|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
92-1468 |
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: 794.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 92 SKKIPEVPQTDDERKIYPLFHTNIISNMFFWWVLPILRVGYKRTIQPNDLFKMDPRMSIETLYDDFEKNMIYYFEKTRKK 171
Cdd:TIGR00957 186 SDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQ 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 172 -----YRKRHPEATEEEVMENA---------KLP----KHTVLRALLFTFKKQYFMSIVFAILANCTSGFNPMITKRLIE 233
Cdd:TIGR00957 266 pvsavYGKKDPSKPKGSSQLDAneevealivKSPhkprKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 234 FVEEKaifhsmHVNKGIGYAIGAclMMFVNG----LTFNHFFHTSQLTGVQAKSILTKAAMKKMFNASNYARHCFPNGKV 309
Cdd:TIGR00957 346 FVNDP------MAPDWQGYFYTG--LLFVCAclqtLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEI 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 310 TSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLGPIALVGIGIFFGGFFISLFAFKLILGFRIAANIFTDARVT 389
Cdd:TIGR00957 418 VNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIK 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 390 MMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIASLVTFLAMYKVNkggrqPGNI-- 467
Cdd:TIGR00957 498 LMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVD-----ENNIld 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 468 ----FASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRLQSLLEAPEDDPnQMIEMKP-SPGFDPKLALKmtHCSFEWEdy 542
Cdd:TIGR00957 573 aekaFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEP-DSIERRTiKPGEGNSITVH--NATFTWA-- 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 543 elndaieeakgeakdegkknkkkrkdtwgkpsastnkakrldnmlkdRDGPEDLEktsfrgfkDLNFDIKKGEFIMITGP 622
Cdd:TIGR00957 648 -----------------------------------------------RDLPPTLN--------GITFSIPEGALVAVVGQ 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 623 IGTGKSSLLNAMAGSMRKTDGKVEVNGDL-LMCGYPWIQNASVRDNIIFGSPFNKEKYDEVVRVCSLKADLDILPAGDMT 701
Cdd:TIGR00957 673 VGCGKSSLLSALLAEMDKVEGHVHMKGSVaYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRT 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 702 EIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECL--TGMLANKTRILATHQLSLIERASRVI 779
Cdd:TIGR00957 753 EIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVII 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 780 VLgTDGQV-DIGTVDELKARNQTLINLLQfSSQNSEKEDEEQEAVVAGELGQLKYESEV---------------KELTEL 843
Cdd:TIGR00957 833 VM-SGGKIsEMGSYQELLQRDGAFAEFLR-TYAPDEQQGHLEDSWTALVSGEGKEAKLIengmlvtdvvgkqlqRQLSAS 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 844 KKKATEMSQTANSGKIV-------ADGHTSSKEERAVNSISLKIYREYIKAaVGKwgFIALpLYAILVVGTTFCSLFSSV 916
Cdd:TIGR00957 911 SSDSGDQSRHHGSSAELqkaeakeETWKLMEADKAQTGQVELSVYWDYMKA-IGL--FITF-LSIFLFVCNHVSALASNY 986
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 917 WLSYWTENKFKN---RPPSFYMGLYsffvfAAFIFMNGQFTILCAM-----GIMASKWLNLRAVKRILHTPMSYIDTTPL 988
Cdd:TIGR00957 987 WLSLWTDDPMVNgtqNNTSLRLSVY-----GALGILQGFAVFGYSMavsigGIQASRVLHQDLLHNKLRSPMSFFERTPS 1061
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 989 GRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIFVLIADHYQSSGREIKRLEAVQRS 1068
Cdd:TIGR00957 1062 GNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRS 1141
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1069 FVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFALIITLLCVTRAFPISAAS 1148
Cdd:TIGR00957 1142 PVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGL 1221
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1149 VGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYaTELPLEASYRKPEMTPPESWPSMGEIIFENVDFAYRPGLPI 1228
Cdd:TIGR00957 1222 VGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEY-SETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDL 1300
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNL 1308
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 DPFNERTDDELWDALvrggaiakdDLPEVKL---QKPDEngthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQS 1385
Cdd:TIGR00957 1381 DPFSQYSDEEVWWAL---------ELAHLKTfvsALPDK-----------LDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1386 KILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWTLFSQEdSIFRSMCSR 1465
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAKD 1519
|
...
gi 398366407 1466 SGI 1468
Cdd:TIGR00957 1520 AGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
103-1477 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 783.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 103 DERKIYPLFHTNIISNMFFWWVLPILRVGYKRTIQPNDLFKMDPRMSIETLYDDFEKnmiyYFEKTRKKyrkrhpeatee 182
Cdd:PLN03130 222 GGEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQK----CWDEELKK----------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 183 evmenaklPKHTVLRALLFTFKKQYFMSIVFAILANCTSGFNPMITKRLIEFVEEKAifhsmHVNKGIGYAIGACLMMFV 262
Cdd:PLN03130 287 --------PKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGE-----PAWIGYIYAFSIFVGVVL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 263 NGLTFNHFFHTSQLTGVQAKSILTKAAMKKMFNASNYARHCFPNGKVTSFVTTDlariefALSFQPF------LAGFPAI 336
Cdd:PLN03130 354 GVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTD------AEALQQIcqqlhtLWSAPFR 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 337 LAICIVLLIVNLGPIALVGigiffggffislfAFKLILGFRIAANIF-------------TDARVTMMREVLNNIKMIKY 403
Cdd:PLN03130 428 IIIAMVLLYQQLGVASLIG-------------SLMLVLMFPIQTFIIskmqkltkeglqrTDKRIGLMNEVLAAMDTVKC 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 404 YTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIASLVTFlAMYKVNKGGRQPGNIFASLSLFQVLSLQMFF 483
Cdd:PLN03130 495 YAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLGGDLTPARAFTSLSLFAVLRFPLFM 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 484 LPIAIGTGIDMIIGLGRLQSLLEAPEDdpnqmiEMKPSPGFDPKL-ALKMTHCSFEWEdyelndaieeAKGEakdegkkn 562
Cdd:PLN03130 574 LPNLITQAVNANVSLKRLEELLLAEER------VLLPNPPLEPGLpAISIKNGYFSWD----------SKAE-------- 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 563 kkkrkdtwgKPSAStnkakrldnmlkdrdgpedlektsfrgfkDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSM-RKT 641
Cdd:PLN03130 630 ---------RPTLS-----------------------------NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 642 DGKVEVNGDLlmcGY----PWIQNASVRDNIIFGSPFNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKAR 717
Cdd:PLN03130 672 DASVVIRGTV---AYvpqvSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQR 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 718 INLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTGMLANKTRILATHQLSLIERASRvIVLGTDGQV-DIGTVDELK 796
