128 LDDGANSIIRVVVTVLGIGAILFylnwqlALVALLPVpLIIAGTYWFQRRIEPRYRAVRE--AVGDLN-----ARLENNL 200
|
....*....
gi 52138554 993 QGLGVIHAY 1001
Cdd:cd18565 201 SGIAVIKAF 209
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
491-725 |
1.51e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.13 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVA----VNG-PLAYVSQQ----------AWIFH 555
Cdd:PRK11022 17 SAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAekleFNGqDLQRISEKerrnlvgaevAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 G---------NVRENILFGEKYnHQ------RYQHTVHVCGL------QKDLNSLPYgdlteigergvNLSGGQRQRISL 614
Cdd:PRK11022 97 DpmtslnpcyTVGFQIMEAIKV-HQggnkktRRQRAIDLLNQvgipdpASRLDVYPH-----------QLSGGMSQRVMI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 615 ARAVYANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELm 690
Cdd:PRK11022 165 AMAIACRPKLLIADEPTTALDVTIQAQIIElllELQQK--ENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI- 241
|
250 260 270
....*....|....*....|....*....|....*
gi 52138554 691 eergryaklihnlrglqFKDPEHIYNVAMVETLKE 725
Cdd:PRK11022 242 -----------------FRAPRHPYTQALLRALPE 259
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
494-693 |
1.54e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK-GVVAVNG-PLAYVSQQAWIFHG--------------- 556
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGkPVKIRNPQQAIAQGiamvpedrkrdgivp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 --NVRENIL--------FGEKYNHQRYQHTVhvcglQKDLNSL----PYGDLtEIGergvNLSGGQRQRISLARAVYANR 622
Cdd:PRK13549 355 vmGVGKNITlaaldrftGGSRIDDAAELKTI-----LESIQRLkvktASPEL-AIA----RLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 623 QLYLLDDPLSAVDahVG-KHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:PRK13549 425 KILILDEPTRGID--VGaKYEIYKLINQLVQqGVAIIVISSELpEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
862-1053 |
1.74e-07 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 54.41 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 862 FGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIM 941
Cdd:cd18576 52 FSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 942 AAVFP-VVLVVLAGLAVIFLIlLRIFHRGVQEL-KQV-ENISRSpwFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEn 1018
Cdd:cd18576 132 FFISWkLTLLMLATVPVVVLV-AVLFGRRIRKLsKKVqDELAEA--NTIVEETLQGIRVVKAFTREDYEIERYRKALER- 207
|
170 180 190
....*....|....*....|....*....|....*
gi 52138554 1019 sshllYFNCALRwFALRMDILMNIVTFVVALLVTL 1053
Cdd:cd18576 208 -----VVKLALK-RARIRALFSSFIIFLLFGAIVA 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1144-1295 |
1.76e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTvGLEDLRTKLTMIPQDPVLF-----VGTV 1218
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFhhltvAEHI 1024
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1219 RYNLDPLGSHTDEMLWHVleRTFMRDTimklpeKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 1295
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEM--EAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
496-690 |
1.80e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQM---QLQKGV-----VAVNG-PLAYV---------------SQQA 551
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGArvtgdVTLNGePLAAIdaprlarlravlpqaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 552 WIFhgNVRENILFGeKYNH-QRYQHTVHVCGLQKDlNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVyanRQLY---- 625
Cdd:PRK13547 96 FAF--SAREIVLLG-RYPHaRRAGALTHRDGEIAW-QALALAGATALVGRDVTtLSGGELARVQFARVL---AQLWpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 626 --------LLDDPLSAVD-AHvgKHVFEECIKKTLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELM 690
Cdd:PRK13547 169 aaqpprylLLDEPTAALDlAH--QHRLLDTVRRLARdwNLGVLAIVHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1127-1340 |
1.81e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLrtkLTM 1206
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQD-------PVLFVGTV---RYN----LDPLGSHTDEMLWHVLERTFMrdtimklpekLQAEVTENGEnFSVGERQLL 1272
Cdd:PRK15056 83 VPQSeevdwsfPVLVEDVVmmgRYGhmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1273 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAF-KSCTVLTIAHRLNTVLN-CDLVlVMENGKVI 1340
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
497-679 |
1.97e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG--------------NVREN 561
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkPVRIRSPRDAIALGigmvhqhfmlvpnlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGEKynhqryqhtvHVCGLQKDLNSLpYGDLTEIGER-GVN---------LSGGQRQRISLARAVYANRQLYLLDDPl 631
Cdd:COG3845 101 IVLGLE----------PTKGGRLDRKAA-RARIRELSERyGLDvdpdakvedLSVGEQQRVEILKALYRGARILILDEP- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 52138554 632 SAV--DAHVgKHVFEecIKKTLK--GKTVVLVTHQLQ-FLESCDEVILLEDGE 679
Cdd:COG3845 169 TAVltPQEA-DELFE--ILRRLAaeGKSIIFITHKLReVMAIADRVTVLRRGK 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
500-680 |
2.25e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 55.19 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWifhgnvRENI--------LFGEKYNH 570
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqPVTADNREAY------RQLFsavfsdfhLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 571 QRYQHTVHVcglQKDLNSLPYGDLTEIgERG----VNLSGGQRQRISLARAVYANRQLYLLD------DPlsavdahVGK 640
Cdd:COG4615 425 DGEADPARA---RELLERLELDHKVSV-EDGrfstTDLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 52138554 641 HVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 680
Cdd:COG4615 494 RVFYTELLPELKarGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
497-673 |
2.59e-07 |
|
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: 51.94 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLgqmqlqkgvvAVNGPLAYVSqqawifhgnvrenilFGEKYNHQRyqhT 576
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------YASGKARLIS---------------FLPKFSRNK---L 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 577 VHVCGLQKdLNSLPYGDLTeIGERGVNLSGGQRQRISLARAVYAN--RQLYLLDDPLSAVDaHVGKHVFEECIKKTL-KG 653
Cdd:cd03238 63 IFIDQLQF-LIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVIKGLIdLG 139
|
170 180
....*....|....*....|
gi 52138554 654 KTVVLVTHQLQFLESCDEVI 673
Cdd:cd03238 140 NTVILIEHNLDVLSSADWII 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
506-666 |
3.25e-07 |
|
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: 51.22 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 506 KGKVLGICGNVGSGKSSLISALLGQMQLQ-KGVVAVNGPLAYVSQQAWIFHgnvrenilfgekynhqryqhtvhvcglqk 584
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 585 dlnslpygdlTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEC------IKKTLKGKTVVL 658
Cdd:smart00382 52 ----------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLKSEKNLTVIL 121
|
....*...