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDR-IILVHEGMIkEEGTYEELS 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 797 ARNQTLINLLQFSSQNSEKEDEEQEAVVAGELGQLKYESEVkelTELKKKATEMSQtANSGKIVadghTSSKEERAVNSI 876
Cdd:PLN03130 828 NNGPLFQKLMENAGKMEEYVEENGEEEDDQTSSKPVANGNA---NNLKKDSSSKKK-SKEGKSV----LIKQEERETGVV 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 877 SLKIYREYIKAAVGKWGFIALPLYAILvvgTTFCSLFSSVWLSYWT-ENKFKNRPPSFYMGLYSFFVFaafifmnGQFTI 955
Cdd:PLN03130 900 SWKVLERYKNALGGAWVVMILFLCYVL---TEVFRVSSSTWLSEWTdQGTPKTHGPLFYNLIYALLSF-------GQVLV 969
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 956 LcamgIMASKWL---NLRAVKR--------ILHTPMSYIDTTPLGRILNRFTKDTDSLD-------NELTESLRLMTSQF 1017
Cdd:PLN03130 970 T----LLNSYWLimsSLYAAKRlhdamlgsILRAPMSFFHTNPLGRIINRFAKDLGDIDrnvavfvNMFLGQIFQLLSTF 1045
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1018 ANIVGVCVMCIvylpWfaiAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFlakS 1097
Cdd:PLN03130 1046 VLIGIVSTISL----W---AIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRM---A 1115
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1098 DFLINKM-NEAGYLVVVL--QRWVGIFLDMVAiafALIItllCVTRAFPIS-----------AASVGVLLTYVLQLPGLL 1163
Cdd:PLN03130 1116 EINGRSMdNNIRFTLVNMssNRWLAIRLETLG---GLMI---WLTASFAVMqngraenqaafASTMGLLLSYALNITSLL 1189
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1164 NTILRAMTQTENDMNSAERLVTYaTELPLEASYRKPEMTPPESWPSMGEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKI 1243
Cdd:PLN03130 1190 TAVLRLASLAENSLNAVERVGTY-IDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKV 1268
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1244 GICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNLDPFNERTDDELWDAL 1323
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESL 1348
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1324 VRggAIAKDDLpevklqkpdengthgKMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDG 1403
Cdd:PLN03130 1349 ER--AHLKDVI---------------RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1404 KIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWTLFSQEDSIFRSMCSRSG---------IVENDFE 1474
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTGaanaqylrsLVFGGDE 1491
|
...
gi 398366407 1475 NRS 1477
Cdd:PLN03130 1492 DRL 1494
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
106-1467 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 718.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 106 KIYPLFHTNIISNMFFWWVLPILRVGYKRTIQPNDLFKMDPRMSIETLYDDFEKnmiYYFEKTRKkyrkrhpeateeevm 185
Cdd:PLN03232 225 NICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQR---CWTEESRR--------------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 186 enaklPKHTVLRALLFTFKKQYFMSIVFAILANCTSGFNPMITKRLIEFVEEKAifhsmhvNKGIGYAIGacLMMFVnGL 265
Cdd:PLN03232 287 -----PKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGD-------PAWVGYVYA--FLIFF-GV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 266 TF-----NHFFHTSQLTGVQAKSILTKAAMKKMFNASNYARHCFPNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAIC 340
Cdd:PLN03232 352 TFgvlceSQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVS 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 341 IVLLIVNLGPIALVGigiffggffiSLFAFKLILGFRIAANIF----------TDARVTMMREVLNNIKMIKYYTWEDAY 410
Cdd:PLN03232 432 MVLLYQQLGVASLFG----------SLILFLLIPLQTLIVRKMrkltkeglqwTDKRVGIINEILASMDTVKCYAWEKSF 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 411 EKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIASLVTFlAMYKVNKGGRQPGNIFASLSLFQVLSLQMFFLPIAIGT 490
Cdd:PLN03232 502 ESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSF-GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQ 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 491 GIDMIIGLGRLQSLLEAPEDDpnqmieMKPSPGFDPKL-ALKMTHCSFEWEdyelndaieeakgeakdegkknkkkrkdt 569
Cdd:PLN03232 581 VVNANVSLQRIEELLLSEERI------LAQNPPLQPGApAISIKNGYFSWD----------------------------- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 570 wgkpsastnkakrldnmlkdrdgpedlEKTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKT-DGKVEVN 648
Cdd:PLN03232 626 ---------------------------SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 649 GDLLMC-GYPWIQNASVRDNIIFGSPFNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKK 727
Cdd:PLN03232 679 GSVAYVpQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 728 KDIYLFDDVLSAVDSRVGKHIMDECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDELkARNQTLINLLQ 807
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLFKKLM 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 808 fssQNSEKEDEEQEAVVAGElgqlkyesevkELTELKKKATEMSQTANSGKIVADGHTSS----KEERAVNSISLKIYRE 883
Cdd:PLN03232 838 ---ENAGKMDATQEVNTNDE-----------NILKLGPTVTIDVSERNLGSTKQGKRGRSvlvkQEERETGIISWNVLMR 903
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 884 YIKAAVGKWGFIALPLYAILvvgTTFCSLFSSVWLSYWT-ENKFKNRPPSFYMGLYSFFVFA--AFIFMNGQFTIlcAMG 960
Cdd:PLN03232 904 YNKAVGGLWVVMILLVCYLT---TEVLRVSSSTWLSIWTdQSTPKSYSPGFYIVVYALLGFGqvAVTFTNSFWLI--SSS 978
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 961 IMASKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPF 1040
Cdd:PLN03232 979 LHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMP 1058
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1041 LLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERfLAKSD---------FLINKMNEAGYLV 1111
Cdd:PLN03232 1059 LLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDR-MAKINgksmdnnirFTLANTSSNRWLT 1137
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1112 VVLQRWVGIFLDMVAiAFALIITLLCVTRAfpISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYaTELP 1191
Cdd:PLN03232 1138 IRLETLGGVMIWLTA-TFAVLRNGNAENQA--GFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNY-IDLP 1213
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1192 LEASYRKPEMTPPESWPSMGEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKI 1271
Cdd:PLN03232 1214 SEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1272 LIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNLDPFNERTDDELWDALVRggAIAKDDLpevklqkpdengthgKM 1351
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALER--AHIKDVI---------------DR 1356
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1352 HKFHLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNY 1431
Cdd:PLN03232 1357 NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC 1436
|
1370 1380 1390
....*....|....*....|....*....|....*.
gi 398366407 1432 DRILVLEKGEVAEFDTPWTLFSQEDSIFRSMCSRSG 1467
Cdd:PLN03232 1437 DKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
196-1462 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 611.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 196 LRALLFTFKKQYFMSIVFAILANCTSGFNPMITKRLIEFVEEKaifhsmhvNKGIGYAIGACLMMFVNGLT---FNH-FF 271
Cdd:PTZ00243 235 LRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDAD--------NATWGRGLGLVLTLFLTQLIqsvCLHrFY 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 272 HTSQLTGVQAKSILTKAAMKKMFNASN--YARHCFPNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLG 349
Cdd:PTZ00243 307 YISIRCGLQYRSALNALIFEKCFTISSksLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 350 PIALVGIGIFFGGFFISLFAFKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQ 429
Cdd:PTZ00243 387 WCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQ 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 430 LSRNFLIAMAMSLPSIASLVTFLAMYKVNKGGRqPGNIFASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRLQSLLEAPE 509
Cdd:PTZ00243 467 LARVATSFVNNATPTLMIAVVFTVYYLLGHELT-PEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDN 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 510 DDPNQMIEM--------KPSP--------------GFDP-KLAL----KMTHCS--FEWEDYELND---------AIEEA 551
Cdd:PTZ00243 546 ATCSTVQDMeeywreqrEHSTacqlaavlenvdvtAFVPvKLPRapkvKTSLLSraLRMLCCEQCRptkrhpspsVVVED 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 552 KGEAKDEGKKNKKKRKDTWG---KPSASTNKAKRldNMLKDRDGPEDLEKTSFRgfkDLNFDIKKGEFIMITGPIGTGKS 628
Cdd:PTZ00243 626 TDYGSPSSASRHIVEGGTGGgheATPTSERSAKT--PKMKTDDFFELEPKVLLR---DVSVSVPRGKLTVVLGATGSGKS 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 629 SLLNAMAGSMRKTDGKVEVNGDLlmcGY----PWIQNASVRDNIIFGSPFNKEKYDEVVRVCSLKADLDILPAGDMTEIG 704
Cdd:PTZ00243 701 TLLQSLLSQFEISEGRVWAERSI---AYvpqqAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIG 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 705 ERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTGMLANKTRILATHQLSLIERASRVIVLGtD 784
Cdd:PTZ00243 778 EKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALG-D 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 785 GQVDIGTVDELKARN---QTLINLLQFS--SQNSEKEDEEQEAVVAGELGQLKYESEVKEltelkKKATEMSQTANSGki 859
Cdd:PTZ00243 857 GRVEFSGSSADFMRTslyATLAAELKENkdSKEGDADAEVAEVDAAPGGAVDHEPPVAKQ-----EGNAEGGDGAALD-- 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 860 VADGHTSSKEERAVNSISLKIYREYIKAAVG--KWGFIalplYAILVVgTTFCSLFSSVWLSYWTENKFKNRPPSfYMGL 937
Cdd:PTZ00243 930 AAAGRLMTREEKASGSVPWSTYVAYLRFCGGlhAAGFV----LATFAV-TELVTVSSGVWLSMWSTRSFKLSAAT-YLYV 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 938 YSFFVFAAFIFMNGQFTILCAMGIMASKWLN---LRAVKRilhTPMSYIDTTPLGRILNRFTKDTDSLDNELTES-LRLM 1013
Cdd:PTZ00243 1004 YLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHrdlLRSVSR---GTMSFFDTTPLGRILNRFSRDIDILDNTLPMSyLYLL 1080
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1014 TSQFanivGVCVMCIVYL---PWFAIAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQ 1090
Cdd:PTZ00243 1081 QCLF----SICSSILVTSasqPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKA 1156
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1091 ERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFALIITLLCVT----RAFPISAASVGVLLTYVLQLPGLLNTI 1166
Cdd:PTZ00243 1157 HLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIgtmlRATSQEIGLVSLSLTMAMQTTATLNWL 1236
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1167 LRAMTQTENDMNSAERLVTYATELPLEAsyrKPEM----------------------TPPESWPSM-------GEIIFEN 1217
Cdd:PTZ00243 1237 VRQVATVEADMNSVERLLYYTDEVPHED---MPELdeevdalerrtgmaadvtgtvvIEPASPTSAaphpvqaGSLVFEG 1313
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1218 VDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDP 1297
Cdd:PTZ00243 1314 VQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP 1393
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1298 VLFRGTIRKNLDPFNERTDDELWDALvrggaiakdDLpeVKLQKPDENGTHGkmhkfhLDQAVEEEGSNFSLGERQLLAL 1377
Cdd:PTZ00243 1394 VLFDGTVRQNVDPFLEASSAEVWAAL---------EL--VGLRERVASESEG------IDSRVLEGGSNYSVGQRQLMCM 1456
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1378 TRALV-RQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:PTZ00243 1457 ARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
....*.