gi 52138554 659 VTHQLQFL 666
Cdd:smart00382 122 TTNDEKDL 129
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1143-1346 |
4.80e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVL--------F 1214
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditvqeL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1215 VGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLpeklqaeVTENGENFSVGERQLLCMARALLRNSKIILLDEATASM 1294
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1295 D--SKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLV-MENGKVIEFDKPE 1346
Cdd:PRK10253 175 DisHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPK 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
504-679 |
5.07e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 504 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQqaWI---FHGNVRENILF-GEKYNHQRYQHTVhv 579
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLRSiTDDLGSSYYKSEI-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 580 cglqkdLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikktl 651
Cdd:PRK13409 438 ------IKPL---QLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE------ 502
|
170 180
....*....|....*....|....*...
gi 52138554 652 KGKTVVLVTHQLQFLESCDEVILLEDGE 679
Cdd:PRK13409 503 REATALVVDHDIYMIDYISDRLMVFEGE 530
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
500-693 |
5.91e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG-----------------NVREN 561
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkaegiipvhSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 562 ILFGEKYNHQRYQHTVHvcGLQKDLNSLPYGDLTEIGERG-----VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDa 636
Cdd:PRK11288 352 INISARRHHLRAGCLIN--NRWEAENADRFIRSLNIKTPSreqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID- 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 637 hVG-KHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:PRK11288 429 -VGaKHEIYNVIYELAAqGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQATERQ 487
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
827-958 |
9.02e-07 |
|
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: 52.48 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 827 SQNNKTACNVDQTLQDTKHHMYQLVYIAsmVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLM 906
Cdd:cd18577 30 TDFGSGESSPDEFLDDVNKYALYFVYLG--IGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELT 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 907 NRFSKDMDELDV----RLPFhaenFLQQFFMVV------FI------LVIMaAVFPVVLVVLAGLAVI 958
Cdd:cd18577 108 SRLTSDTNLIQDgigeKLGL----LIQSLSTFIagfiiaFIyswkltLVLL-ATLPLIAIVGGIMGKL 170
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
488-694 |
9.31e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAY-------VSQQA-------- 551
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkPLDYskrgllaLRQQVatvfqdpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 552 -WIFHGNVRENILFgekynhqryqhTVHVCGLQKDLNSLPYGD-LTEIGERGVN------LSGGQRQRISLARAVYANRQ 623
Cdd:PRK13638 88 qQIFYTDIDSDIAF-----------SLRNLGVPEAEITRRVDEaLTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52138554 624 LYLLDDPLSAVDAhVGKHVFEECIKKTL-KGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKG------THKELMEERG 694
Cdd:PRK13638 157 YLLLDEPTAGLDP-AGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
881-1049 |
9.95e-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: 52.15 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 881 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvRLPFHAenfLQQFFMVVFILVIMAAVFPVVLVVLAGLAVI-- 958
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVE-RLIADG---IPQGITNVLTLVGVAIILFSINPKLALLTLIpi 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 959 -FLILL-RIFHRGVQEL-KQVENISrspwfSHITS----SIQGLGVIHAYDKKDDCISKFKTLNDEnsshllYFNCALRw 1031
Cdd:cd18778 151 pFLALGaWLYSKKVRPRyRKVREAL-----GELNAllqdNLSGIREIQAFGREEEEAKRFEALSRR------YRKAQLR- 218
|
170 180
....*....|....*....|..
gi 52138554 1032 fALRmdiLMNI----VTFVVAL 1049
Cdd:cd18778 219 -AMK---LWAIfhplMEFLTSL 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1144-1339 |
1.04e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA-SGTIIID--EVDICTVgLEDLRTKLTMIPQD-------PVL 1213
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINgkPVDIRNP-AQAIRAGIAMVPEDrkrhgivPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1214 FVGTvRYNLDPLGSHTDEM-LWHVLERTFMRDTIMKLPEKLQAEVTENGeNFSVGERQLLCMARALLRNSKIILLDEATA 1292
Cdd:TIGR02633 355 GVGK-NITLSVLKSFCFKMrIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 52138554 1293 SMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 1339
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
851-1000 |
1.23e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 51.75 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 851 VYIASMVSVLMFGIIKGFTFTNTTLMASSS----LHNRVFNKIVRSPMSFFDTTPTGRLMnrfsKDMDELD-VRlpfhae 925
Cdd:cd18783 43 VLTIGVVIALLFEGILGYLRRYLLLVATTRidarLALRTFDRLLSLPIDFFERTPAGVLT----KHMQQIErIR------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 926 NFL-QQFFMVVF----ILVIMAAVF----PVVLVVLAGLAVIFLIL---LRIFHRGVQELKQVEnISRSpwfSHITSSIQ 993
Cdd:cd18783 113 QFLtGQLFGTLLdatsLLVFLPVLFfyspTLALVVLAFSALIALIIlafLPPFRRRLQALYRAE-GERQ---AFLVETVH 188
|
....*..
gi 52138554 994 GLGVIHA 1000
Cdd:cd18783 189 GIRTVKS 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
496-678 |
1.23e-06 |
|
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: 50.90 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV---NGP------------------LAYVSQ----- 549
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvdlaqaspreilalrrrtIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 550 ----------QAWIFHGnvrenilFGEKYNHQRYQHTVHVCGLQKDLNSLPygdlteigerGVNLSGGQRQRISLARAVY 619
Cdd:COG4778 106 prvsaldvvaEPLLERG-------VDREEARARARELLARLNLPERLWDLP----------PATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 620 ANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDG 678
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1139-1341 |
1.40e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1139 NTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALfrLVEPA----SGTIIIDEVDICTVGLEDlRTKLTMIP--QDPV 1212
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESILDLEPEE-RAHLGIFLafQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1213 LFVGT-------VRYN----------LDPLgshtdEMLWHVLERtfmrdtiMKLPEKLQAEVTEN-GENFSVGER---QL 1271
Cdd:CHL00131 95 EIPGVsnadflrLAYNskrkfqglpeLDPL-----EFLEIINEK-------LKLVGMDPSFLSRNvNEGFSGGEKkrnEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1272 LCMAralLRNSKIILLDEATASMDskTDTL--VQSTIKEAFKSCT-VLTIAH--RLNTVLNCDLVLVMENGKVIE 1341
Cdd:CHL00131 163 LQMA---LLDSELAILDETDSGLD--IDALkiIAEGINKLMTSENsIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1134-1353 |
1.46e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1134 MRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTV---GLEDLRTKLTM 1206
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggqiAPDHGEILFDGENIPAMsrsRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1207 IPQDPVLFVG-TVRYNLD-PLGSHTDemlwhvLERTFMRDTIMKlpeKLQAEVTENGEN-----FSVGERQLLCMARALL 1279
Cdd:PRK11831 89 LFQSGALFTDmNVFDNVAyPLREHTQ------LPAPLLHSTVMM---KLEAVGLRGAAKlmpseLSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52138554 1280 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 1353
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
488-709 |
1.56e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------------LAY 546
Cdd:PRK13649 12 YQAGTPfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvgLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 547 VSQQAWIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDL-NSLPYgdlteigergvNLSGGQRQRISLARAV 618
Cdd:PRK13649 92 QFPESQLFEETVLKDVAFGpqnfgvsQEEAEALAREKLALVGISESLfEKNPF-----------ELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 619 YANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHK------ELME 691
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGKPKdifqdvDFLE 240
|
250 260
....*....|....*....|....