gi 398366407 1457 SIFRSM 1462
Cdd:PTZ00243 1537 SIFHSM 1542
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
897-1187 |
1.06e-150 |
|
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: 459.25 E-value: 1.06e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 897 LPLYAILVVGTTFCSLFSSVWLSYWTENKFkNRPPSFYMGLYSFFVFAAFIFMNGQFTILCAMGIMASKWLNLRAVKRIL 976
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFF-GLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 977 HTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIFVLIADHYQSSG 1056
Cdd:cd18606 80 RAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1057 REIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFALIITLL 1136
Cdd:cd18606 160 RELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 398366407 1137 CVTRAFPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYA 1187
Cdd:cd18606 240 CVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
209-501 |
1.13e-119 |
|
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: 376.02 E-value: 1.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 209 MSIVFAILANCTSGFNPMITKRLIEFVEEKA-IFHSMHVNKGIGYAIGACLMMFVNGLTFNHFFHTSQLTGVQAKSILTK 287
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYlGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 288 AAMKKMFNASNYARHCFPNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLGPIALVGIGIFFGGFFISL 367
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 368 FAFKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIAS 447
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398366407 448 LVTFLAMYKVNkGGRQPGNIFASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRL 501
Cdd:cd18597 241 MLSFITYYATG-HTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
109-1466 |
1.77e-116 |
|
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: 401.21 E-value: 1.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 109 PLFHTNIISNMFFWWVLPILRVGYKRTIQPNDLFKMDPRMSIETLYDDFEKNMiyyfektrkkyrkrhpeatEEEVMENA 188
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREW-------------------DRELASAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 189 KLPKhtVLRALLFTFKKQYFMSIVFAILANCTSGFNPMITKRLIEFVEEkaiFHSMHVNKGIGYAIGACLMMFVNGLTFN 268
Cdd:TIGR01271 66 KNPK--LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDP---FNAPEREIAYYLALGLCLLFIVRTLLLH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 269 HFFHTSQLTGVQAKSILTKAAMKKMFNASNYARHCFPNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNL 348
Cdd:TIGR01271 141 PAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 349 GPIALVGIGIFFGGFFISLFAFKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKM 428
Cdd:TIGR01271 221 EVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 429 QLSRNFLIAmamSLPSIASLVTFLAM--YKVNKGGRQPgNIFASLSLFQVLSLQMFF-LPIAIGTGIDMIIGLGRLQSLL 505
Cdd:TIGR01271 301 AYLRYFYSS---AFFFSGFFVVFLSVvpYALIKGIILR-RIFTTISYCIVLRMTVTRqFPGAIQTWYDSLGAITKIQDFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 506 EAPEddpNQMIEMKPSpgfdpKLALKMTHCSFEWedyelndaiEEAKGEAKDegkknkkkrkdtwgkpsastnKAKRLDN 585
Cdd:TIGR01271 377 CKEE---YKTLEYNLT-----TTEVEMVNVTASW---------DEGIGELFE---------------------KIKQNNK 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 586 MLKDRDGPEDLEKTSFRGF-----KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCG-YPWI 659
Cdd:TIGR01271 419 ARKQPNGDDGLFFSNFSLYvtpvlKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPqTSWI 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 660 QNASVRDNIIFGSPFNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSA 739
Cdd:TIGR01271 499 MPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 740 VDSRVGKHIMDECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKAR----NQTLINLLQFSSQNSEK 815
Cdd:TIGR01271 579 LDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKrpdfSSLLLGLEAFDNFSAER 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 816 ED------------EEQEAVVAG-------------ELGQLKYESEV------------KELTELKKKATEMSQTANS-- 856
Cdd:TIGR01271 659 RNsiltetlrrvsiDGDSTVFSGpetikqsfkqpppEFAEKRKQSIIlnpiasarkfsfVQMGPQKAQATTIEDAVREps 738
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 857 -------------------GKIVADG----------------HTSSKEE---------RAVNSIS--------LKIY--- 881
Cdd:TIGR01271 739 erkfslvpedeqgeeslprGNQYHHGlqhqaqrrqsvlqlmtHSNRGENrreqlqtsfRKKSSITqqnelaseLDIYsrr 818
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 882 ------------------------REYIKAAVGKW-----------GFIALPLYAILVVGTTFCSLFSSVWL-------- 918
Cdd:TIGR01271 819 lskdsvyeiseeineedlkecfadERENVFETTTWntylryittnrNLVFVLIFCLVIFLAEVAASLLGLWLitdnpsap 898
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 919 -----SYWTENKFKNRPPSFYMGLYSFFVFaaFIFMNGQFTILcAMG-----------IMASKWLNLRAVKRILHTPMSY 982
Cdd:TIGR01271 899 nyvdqQHANASSPDVQKPVIITPTSAYYIF--YIYVGTADSVL-ALGffrglplvhtlLTVSKRLHEQMLHSVLQAPMAV 975
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 983 IDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVG-VCVMCIVYLPWFAIAIPfLLVIFVLIADHYQSSGREIKR 1061
Cdd:TIGR01271 976 LNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGaIFVVSVLQPYIFIAAIP-VAVIFIMLRAYFLRTSQQLKQ 1054
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1062 LEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFALIITLLCVTrA 1141
Cdd:TIGR01271 1055 LESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIG-T 1133
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1142 FPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYaTELPLEASYRKPEMTPPES--------------W 1207
Cdd:TIGR01271 1134 NQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKF-IDLPQEEPRPSGGGGKYQLstvlvienphaqkcW 1212
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1208 PSMGEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNElTAGKILIDNVDISQLGLFDLR 1287
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR 1291
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQDPVLFRGTIRKNLDPFNERTDDELWDALVRGGaiakddLPEVKLQKPDEngthgkmhkfhLDQAVEEEGSNF 1367
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVG------LKSVIEQFPDK-----------LDFVLVDGGYVL 1354
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1368 SLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDT 1447
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
1530
....*....|....*....
gi 398366407 1448 PWTLFSqEDSIFRSMCSRS 1466
Cdd:TIGR01271 1435 IQKLLN-ETSLFKQAMSAA 1452
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1211-1448 |
3.02e-114 |
|
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: 358.34 E-value: 3.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1211 GEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKL 1290
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDPVLFRGTIRKNLDPFNERTDDELWDALVRGGaiakddLPEVKLQKPDengthgkmhkfHLDQAVEEEGSNFSLG 1370
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVG------LKEFVESLPG-----------GLDTVVEEGGENLSVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTP 1448
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
878-1462 |
9.60e-109 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 357.17 E-value: 9.60e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 878 LKIYREYikaavgKWGFIALplyAILVVGTTFCSLFSSVWLSYWTENKFKNRPPS---FYMGLYSFFVFAAFIFMNGQFT 954
Cdd:COG1132 13 LRYLRPY------RGLLILA---LLLLLLSALLELLLPLLLGRIIDALLAGGDLSallLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 955 ILCAMGIMASKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWF 1034
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1035 AIAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVL 1114
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1115 QRWVGIFLDMVAIAFALIITLLCVTRAF--PISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTY-ATELP 1191
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLsgSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELlDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1192 LEASYRKPEMTPPEswpsmGEIIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKI 1271
Cdd:COG1132 324 IPDPPGAVPLPPVR-----GEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1272 LIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNL---DPfnERTDDELWDALVRGGA---IAKddLPEvklqkpden 1345
Cdd:COG1132 398 LIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAhefIEA--LPD--------- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1346 gthGkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRL 1425
Cdd:COG1132 465 ---G------YDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRL 535
|
570 580 590
....*....|....*....|....*....|....*..
gi 398366407 1426 KTIVNYDRILVLEKGEVAEFDTPWTLfSQEDSIFRSM 1462
Cdd:COG1132 536 STIRNADRILVLDDGRIVEQGTHEEL-LARGGLYARL 571
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
597-786 |
1.32e-99 |
|
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: 317.10 E-value: 1.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 597 EKTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDL-LMCGYPWIQNASVRDNIIFGSPFN 675
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIaYVSQEPWIQNGTIRENILFGKPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 676 KEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTG 755
Cdd:cd03250 94 EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILG 173
|
170 180 190
....*....|....*....|....*....|..
gi 398366407 756 MLA-NKTRILATHQLSLIERASRVIVLGtDGQ 786
Cdd:cd03250 174 LLLnNKTRILVTHQLQLLPHADQIVVLD-NGR 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
967-1448 |
5.56e-91 |
|
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: 311.38 E-value: 5.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 967 LNLRAVKRILHTPMSYIDTTPLGRILNRFtKDTDSLDNelteslrLMTSQFANIVGVCVMCIVYL-------PWFA---- 1035
Cdd:COG2274 231 LSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIRE-------FLTGSLLTALLDLLFVLIFLivlffysPPLAlvvl 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1036 IAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYnnlnEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQ 1115
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLV----ETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1116 RWVGIFLDMVAIAFALIITLLCVTRAF--PIS-----AAS--VGVLLTYVLQLPGLLNTILRAMTqtendmnSAERL--V 1184
Cdd:COG2274 379 NLLSTLSGLLQQLATVALLWLGAYLVIdgQLTlgqliAFNilSGRFLAPVAQLIGLLQRFQDAKI-------ALERLddI 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1185 TyatELPLEASYRKPEMTPPESwpsMGEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLN 1264
Cdd:COG2274 452 L---DLPPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1265 ELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNL---DPfnERTDDELWDALVRGGA---IAKddLPevk 1338
Cdd:COG2274 526 EPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLhdfIEA--LP--- 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1339 lqkpdeNGthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTI 1418
Cdd:COG2274 599 ------MG---------YDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV 663
|
490 500 510
....*....|....*....|....*....|
gi 398366407 1419 LCIAHRLKTIVNYDRILVLEKGEVAEFDTP 1448
Cdd:COG2274 664 IIIAHRLSTIRLADRIIVLDKGRIVEDGTH 693
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
897-1187 |
4.86e-89 |
|
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: 291.33 E-value: 4.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 897 LPLYAILVVGTTFCSLFSSVWLSYWTEN--KFKNRPPSFYMGLYSFFVFAAFIFMN-GQFTILCAMGIMASKWLNLRAVK 973
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDwsSSPNSSSGYYLGVYAALLVLASVLLVlLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 974 RILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIFVLIADHYQ 1053
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1054 SSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFALII 1133
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1134 TLLCVTRAFPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYA 1187
Cdd:cd18580 241 ALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1207-1448 |
5.61e-89 |
|
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: 287.77 E-value: 5.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1207 WPSMGEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDL 1286
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1287 RRKLAIIPQDPVLFRGTIRKNLDPFNERTDDELWDALvrggaiakddlpevklqkpdengthgkmhkfhldqAVEEEGSN 1366
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL-----------------------------------RVSEGGLN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1367 FSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFD 1446
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
..
gi 398366407 1447 TP 1448
Cdd:cd03369 206 HP 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
899-1186 |
7.99e-71 |
|
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: 239.68 E-value: 7.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 899 LYAILVVGTTFCSLFSSVWLSYWTE--NKFKNRPPS-----FYMGLYSFFVFAAFIFMNGQFTILCAMGIMASKWLNLRA 971
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWASayETSSALPPSevsvlYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 972 VKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIFVLIADH 1051
Cdd:cd18604 83 LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1052 YQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFAL 1131
Cdd:cd18604 163 YLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1132 IITLLCVTRAfPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTY 1186
Cdd:cd18604 243 ATAALLVYGP-GIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
989-1465 |
3.38e-70 |
|
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: 246.99 E-value: 3.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 989 GRILNRFTKDTDSLDNELtesLRL---MTSQFANIVGVCVMCIVYLPWFA--IAIPFLLVIFVLIADHYQSSGREIKRLE 1063
Cdd:COG4987 112 GDLLNRLVADVDALDNLY---LRVllpLLVALLVILAAVAFLAFFSPALAlvLALGLLLAGLLLPLLAARLGRRAGRRLA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1064 AvQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAgylvvvlQR------WVGIFLDMVAIAFALIITLLC 1137
Cdd:COG4987 189 A-ARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAA-------QRrlarlsALAQALLQLAAGLAVVAVLWL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1138 VTRAF---PISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLvtyaTELpLEASYRKPEMTPPESWPSMGEII 1214
Cdd:COG4987 261 AAPLVaagALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRL----NEL-LDAPPAVTEPAEPAPAPGGPSLE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1215 FENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIP 1294
Cdd:COG4987 336 LEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVP 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1295 QDPVLFRGTIRKNL---DPfnERTDDELWDALVRggaiakddlpeVKLQKPDENGTHGkmhkfhLDQAVEEEGSNFSLGE 1371
Cdd:COG4987 416 QRPHLFDTTLRENLrlaRP--DATDEELWAALER-----------VGLGDWLAALPDG------LDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWTL 1451
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|....