gi 52138554 692 ERG----RYAKLIHNL--RGLQFK 709
Cdd:PRK13649 241 EKQlgvpKITKFAQRLadRGISFS 264
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
859-972 |
1.64e-06 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 51.48 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 859 VLMFGIIKGFTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD----VRLPFHAENFL 928
Cdd:cd18780 49 LGVVLIGSIATFLRSWLFTLAGervvarLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQnavtVNLSMLLRYLV 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 52138554 929 QQFFMVVFILV-------IMAAVFPVVLVVlaglAVIFLILLRIFHRGVQE 972
Cdd:cd18780 129 QIIGGLVFMFTtswkltlVMLSVVPPLSIG----AVIYGKYVRKLSKKFQD 175
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
604-689 |
1.71e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.07 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 604 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTH-QLQFLESCDEVILLEDGEICE 682
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDP-ENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 52138554 683 KGTHKEL 689
Cdd:PRK14247 226 WGPTREV 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
488-719 |
1.82e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.63 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 488 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-LAYVSQQAW---------IFHG- 556
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWravrsdiqmIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 557 ----NVRENI---------LFGEKYNHQRYQHTVHV----CGLQKDL-NSLPYgdlteigergvNLSGGQRQRISLARAV 618
Cdd:PRK15079 108 laslNPRMTIgeiiaeplrTYHPKLSRQEVKDRVKAmmlkVGLLPNLiNRYPH-----------EFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 619 YANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELmeerg 694
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVN--LLQQLQremGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV----- 249
|
250 260
....*....|....*....|....*
gi 52138554 695 ryaklihnlrglqFKDPEHIYNVAM 719
Cdd:PRK15079 250 -------------YHNPLHPYTKAL 261
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
178-411 |
1.87e-06 |
|
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: 51.40 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 178 VLFWALAWAINY-------RTAIRLKVALSTLIFENL--LSFKTLTHISAGEVLNILSSDSYS---LFEAALFCPLPATI 245
Cdd:cd07346 46 LLLALLRALLSYlrrylaaRLGQRVVFDLRRDLFRHLqrLSLSFFDRNRTGDLMSRLTSDVDAvqnLVSSGLLQLLSDVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 246 piLMVVCAVYAFFILGSTALVGISVY-LIFIPIQMFMAKLNSTFRRSAISVtDKRVQTMNEFLTCIKLIKMYAWEESFIN 324
Cdd:cd07346 126 --TLIGALVILFYLNWKLTLVALLLLpLYVLILRYFRRRIRKASREVRESL-AELSAFLQESLSGIRVVKAFAAEEREIE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 325 TIHDIRKREKKLLEKAGYVQSGNSALAPIVSTI--AIVSTFTCHIFLKRKLTAPVAFSVIAMFNVMKFSIAILPFSVKAV 402
Cdd:cd07346 203 RFREANRDLRDANLRAARLSALFSPLIGLLTALgtALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQL 282
|
....*....
gi 52138554 403 AEASVSLRR 411
Cdd:cd07346 283 QQALASLER 291
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
503-663 |
2.19e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 503 VVRKGKVLGICGNVGSGKSSLISALLGQM-----------------------QLQ--------KGVVAVNGPlAYVSQQA 551
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELipnlgdyeeepswdevlkrfrgtELQnyfkklynGEIKVVHKP-QYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 552 WIFHGNVREnILfgEKYNhQRyqhtvhvcGLQKDLNSLPygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:PRK13409 174 KVFKGKVRE-LL--KKVD-ER--------GKLDEVVERL--GLENILDRDIsELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*...
gi 52138554 631 LSAVDahvgkhVFE-----ECIKKTLKGKTVVLVTHQL 663
Cdd:PRK13409 240 TSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDL 271
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
500-689 |
2.35e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWI---------FHgnvreniLF----- 564
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkPVTAEQPEDYRklfsavftdFH-------LFdqllg 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 565 --GEKYNHQRYQHTVHVCGLQKDLnSLPYGDLTEIgergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgKHV 642
Cdd:PRK10522 415 peGKPANPALVEKWLERLKMAHKL-ELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RRE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 52138554 643 FEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICE-KGTHKEL 689
Cdd:PRK10522 488 FYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
496-660 |
2.45e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGplayvsqqawifHGNVRenilfGEKYNHQRYqh 575
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG------------KTATR-----GDRSRFMAY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 576 TVHVCGLQKDLNSL-----------------PYGDLTEIGERGV------NLSGGQRQRISLARAVYANRQLYLLDDPLS 632
Cdd:PRK13543 87 LGHLPGLKADLSTLenlhflcglhgrrakqmPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180
....*....|....*....|....*...
gi 52138554 633 AVDAHvGKHVFEECIKKTLKGKTVVLVT 660
Cdd:PRK13543 167 NLDLE-GITLVNRMISAHLRGGGAALVT 193
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
506-673 |
2.49e-06 |
|
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: 48.90 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 506 KGKVLGICGNVGSGKSSLISALLgqmqlqkgvvavngplayvsqqawifhgnvrenILFGEKYNHQRYQHTVHvCGLQKd 585
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGVK-AGCIV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 586 lnslPYGDLTEIGERgVNLSGGQRQRISLARAV----YANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTH 661
Cdd:cd03227 65 ----AAVSAELIFTR-LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
170
....*....|..
gi 52138554 662 QLQFLESCDEVI 673
Cdd:cd03227 140 LPELAELADKLI 151
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
850-1000 |
3.32e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 50.67 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 850 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSkdmdELD-VRlpfhaeNFL 928
Cdd:cd18782 46 VVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS----ELDtIR------GFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 929 QQ---------FFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLrIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIH 999
Cdd:cd18782 116 TGtalttlldvLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF-LFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVK 194
|
.