gi 398366407 1452 fSQEDSIFRSMCSR 1465
Cdd:COG4987 557 -LAQNGRYRQLYQR 569
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
899-1187 |
2.84e-69 |
|
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: 235.07 E-value: 2.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 899 LYAILVVGTTFCSLFSSVWLSYWTENKFKNRPPS-----FYMGLYSFFVFAAFIFMNGQFTILCAMGIMASKWLNLRAVK 973
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDteqrdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 974 RILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIFVLIADHYQ 1053
Cdd:cd18603 83 NILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1054 SSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFALII 1133
Cdd:cd18603 163 ATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1134 TLLCVTRAFPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYA 1187
Cdd:cd18603 243 ALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1211-1454 |
7.84e-69 |
|
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: 230.96 E-value: 7.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1211 GEIIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKL 1290
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDPVLFRGTIRKNLDPFNERTDDELWDALVRggAIAKDDLPEvKLqkpdENGthgkmhkfhLDQAVEEEGSNFSLG 1370
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAK--EAGAHDFIM-KL----PNG---------YDTVLGENGGNLSQG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWT 1450
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDE 223
|
....
gi 398366407 1451 LFSQ 1454
Cdd:cd03254 224 LLAK 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1211-1462 |
2.41e-66 |
|
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: 225.17 E-value: 2.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1211 GEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKL 1290
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDPVLFRGTIRKNLDPFNERTDDELWDALvrggaiakdDLPEVKLQKPDENGThgkmhkfhLDQAVEEEGSNFSLG 1370
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEAL---------EIAQLKNMVKSLPGG--------LDAVVTEGGENFSVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWT 1450
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPEN 240
|
250
....*....|..
gi 398366407 1451 LFSQEDSIFRSM 1462
Cdd:cd03288 241 LLAQEDGVFASL 252
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1213-1441 |
3.23e-63 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 212.63 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRGTIRKNLdpfnertddelwdalvrggaiakddlpevklqkpdengthgkmhkfhldqaveeegsnFSLGER 1372
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------------------------LSGGQR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1373 QLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGE 1441
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
878-1455 |
5.45e-62 |
|
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: 222.71 E-value: 5.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 878 LKIYREYIKAAVGkWGFIAlplyAILVVGTTFC--SLFSSVWlsywtenkFKNRPPSFYMGLYSFFVF-----AAFIFMN 950
Cdd:COG4988 12 ARGARRWLALAVL-LGLLS----GLLIIAQAWLlaSLLAGLI--------IGGAPLSALLPLLGLLLAvlllrALLAWLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 951 GQFTILCAMGIMAskwlNLRA--VKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLrlmtSQFANIVGVCVM-- 1026
Cdd:COG4988 79 ERAAFRAAARVKR----RLRRrlLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYL----PQLFLAALVPLLil 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1027 -CIVYLPW-----FAIAIPFLLVIFVLIADHYQSSGReiKRLEAVQR---SFVynnlnEVLGGMDTIKAY---RSQERFL 1094
Cdd:COG4988 151 vAVFPLDWlsgliLLVTAPLIPLFMILVGKGAAKASR--RQWRALARlsgHFL-----DRLRGLTTLKLFgraKAEAERI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1095 AKS--DFLINKMNeagylvvVLQrwvgifldmvaIAFALIITLLCVTRafpISAASVGVLLtyVLQL--------PGLLN 1164
Cdd:COG4988 224 AEAseDFRKRTMK-------VLR-----------VAFLSSAVLEFFAS---LSIALVAVYI--GFRLlggsltlfAALFV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1165 TIL--------RAMTQ----TENDMNSAERLVTYAtELPLEAsyrKPEMTPPESWPSMGEIIFENVDFAYRPGLPiVLKN 1232
Cdd:COG4988 281 LLLapefflplRDLGSfyhaRANGIAAAEKIFALL-DAPEPA---APAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1233 LNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNLDPFN 1312
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1313 -ERTDDELWDALVRGGAiakDDLPEvklQKPDengthGkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILD 1391
Cdd:COG4988 436 pDASDEELEAALEAAGL---DEFVA---ALPD-----G------LDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLD 498
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1392 EATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWTLFSQE 1455
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
210-501 |
6.59e-61 |
|
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: 210.81 E-value: 6.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 210 SIVFAILANCTSGFNPMITKRLIEFVEEKaifHSMHVNKGIGYAIGACLMMFVNGLTFNHFFHTSQLTGVQAKSILTKAA 289
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSY---PDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 290 MKKMFNASNYARHCFPNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLGPIALVGIGIFFGGFFISLFA 369
Cdd:cd18579 79 YRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 370 FKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIASLV 449
Cdd:cd18579 159 AKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 398366407 450 TFLAMYKVnkGGR-QPGNIFASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRL 501
Cdd:cd18579 239 TFATYVLL--GNPlTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
981-1454 |
3.19e-57 |
|
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: 209.17 E-value: 3.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 981 SYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFA----IAIPFLLVIFVLIADHYQSSG 1056
Cdd:TIGR02204 107 SFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTslvlLAVPLVLLPILLFGRRVRKLS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1057 REIKRLEAVQRSFVynnlNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLdmVAIAFALIITLL 1136
Cdd:TIGR02204 187 RESQDRIADAGSYA----GETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIV--IVLVFGAIVGVL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1137 CV----TRAFPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVtyatELpLEAsyrKPEMTPPE-----SW 1207
Cdd:TIGR02204 261 WVgahdVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLI----EL-LQA---EPDIKAPAhpktlPV 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1208 PSMGEIIFENVDFAY--RPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD 1285
Cdd:TIGR02204 333 PLRGEIEFEQVNFAYpaRPDQP-ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 LRRKLAIIPQDPVLFRGTIRKNLDPFN-ERTDDELWDALVRGGAiakddlPEVKLQKPDENGTHgkmhkfhldqaVEEEG 1364
Cdd:TIGR02204 412 LRARMALVPQDPVLFAASVMENIRYGRpDATDEEVEAAARAAHA------HEFISALPEGYDTY-----------LGERG 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1365 SNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE 1444
Cdd:TIGR02204 475 VTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVA 554
|
490
....*....|
gi 398366407 1445 FDTPWTLFSQ 1454
Cdd:TIGR02204 555 QGTHAELIAK 564
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
899-1187 |
2.66e-56 |
|
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: 198.21 E-value: 2.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 899 LYAILVVGTTFCSLFSSVWLSYWTEN--------------KFKNRPPSFYMGLYSFFVFAAFIFMNGQFTILCAMGIMAS 964
Cdd:cd18602 3 LVLALALLKQGLRVATDFWLADWTEAnhdvasvvfnitssSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 965 KWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVI 1044
Cdd:cd18602 83 RRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1045 FVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDM 1124
Cdd:cd18602 163 YYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1125 V--AIAFALIITLLCVTRAFPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYA 1187
Cdd:cd18602 243 LgaVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1213-1465 |
4.56e-56 |
|
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: 194.76 E-value: 4.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIvLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:cd03253 1 IEFENVTFAYDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRGTIRKNLDPFNER-TDDELWDAlVRGGAIakddlpevklqkpdengtHGKMHKF--HLDQAVEEEGSNFSL 1369
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDaTDEEVIEA-AKAAQI------------------HDKIMRFpdGYDTIVGERGLKLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPW 1449
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHE 220
|
250
....*....|....*.