gi 52138554 1000 A 1000
Cdd:cd18782 195 A 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
497-679 |
4.81e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQ---------------------LQKGVVAVNGPLAYVSQQawifh 555
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkdsgsilfqgkeidfksskeaLENGISMVHQELNLVLQR----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 gNVRENILFGekynhqRYQHTvhvcGLQKDLNSLpYGDLTEI----------GERGVNLSGGQRQRISLARAVYANRQLY 625
Cdd:PRK10982 89 -SVMDNMWLG------RYPTK----GMFVDQDKM-YRDTKAIfdeldididpRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 626 LLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGE 679
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
497-684 |
5.54e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.54 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQQ--------AWIF-HGNVRE- 560
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrDLYALSEAerrrllrtEWGFvHQHPRDg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 561 ---------NIlfGEKYNHQRYQHtvhvcglqkdlnslpYGDLTE---------------IGERGVNLSGGQRQRISLAR 616
Cdd:PRK11701 102 lrmqvsaggNI--GERLMAVGARH---------------YGDIRAtagdwlerveidaarIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 617 AVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTL---KGKTVVLVTHQL---QFLesCDEVILLEDGEICEKG 684
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLD--LLRGLvreLGLAVVIVTHDLavaRLL--AHRLLVMKQGRVVESG 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
494-680 |
5.93e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 49.31 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGplAYVSQQ------AWI---F---------H 555
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG--KDVTKLpeykraKYIgrvFqdpmmgtapS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 556 GNVRENILF----GEKY------NHQRYQH------TVHVcGLQKDLNslpygdlTEIGergvNLSGGQRQRISLARAVY 619
Cdd:COG1101 97 MTIEENLALayrrGKRRglrrglTKKRRELfrellaTLGL-GLENRLD-------TKVG----LLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 620 ANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlKGKTVVLVTHQLQF-LESCDEVILLEDGEI 680
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
883-1047 |
6.70e-06 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 49.76 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 883 NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdVRLPFHA-ENFLQQFFMVVFILVIMAAVFP----VVLVVLAGLAV 957
Cdd:cd18549 79 RDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDI-SELAHHGpEDLFISIITIIGSFIILLTINVpltlIVFALLPLMII 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 958 IFLILLRIFHRGVQELK-QVENISrspwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDE--NSSHLLYFNCAlrWFAL 1034
Cdd:cd18549 158 FTIYFNKKMKKAFRRVReKIGEIN-----AQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRflESKKKAYKAMA--YFFS 230
|
170
....*....|...
gi 52138554 1035 RMDILMNIVTFVV 1047
Cdd:cd18549 231 GMNFFTNLLNLVV 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
504-693 |
6.71e-06 |
|
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: 50.55 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 504 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQqaWI---FHGNVRENI--LFGEKYNHQRYQHTVh 578
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YIspdYDGTVEEFLrsANTDDFGSSYYKTEI- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 579 vcglqkdLNSLpygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikkt 650
Cdd:COG1245 440 -------IKPL---GLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAEN----- 504
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52138554 651 lKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEER 693
Cdd:COG1245 505 -RGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMR 546
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
499-692 |
7.70e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 49.73 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW---------IF---HG--N----VR 559
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSGRELrplrrrmqmVFqdpYAslNprmtVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFGEKYNH--------QRYQHTVHVCGLQKD-LNSLPYgdlteigErgvnLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:COG4608 116 DIIAEPLRIHGlaskaerrERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 631 LSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 692
Cdd:COG4608 185 VSALDVSIQAQVlnlLED-LQDEL-GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
836-994 |
8.13e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 49.43 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 836 VDQTLQDTKHHMYQLVYIASMVSVLMFGI---IKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRF-SK 911
Cdd:cd18555 29 IDNVIVPGNLNLLNVLGIGILILFLLYGLfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAnSN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 912 DMdeldVRlpfhaeNFLQQ--------FFMVVFILVIMaAVFPVVL--VVLAGLAVIFLILLrIFHRGVQELKQVENISR 981
Cdd:cd18555 109 VY----IR------QILSNqvisliidLLLLVIYLIYM-LYYSPLLtlIVLLLGLLIVLLLL-LTRKKIKKLNQEEIVAQ 176
|
170
....*....|...
gi 52138554 982 SPWFSHITSSIQG 994
Cdd:cd18555 177 TKVQSYLTETLYG 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
489-715 |
9.55e-06 |
|
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: 50.07 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 489 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSslISALlGQMQLqkgvvaVNGPLAYVSQQAWiFHGnvrENIL-FGEK 567
Cdd:COG4172 18 QGGGTVEAVKGVSFDIAAGETLALVGESGSGKS--VTAL-SILRL------LPDPAAHPSGSIL-FDG---QDLLgLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 568 Y-NHQR-------YQ---------HTV----------HVcGLQK--------DLnslpygdLTEIG----ERGVN----- 603
Cdd:COG4172 85 ElRRIRgnriamiFQepmtslnplHTIgkqiaevlrlHR-GLSGaaararalEL-------LERVGipdpERRLDayphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 604 LSGGQRQRISLARAVyANR-QLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQL----QFlesCDEVILL 675
Cdd:COG4172 157 LSGGQRQRVMIAMAL-ANEpDLLIADEPTTALDVTVQAQILD--LLKDLQrelGMALLLITHDLgvvrRF---ADRVAVM 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 52138554 676 EDGEICEKGTHKELmeergryaklihnlrglqFKDPEHIY 715
Cdd:COG4172 231 RQGEIVEQGPTAEL------------------FAAPQHPY 252
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
605-736 |
9.74e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 605 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF-------EECikktlkGKTVVLVTHQLQFLES-CDEVILLE 676
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLnlmmdlqQEL------GLSYVFISHDLSVVEHiADEVMVMY 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 677 DGEICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMVE-TLKESPAQRDEDAVL 736
Cdd:PRK11308 230 LGRCVEKGTKEQI------------------FNNPRHPYTQALLSaTPRLNPDDRRERIKL 272
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
856-1013 |
1.01e-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: 48.98 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 856 MVSVLMFGII---KGFTFTNTTLMA--SSSLHNRV----FNKIVRSPMSFFDTTPTGRLMNRFSkdmDELDVRlpfhaeN 926
Cdd:cd18570 43 IISIGLILLYlfqSLLSYIRSYLLLklSQKLDIRLilgyFKHLLKLPLSFFETRKTGEIISRFN---DANKIR------E 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 927 FLQQ--------FFMVVFILVIMAA----VFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRspwfSHITSSIQG 994
Cdd:cd18570 114 AISSttislfldLLMVIISGIILFFynwkLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELN----SYLIESLKG 189
|
170
....*....|....*....
gi 52138554 995 LGVIHAYDKKDDCISKFKT 1013
Cdd:cd18570 190 IETIKSLNAEEQFLKKIEK 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
493-542 |
1.02e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 1.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 52138554 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG 542
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
881-968 |
1.05e-05 |
|
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: 49.02 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 881 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDEldVR-----LPFhaenFLQQFFMVVFILVIMAAVFPVV-LVVLAG 954
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSL--VQrflafGPF----LLGNLLTLVVGLVVMLVLSPPLaLVALAS 147
|
90
....*....|....
gi 52138554 955 LAVIFLILLRIFHR 968
Cdd:cd18543 148 LPPLVLVARRFRRR 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
497-693 |
1.18e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKG-------VVAVNGPLAyvSQQAW--IFHG--------NVR 559
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkEVTFNGPKS--SQEAGigIIHQelnlipqlTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 560 ENILFG-EKYNH-------QRYQHTVhvcGLQKDLNsLPYGDLTEIGErgvnLSGGQRQRISLARAVYANRQLYLLDDPL 631
Cdd:PRK10762 98 ENIFLGrEFVNRfgridwkKMYAEAD---KLLARLN-LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 632 SAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQ-FLESCDEVILLEDGE-ICEKGThKELMEER 693
Cdd:PRK10762 170 DALTDTETESLFR--VIRELKsqGRGIVYISHRLKeIFEICDDVTVFRDGQfIAEREV-ADLTEDS 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1143-1341 |
1.20e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.54 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDlrtklTMIPQDPVLF-----VGT 1217
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLpwrnvQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1218 VRYNLDPLGshtdemlwhvLERTFMRDTIMKLPEKLQAEvtENGENF----SVGERQLLCMARALLRNSKIILLDEATAS 1293
Cdd:PRK11248 91 VAFGLQLAG----------VEKMQRLEIAHQMLKKVGLE--GAEKRYiwqlSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1294 MDSKT----DTLVQSTIKEAFKSctVLTIAHRLN--TVLNCDLVLVMEN-GKVIE 1341
Cdd:PRK11248 159 LDAFTreqmQTLLLKLWQETGKQ--VLLITHDIEeaVFMATELVLLSPGpGRVVE 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
468-765 |
1.93e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 468 QRPELYSEQSRSDQGVASPEWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALL------------GQMQLQK 535
Cdd:PRK10261 3 HSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqagglvqcDKMLLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 536 ---GVVAVNGPLAYVSQQ------AWIFHGNVRE-NILF--GEKYN-----HQRYQHTVHVCGLQKDLNSLPYGDLTEIG 598
Cdd:PRK10261 83 rsrQVIELSEQSAAQMRHvrgadmAMIFQEPMTSlNPVFtvGEQIAesirlHQGASREEAMVEAKRMLDQVRIPEAQTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 599 ERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGKT---VVLVTHQLQFL-ESCDEVI 673
Cdd:PRK10261 163 SRYPHqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVVaEIADRVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 674 LLEDGEICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMVETLKESPAQRDEDA----VLASGDEKDEgKEPE 749
Cdd:PRK10261 241 VMYQGEAVETGSVEQI------------------FHAPQHPYTRALLAAVPQLGAMKGLDYprrfPLISLEHPAK-QEPP 301
|
330
....*....|....*.
gi 52138554 750 TEEfvDTNAPAHQLIQ 765
Cdd:PRK10261 302 IEQ--DTVVDGEPILQ 315
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1135-1341 |
2.16e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.26 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE--PASGTIIIDEVDIC--TVGLEDLRTKLTmiPQD 1210
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGreASLIDAIGRKGD--FKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1211 PVLFVGTVRYNldplgshtDEMLWhvlERTFmrdtimklpeklqaevtengENFSVGERQLLCMARALLRNSKIILLDEA 1290
Cdd:COG2401 115 AVELLNAVGLS--------DAVLW---LRRF--------------------KELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 1291 TASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTV--LNCDLVLVMENGKVIE 1341
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAgiTLVVATHHYDVIddLQPDLLIFVGYGGVPE 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1153-1346 |
2.24e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.83 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1153 SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIdevdictVGLEDLRTKLTMipqdpvlfvgtvrynldplgshtdem 1232
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLD-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1233 lwhvlertfmrdtimklpEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQS-------T 1305
Cdd:smart00382 48 ------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrllL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 52138554 1306 IKEAFKSCTVLTIAHRLNTVLncDLVLVMENGKVIEFDKPE 1346
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLIL 148
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
499-689 |
2.57e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGqmqlqkgVVAVNGplaYVSQQAwIFHG----NVRENILfgekyNHQRYQ 574
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMG-------LLAANG---RIGGSA-TFNGreilNLPEKEL-----NKLRAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 575 HTVHVcgLQKDLNSL-PY---GD-LTEI------------GERGVNL--------------------SGGQRQRISLARA 617
Cdd:PRK09473 98 QISMI--FQDPMTSLnPYmrvGEqLMEVlmlhkgmskaeaFEESVRMldavkmpearkrmkmyphefSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52138554 618 VYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLE-SCDEVILLEDGEICEKGTHKEL 689
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMT--LLNELKrefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
881-1049 |
2.64e-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: 47.86 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 881 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFP-------VVLVVLA 953
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWklalivlAVVPVLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 954 GLAVIFLILLRIFHRGVQELkqveNisrspwfSHITSS----IQGLGVIHAYDKKDDCISKFKTLNDE---NSSHLLYFN 1026
Cdd:cd18540 157 VVSIYFQKKILKAYRKVRKI----N-------SRITGAfnegITGAKTTKTLVREEKNLREFKELTEEmrrASVRAARLS 225
|
170 180
....*....|....*....|...
gi 52138554 1027 calrwfALRMDILMNIVTFVVAL 1049
Cdd:cd18540 226 ------ALFLPIVLFLGSIATAL 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1135-1351 |
2.80e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTPL-VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRtKLTM--IPQDP 1211
Cdd:COG3845 264 SVRDDRGVpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR-RLGVayIPEDR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1212 vLFVG-----TVRYNLDpLGSHTDEMLWHvleRTFM-RDTIMKLPEKLQAE---VTENGE----NFSVGERQLLCMARAL 1278
Cdd:COG3845 343 -LGRGlvpdmSVAENLI-LGRYRRPPFSR---GGFLdRKAIRAFAEELIEEfdvRTPGPDtparSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1279 LRNSKIIL-------LDEATASMdsktdtlVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVI-EFDKPEVL 1348
Cdd:COG3845 418 SRDPKLLIaaqptrgLDVGAIEF-------IHQRLLELRDAgAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEAT 490
|
...