gi 398366407 1450 TLFsQEDSIFRSMCSR 1465
Cdd:cd03253 221 ELL-AKGGLYAEMWKA 235
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
894-1186 |
3.02e-55 |
|
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: 194.67 E-value: 3.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 894 FIALPLYAILVVGTtfcSLFSSVWLSYWTeNKFKNRPPSFYMGLYSFF--VFAAFIFMNGQFTILCAM-----GIMASKW 966
Cdd:cd18605 1 LILILLSLILMQAS---RNLIDFWLSYWV-SHSNNSFFNFINDSFNFFltVYGFLAGLNSLFTLLRAFlfaygGLRAARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 967 LNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIFV 1046
Cdd:cd18605 77 LHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1047 LIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVA 1126
Cdd:cd18605 157 RIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1127 IAFALIITLLCVTRAF---PISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTY 1186
Cdd:cd18605 237 VLIVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1213-1455 |
3.08e-55 |
|
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: 192.37 E-value: 3.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAY--RPGLPIvLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKL 1290
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDPVLFRGTIRKNL---DpfNERTDDELWDALVRGGA---IAKddLPEvklqkpdengthgkmhkfHLDQAVEEEG 1364
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygK--PDATDEEVEEAAKKANIhdfIMS--LPD------------------GYDTLVGERG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1365 SNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE 1444
Cdd:cd03249 138 SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
250
....*....|.
gi 398366407 1445 FDTPWTLFSQE 1455
Cdd:cd03249 218 QGTHDELMAQK 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
933-1456 |
3.78e-55 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 206.11 E-value: 3.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 933 FYMGLYSFFVFAAFIFMNGQFTIlcAMGIMASKwLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRL 1012
Cdd:TIGR00958 205 FFMCLLSIASSVSAGLRGGSFNY--TMARINLR-IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1013 MTSQFANIVG-VCVMC-------IVYLpwfaIAIPFLLVIFVLIADHYQSSGREIKrlEAVQRSfvyNNL-NEVLGGMDT 1083
Cdd:TIGR00958 282 LLRNLVMLLGlLGFMLwlsprltMVTL----INLPLVFLAEKVFGKRYQLLSEELQ--EAVAKA---NQVaEEALSGMRT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1084 IKAYRSQERFLAK-SDFL--INKMNEAGYLVVVLQRWVGIFLDMVAIAFALIITLLCVTRafpiSAASVGVLLTYVL--- 1157
Cdd:TIGR00958 353 VRSFAAEEGEASRfKEALeeTLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLT----GKVSSGNLVSFLLyqe 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1158 QLPGLLNTILRAMTQTENDMNSAERLVTYATelpleasyRKPEMTPPESW---PSMGEIIFENVDFAY--RPGLPiVLKN 1232
Cdd:TIGR00958 429 QLGEAVRVLSYVYSGMMQAVGASEKVFEYLD--------RKPNIPLTGTLaplNLEGLIEFQDVSFSYpnRPDVP-VLKG 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1233 LNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNLDPFN 1312
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1313 ERTDDELWDALVRgGAIAKDDLPEvklqkpDENGthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDE 1392
Cdd:TIGR00958 580 TDTPDEEIMAAAK-AANAHDFIME------FPNG---------YDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1393 ATSSVDYETDGKIQTRivEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:TIGR00958 644 ATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
893-1187 |
1.07e-54 |
|
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: 193.55 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 893 GFIALPLYAILVVGTTFCSLFSSVWLSYW------------------TENKFKNRPPSFYMGLYSffVFAAFIFMNGQFT 954
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgnttnnvdnstvdSGNISDNPDLNFYQLVYG--GSILVILLLSLIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 955 ILCAMGIM--ASKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLP 1032
Cdd:cd18599 79 GFVFVKVTlrASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1033 WFAIAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVV 1112
Cdd:cd18599 159 WFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1113 VLQRWVGIFLDMVAIAFALIITLLCVTRAFPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYA 1187
Cdd:cd18599 239 CAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1213-1455 |
1.51e-54 |
|
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: 190.13 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRGTIRKNL---DPfnERTDDELWDALVRGGA---IakDDLPEvklqkpdengthgkmhkfHLDQAVEEEGSN 1366
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRP--GATREEVEEAARAANAhefI--MELPE------------------GYDTVIGERGVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1367 FSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFD 1446
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERG 218
|
....*....