gi 52138554 1349 AEK 1351
Cdd:COG3845 491 REE 493
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1127-1320 |
2.81e-05 |
|
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: 48.39 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEvdicTVGLEdlrt 1202
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMItgqeQPDSGTIEIGE----TVKLA---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1203 kltmipqdpvlFVGTVRYNLDPlgshtDEMLWHVLERTFmrDTIMKLPEKLQAEVTENGENF------------SVGERQ 1270
Cdd:TIGR03719 389 -----------YVDQSRDALDP-----NKTVWEEISGGL--DIIKLGKREIPSRAYVGRFNFkgsdqqkkvgqlSGGERN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 52138554 1271 LLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIkEAFKSCTVLtIAH 1320
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVV-ISH 498
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1126-1340 |
2.87e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.77 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1126 EITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-----------DEVD 1191
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1192 ICTVGLEDLRTKLTMIPQDPVLF--VGTV----RYNLdplgshtdemlwhvLERTFMRDTI-----MKLP----EKLQAE 1256
Cdd:PRK13651 82 KVLEKLVIQKTRFKKIKKIKEIRrrVGVVfqfaEYQL--------------FEQTIEKDIIfgpvsMGVSkeeaKKRAAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1257 VTE-----------NGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNT 1324
Cdd:PRK13651 148 YIElvgldesylqrSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDN 227
|
250
....*....|....*..
gi 52138554 1325 VLN-CDLVLVMENGKVI 1340
Cdd:PRK13651 228 VLEwTKRTIFFKDGKII 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1143-1344 |
3.30e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPAS--GTIIIDEVDIctvgledlrTKLTM-----IPQDPVLFV 1215
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP---------TKQILkrtgfVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1216 G-TVRynldplgshtdEMLWHV----LERTFMRDTIMKLPEKLQAEV----TEN---GENF----SVGERQLLCMARALL 1279
Cdd:PLN03211 154 HlTVR-----------ETLVFCsllrLPKSLTKQEKILVAESVISELgltkCENtiiGNSFirgiSGGERKRVSIAHEML 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52138554 1280 RNSKIILLDEATASMDSKTD-TLVQSTIKEAFKSCTVLTIAHRLNTVL--NCDLVLVMENGKVIEFDK 1344
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEGRCLFFGK 290
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1144-1320 |
3.50e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED---LRTKLTMIPQDPVLFVG-TVR 1219
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1220 YNLD-PL---GSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATA 1292
Cdd:PRK10908 98 DNVAiPLiiaGASGDDIRRRVsaaLDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|..
gi 52138554 1293 SMDsktDTLVQSTIK--EAFK--SCTVLTIAH 1320
Cdd:PRK10908 167 NLD---DALSEGILRlfEEFNrvGVTVLMATH 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
604-691 |
3.85e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 604 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 680
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
90
....*....|.
gi 52138554 681 CEKGTHKELME 691
Cdd:PRK11650 214 EQIGTPVEVYE 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1147-1358 |
4.64e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1147 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVGLEDL-RTKLTMIPQDPVLFVGTVRYNLD-- 1223
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1224 -PLGSHTDEmLWHVLERTFMRdtiMKLPEKLQAEVTengeNFSVGERQLLCMARALLR-------NSKIILLDEATASMD 1295
Cdd:PRK03695 94 qPDKTRTEA-VASALNEVAEA---LGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1296 SKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMENGKVI------EFDKPEVLAEkpdsAFAM 1358
Cdd:PRK03695 166 VAQQAALDRLLSElCQQGIAVVMSSHDLNHTLrHADRVWLLKQGKLLasgrrdEVLTPENLAQ----VFGV 232
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
836-1075 |
4.79e-05 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 46.86 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 836 VDQTLQDTKHHMYQLVYIASMVSVLMfGIIKGFTFTNTTLMAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRF 909
Cdd:cd18556 29 TDLLTSSSSDSYNYIVVLAALYVITI-SATKLLGFLSLYLQSSlrveliISISSSYFRYLYEQPKTFFVKENSGDITQRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 910 SKDMDELDVRLPFHAENF----LQQFFMVVFIL----VIMAAVFPVvlvvlagLAVIFLILLRIFHRGVQELKQ-VENIS 980
Cdd:cd18556 108 NQASNDLYTLVRNLSTNIlpplLQLIIAIVVILssgdYFVAALFLL-------YAVLFVINNTIFTKKIVSLRNdLMDAG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 981 RSPwFSHITSSIQGLGVIHAYDKKDDCISKFK-TLNDENSSHLLYFNCALRWFALrmDILMNIVTFVVALLVTLSFSSIS 1059
Cdd:cd18556 181 RKS-YSLLTDSVKNIVAAKQNNAFDFLFKRYEaTLTNDRNSQKRYWKLTFKMLIL--NSLLNVILFGLSFFYSLYGVVNG 257
|
250
....*....|....*....
gi 52138554 1060 ASSKG---LSLSYIIQLSG 1075
Cdd:cd18556 258 QVSIGhfvLITSYILLLST 276
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
799-1018 |
5.47e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 46.74 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 799 FFLMMGSSAFST---WWLGIWLDRgsqvVCASQNNKTACNVDQTLQDTKhhmYQLVYIASMVSVLMFGIIKGFTFTNTTL 875
Cdd:cd18564 5 LLALLLETALRLlepWPLKVVIDD----VLGDKPLPGLLGLAPLLGPDP---LALLLLAAAALVGIALLRGLASYAGTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 876 MAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhaENFLQ----QFFMVVFILVIMAAVF 945
Cdd:cd18564 78 TALvgqrvvLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAI--------QDLLVsgvlPLLTNLLTLVGMLGVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 946 PVV-----LVVLAGLAVIFLILLRI---FHRGVQELKQVEnisrspwfSHITSSIQ-GLG---VIHAYDKKDDCISKFKT 1013
Cdd:cd18564 150 FWLdwqlaLIALAVAPLLLLAARRFsrrIKEASREQRRRE--------GALASVAQeSLSairVVQAFGREEHEERRFAR 221
|
....*
gi 52138554 1014 LNDEN 1018
Cdd:cd18564 222 ENRKS 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1143-1295 |
8.06e-05 |
|
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: 45.18 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL 1222
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1223 DPLGS-HTDEMLWHVLertfmrdtimklpeklqAEVTENG------ENFSVGERQLLCMARALLRNSKIILLDEATASMD 1295
Cdd:cd03231 95 RFWHAdHSDEQVEEAL-----------------ARVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
853-1051 |
9.03e-05 |
|
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: 45.85 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 853 IASMVSVLmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhaENFLQQFF 932
Cdd:cd18548 47 LLALLGLI-AGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQV--------QNFVMMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 933 MVVF---ILVI------------MAAVFPVVLVVLAG-LAVIFLILLRIFHRgVQelKQVENISRSpwfshITSSIQGLG 996
Cdd:cd18548 118 RMLVrapIMLIgaiimafrinpkLALILLVAIPILALvVFLIMKKAIPLFKK-VQ--KKLDRLNRV-----VRENLTGIR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 997 VIHAYDKKDDCISKFKTLNDENSSHLLYfncALRWFALRMDILMNIVTFVVALLV 1051
Cdd:cd18548 190 VIRAFNREDYEEERFDKANDDLTDTSLK---AGRLMALLNPLMMLIMNLAIVAIL 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1143-1353 |
9.14e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.95 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDP--VLFVGTVRY 1220
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1221 NL--DPLGSHTD-EMLWHVLERTFMRDTIMKLPEKLQaevtengENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 1297
Cdd:PRK13652 99 DIafGPINLGLDeETVAHRVSSALHMLGLEELRDRVP-------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1298 -TDTLVQ--STIKEAFkSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 1353
Cdd:PRK13652 172 gVKELIDflNDLPETY-GMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
597-679 |
9.33e-05 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.68 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 597 IGERGVNLSGGQRQRISLARAVyANRQ----LYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEV 672
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWI 241
|
....*....
gi 52138554 673 ILL--EDGE 679
Cdd:cd03271 242 IDLgpEGGD 250
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
836-912 |
9.62e-05 |
|
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: 45.97 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 836 VDQTLQDTKHHMYQLVYIA-SMVSVLMFGIIkgFTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 908
Cdd:cd18573 26 ASKESGDIEIFGLSLKTFAlALLGVFVVGAA--ANFGRVYLLRIAGerivarLRKRLFKSILRQDAAFFDKNKTGELVSR 103
|
....
gi 52138554 909 FSKD 912
Cdd:cd18573 104 LSSD 107
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
850-961 |
9.66e-05 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 45.93 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 850 LVYIASMVSVLMFGIIkgftFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQ 929
Cdd:cd18589 44 LLTIASAVSEFVCDLI----YNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMW 119
|
90 100 110
....*....|....*....|....*....|...
gi 52138554 930 QFFMVVFILVIMAAVFP-VVLVVLAGLAVIFLI 961
Cdd:cd18589 120 YLARGLFLFIFMLWLSPkLALLTALGLPLLLLV 152
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1127-1356 |
1.12e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.09 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTVGLEDlRT 1202
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAEN-RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1203 KLTMIpQDPVLFVG-TVRYN----LDPLGSHTDEMLWHVLERTFMrdtimklpEKLQAEVTENGENFSVGERQLLCMARA 1277
Cdd:PRK09452 88 VNTVF-QSYALFPHmTVFENvafgLRMQKTPAAEITPRVMEALRM--------VQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1278 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDS 1354
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
..
gi 52138554 1355 AF 1356
Cdd:PRK09452 239 LF 240
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
861-961 |
1.15e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 45.76 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 861 MFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVI 940
Cdd:cd18784 51 VAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVF 130
|
90 100
....*....|....*....|..
gi 52138554 941 MAAV-FPVVLVVLAGLAVIFLI 961
Cdd:cd18784 131 MFKLsWQLSLVTLIGLPLIAIV 152
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
597-689 |
1.40e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 597 IGERGVNLSGGQRQRISLARAVYA---NRQLYLLDDPLSavdahvGKHvFEEcIKKTL--------KGKTVVLVTHQLQF 665
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTT------GLH-FDD-IKKLLevlqrlvdKGNTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|
gi 52138554 666 LESCDEVILL------EDGEICEKGTHKEL 689
Cdd:TIGR00630 895 IKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1127-1297 |
1.56e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1127 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTvgLEDLRT 1202
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVagleRITSGEIWIGGRVVNE--LEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1203 KLTMIPQDpvlfvgtvrYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKlQAEVTENGE-------NFSVGERQLLCMA 1275
Cdd:PRK11650 77 DIAMVFQN---------YALYPHMSVRENMAYGLKIRGMPKAEIEERVAE-AARILELEPlldrkprELSGGQRQRVAMG 146
|
170 180
....*....|....*....|..
gi 52138554 1276 RALLRNSKIILLDEATASMDSK 1297
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAK 168
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
859-915 |
1.84e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 45.23 E-value: 1.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 859 VLMFGIIKGFTFTNTTLMA------SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDE 915
Cdd:cd18574 49 LGLYLLQSLLTFAYISLLSvvgervAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQE 111
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
853-966 |
1.86e-04 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. 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). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 45.18 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 853 IASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRfskdMDELD-VRlpfhaeNFLQ-Q 930
Cdd:cd18588 49 LVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR----VRELEsIR------QFLTgS 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 52138554 931 FFMVV----FILVIMAAVF----PVVLVVLAGLAVIFLILLRIF 966
Cdd:cd18588 119 ALTLVldlvFSVVFLAVMFyyspTLTLIVLASLPLYALLSLLVT 162
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
594-745 |
2.00e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 594 LTEI-GERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDE 671
Cdd:NF000106 134 LTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHE 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 672 VILLEDGEICEKGTHKELMEERGRyaklihnlRGLQFKdPEHiynVAMVETLKESPAQRDEDAVLASGDEKDEG 745
Cdd:NF000106 214 LTVIDRGRVIADGKVDELKTKVGG--------RTLQIR-PAH---AAELDRMVGAIAQAGLDGIAGATADHEDG 275
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
503-679 |
2.32e-04 |
|
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: 43.33 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 503 VVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAwifhgnvrenilfgekynhqryqhtvhvcgl 582
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 583 qkdlnslpygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikktlKGKT 655
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKT 124
|
170 180
....*....|....*....|....
gi 52138554 656 VVLVTHQLQFLESCDEVILLEDGE 679
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
597-678 |
3.95e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 597 IGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVI 673
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELL 1091
|
....*
gi 52138554 674 LLEDG 678
Cdd:PLN03140 1092 LMKRG 1096
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1131-1339 |
4.70e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1131 DYRMRYRDNTPLVLDGL---------NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGlED 1199
Cdd:PRK11288 247 GYRPRPLGEVRLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDgkPIDIRSPR-DA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1200 LRTKLTMIPQD----PVLFVGTVRYNLD--------PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVtengeNFSVG 1267
Cdd:PRK11288 326 IRAGIMLCPEDrkaeGIIPVHSVADNINisarrhhlRAGCLINNRWEAENADRFIRSLNIKTPSREQLIM-----NLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1268 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 1339
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
605-679 |
5.24e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 5.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 605 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTlkgKTVVLVTHQLQFLESCDEVILLEDGE 679
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNTVVTDILHLHGQ 417
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
859-1053 |
5.50e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 43.63 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 859 VLMFGIIKGFTFTNTTLMA---SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVV 935
Cdd:cd18575 46 ALVLALASALRFYLVSWLGervVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 936 FILVIMAAVFP-VVLVVLAGLAVIFLILLrIFHRGVQEL-----KQVENISrspwfSHITSSIQGLGVIHAYDKKDDCIS 1009
Cdd:cd18575 126 GGLVMLFITSPkLTLLVLLVIPLVVLPII-LFGRRVRRLsrasqDRLADLS-----AFAEETLSAIKTVQAFTREDAERQ 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52138554 1010 KFKTLNDEnsshllYFNCALRWFALRmDILMNIVTFVVALLVTL 1053
Cdd:cd18575 200 RFATAVEA------AFAAALRRIRAR-ALLTALVIFLVFGAIVF 236
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
604-675 |
6.10e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 6.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52138554 604 LSGGQRQRISLARAVYA---NRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILL 675
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1151-1350 |
7.06e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.88 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1151 IQSGQTVGIVGRTGSGKSSLGMAL-FRL---VEpASGTIIIDEVDIctvGLEDLRTKLTMIPQDPvLFVG--TVRYNLD- 1223
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALaFRSpkgVK-GSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPtlTVREHLMf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1224 ----PLGSHTD-----EMLWHVLERTFMR---DTIMKLPEKLQAevtengenFSVGERQLLCMARALLRNSKIILLDEAT 1291
Cdd:TIGR00955 123 qahlRMPRRVTkkekrERVDEVLQALGLRkcaNTRIGVPGRVKG--------LSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52138554 1292 ASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNC--DLVLVMENGKVIEFDKPEVLAE 1350
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
604-691 |
7.29e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 604 LSGGQRQRISLARAVYANRQ--LYLLDDPlsavdaHVGKHVFE-ECIKKTLK-----GKTVVLVTHQLQFLESCDEVILL 675
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEP------SIGLHQRDnRRLINTLKrlrdlGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100
....*....|....*....|..
gi 52138554 676 ------EDGEICEKGTHKELME 691
Cdd:TIGR00630 563 gpgageHGGEVVASGTPEEILA 584
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1143-1196 |
1.56e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52138554 1143 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALF-----RLVepaSGTIIID--EVDICTVG 1196
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDgkEVDVSTVS 332
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1144-1341 |
1.93e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEvDICTVGleDLRT-----------KLTMIPQ 1209
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKVLSGVYPHgsyEGEILFDG-EVCRFK--DIRDsealgiviihqELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1210 DPV---LFVG--TVRY---NLDPLGSHTDEMLWHVlertfmrdtimKLPEKLQAEVTENGenfsVGERQLLCMARALLRN 1281
Cdd:NF040905 93 LSIaenIFLGneRAKRgviDWNETNRRARELLAKV-----------GLDESPDTLVTDIG----VGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52138554 1282 SKIILLDEATASM-DSKTDTLVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 1341
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLD-LLLE-LKAqgITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
603-679 |
2.43e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.23 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 603 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH----VGKHVFEecikktLKGkTVVLVTHQLQFLESCDEVIL-LED 677
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQE------YPG-TVVAVTHDRYFLDNVAGWILeLDR 233
|
..
gi 52138554 678 GE 679
Cdd:TIGR03719 234 GR 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
499-694 |
2.64e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 499 NISFVVRKGKVLGICGNVGSGKSS-------LISA------LLGQ------MQLQKGVvavngplAYVSQqAWIFHG--N 557
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPAsegeawLFGQpvdagdIATRRRV-------GYMSQ-AFSLYGelT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 558 VRENI-----LFG--EKYNHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDP 630
Cdd:NF033858 356 VRQNLelharLFHlpAAEIAARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52138554 631 LSAVDAhVGKHVFEEcikkTL------KGKTVVLVTHqlqFL---ESCDEVILLEDGEICEKGTHKELMEERG 694
Cdd:NF033858 425 TSGVDP-VARDMFWR----LLielsreDGVTIFISTH---FMneaERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1144-1320 |
3.91e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.69 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1144 LDGLNLNIQSGQ-----TVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQ----DpvlF 1214
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyispD---Y 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1215 VGTVRYNL-----DPLGSHtdeMLWH-VLERtfmrdtiMKLPEKLQAEVTEngenFSVGERQLLCMARALLRNSKIILLD 1288
Cdd:COG1245 415 DGTVEEFLrsantDDFGSS---YYKTeIIKP-------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190
....*....|....*....|....*....|....*
gi 52138554 1289 EATASMDSKTDTLVQSTIK---EAFKScTVLTIAH 1320
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRrfaENRGK-TAMVVDH 514
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
602-680 |
4.29e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 40.24 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 602 VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEECIKktlKGKTVVLVTHQLQFLESCD-EVILLED 677
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNR---VGVTVLMATHDIGLISRRSyRMLTLSD 212
|
...
gi 52138554 678 GEI 680
Cdd:PRK10908 213 GHL 215
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1156-1194 |
4.77e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 40.90 E-value: 4.77e-03
10 20 30
....*....|....*....|....*....|....*....
gi 52138554 1156 TVGIVGRTGSGKSSLGMALFRlvepaSGTIIIDEVDICT 1194
Cdd:COG3596 41 VIALVGKTGAGKSSLINALFG-----AEVAEVGVGRPCT 74
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
877-963 |
5.99e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 40.47 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 877 ASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlPFHAEnFLQQFFMVVFI-LVIMAAVFP------VVL 949
Cdd:cd18584 68 VKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALD---GYFAR-YLPQLVLAAIVpLLILVAVFPldwvsaLIL 143
|
90
....*....|....
gi 52138554 950 VVLAGLAVIFLILL 963
Cdd:cd18584 144 LVTAPLIPLFMILI 157
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1135-1322 |
6.47e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 40.04 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTpLVLDGLNLnIQSGQTVGIVGRTGSGKSS--------LGMALFRLVEPASGTIIID-----EVDICTVGLEDLR 1201
Cdd:cd03236 9 RYGPNS-FKLHRLPV-PREGQVLGLVGPNGIGKSTalkilagkLKPNLGKFDDPPDWDEILDefrgsELQNYFTKLLEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52138554 1202 TKLTMIPQD----PVLFVGTVRYNLDplgsHTDEmlwhvlerTFMRDTIMKLPEkLQAEVTENGENFSVGERQLLCMARA 1277
Cdd:cd03236 87 VKVIVKPQYvdliPKAVKGKVGELLK----KKDE--------RGKLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52138554 1278 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRL 1322
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDnYVLVVEHDL 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1135-1174 |
6.59e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 6.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 52138554 1135 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMAL 1174
Cdd:NF033858 10 RYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSL-LSL 46
|
|
| |