gi 398366407 1447 TPWTLFSQE 1455
Cdd:cd03251 219 THEELLAQG 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1127-1444 |
8.26e-53 |
|
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: 196.58 E-value: 8.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1127 IAFALIITLLCVTRAFPISAASVG--VLL-TYVLQL--P-GLLNTILRAMTQTENDMnsaERLVtyatELpLEasyRKPE 1200
Cdd:COG5265 273 IALGLTAMMLMAAQGVVAGTMTVGdfVLVnAYLIQLyiPlNFLGFVYREIRQALADM---ERMF----DL-LD---QPPE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1201 MT-PPESWP---SMGEIIFENVDFAYRPGLPIvLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNV 1276
Cdd:COG5265 342 VAdAPDAPPlvvGGGEVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1277 DISQLGLFDLRRKLAIIPQDPVLFRGTIRKNL---DPfnERTDDELWDAlVRGGAIakDD----LPEvklqkpdenGthg 1349
Cdd:COG5265 421 DIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAA-ARAAQI--HDfiesLPD---------G--- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1350 kmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIV 1429
Cdd:COG5265 484 ------YDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557
|
330
....*....|....*
gi 398366407 1430 NYDRILVLEKGEVAE 1444
Cdd:COG5265 558 DADEILVLEAGRIVE 572
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1211-1442 |
3.01e-52 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 183.17 E-value: 3.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1211 GEIIFENVDFAYrPGLPI-VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRK 1289
Cdd:cd03245 1 GRIEFRNVSFSY-PNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVLFRGTIRKNLDPFN-ERTDDELWDALVRGGAiakDDLpeVKLQKpdengtHGkmhkfhLDQAVEEEGSNFS 1368
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGApLADDERILRAAELAGV---TDF--VNKHP------NG------LDLQIGERGRGLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1369 LGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEV 1442
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
976-1455 |
7.23e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 193.78 E-value: 7.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 976 LHTPMSYIDTTPLGRILNRFTKDTdsldnELTESLRLMTS----QFANIVGVCVMCIVYLPW----FAIAI-PFLLVIFV 1046
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDT-----EVIRDLYVTVVatvlRSAALIGAMLVAMFSLDWrmalVAIMIfPAVLVVMV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1047 LiadhYQSSGREIKRLeavQRSF---VYNNLNEVLGGMDTIKAYRSQERFLAKsdflINKMNEAGYLVVvLQ--RWVGIF 1121
Cdd:PRK10790 184 I----YQRYSTPIVRR---VRAYladINDGFNEVINGMSVIQQFRQQARFGER----MGEASRSHYMAR-MQtlRLDGFL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1122 L-DMVAIAFALIITLLCVTRAF-PISAASVGVLLTYVLQLpGLLNTILRAMTQTENDMNSAerlvTYATELPLEASYRKP 1199
Cdd:PRK10790 252 LrPLLSLFSALILCGLLMLFGFsASGTIEVGVLYAFISYL-GRLNEPLIELTTQQSMLQQA----VVAGERVFELMDGPR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1200 EMTPPESWP-SMGEIIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDI 1278
Cdd:PRK10790 327 QQYGNDDRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1279 SQLGLFDLRRKLAIIPQDPVLFRGTIRKNLDPFNERTDDELWDAL--VRGGAIAKdDLPEvklqkpdenGTHGKMHkfhl 1356
Cdd:PRK10790 406 SSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALetVQLAELAR-SLPD---------GLYTPLG---- 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1357 dqaveEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT--RIVEEfgDCTILCIAHRLKTIVNYDRI 1434
Cdd:PRK10790 472 -----EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQalAAVRE--HTTLVVIAHRLSTIVEADTI 544
|
490 500
....*....|....*....|.
gi 398366407 1435 LVLEKGEVAEFDTPWTLFSQE 1455
Cdd:PRK10790 545 LVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
893-1187 |
1.89e-51 |
|
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: 184.45 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 893 GFIALPLYAILVVGTTFCSLFSSVWLSYW---------------TENKFKNRPP----SFYMGLYSFFVFAAFIFMNGQF 953
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanleeklndttdrvqGENSTNVDIEdldrDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 954 TILCAMGIMASKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPW 1033
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1034 FAIAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVV 1113
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1114 LQRWVGIFLDMVAIAFALIITLLCVTRAFPISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYA 1187
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1213-1455 |
1.94e-49 |
|
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: 175.75 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRGTIRKNLdpfnertddelwdALVRGGAIAKDDLPEVKLQkpdenGTHGKMHKFHL--DQAVEEEGSNFSLG 1370
Cdd:cd03252 81 VLQENVLFNRSIRDNI-------------ALADPGMSMERVIEAAKLA-----GAHDFISELPEgyDTIVGEQGAGLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWT 1450
Cdd:cd03252 143 QRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDE 222
|
....*
gi 398366407 1451 LFSQE 1455
Cdd:cd03252 223 LLAEN 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
897-1166 |
6.48e-49 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 175.52 E-value: 6.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 897 LPLYAILVVGTTFCSLFSSVWLSYWTENKFKNRPPS-----FYMGLYSFFVFAAFIFMNGQFTILCAMGIMASKWLNLRA 971
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqalnVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 972 VKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIFVLIADH 1051
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1052 YQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFAL 1131
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 398366407 1132 IITLLCVTRAFPiSAASVGVLLTYVLQLPGLLNTI 1166
Cdd:pfam00664 241 LALWFGAYLVIS-GELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
606-785 |
4.16e-47 |
|
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: 168.28 E-value: 4.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGY------------------PWIQNASVRDN 667
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfeatrsrnrysvayaaqkPWLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGSPFNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKH 747
Cdd:cd03290 99 ITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398366407 748 IMDECLTGMLAN--KTRILATHQLSLIERASRVIVLgTDG 785
Cdd:cd03290 179 LMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAM-KDG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
970-1444 |
2.28e-46 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 177.13 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 970 RAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMcIVYLPWFAIAIPFLLVIFVLIA 1049
Cdd:PRK11176 103 RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIM-MFYYSWQLSLILIVIAPIVSIA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1050 DHYQSsgreiKRLEAVQRSfVYNNLNEV-------LGGMDTIKAYRSQ----ERFlaksDFLINKMNEAGYLVVVLQRWV 1118
Cdd:PRK11176 182 IRVVS-----KRFRNISKN-MQNTMGQVttsaeqmLKGHKEVLIFGGQevetKRF----DKVSNRMRQQGMKMVSASSIS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1119 GIFLDMVAiAFALIITLLCVTraFP-----ISAASVGVLLTYVLQLPGLLNTILRAMTQTENDMNSAERLVTYaTELPLE 1193
Cdd:PRK11176 252 DPIIQLIA-SLALAFVLYAAS--FPsvmdtLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAI-LDLEQE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1194 ASYRKPEMTPPEswpsmGEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILI 1273
Cdd:PRK11176 328 KDEGKRVIERAK-----GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1274 DNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNLdpfnertddelwdALVRGGAIAKDDLPEV-----------KLqkp 1342
Cdd:PRK11176 403 DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNI-------------AYARTEQYSREQIEEAarmayamdfinKM--- 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1343 dENGthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIA 1422
Cdd:PRK11176 467 -DNG---------LDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA 536
|
490 500
....*....|....*....|..
gi 398366407 1423 HRLKTIVNYDRILVLEKGEVAE 1444
Cdd:PRK11176 537 HRLSTIEKADEILVVEDGEIVE 558
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
941-1446 |
2.38e-46 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 177.08 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 941 FVFAAFifmnGQFTILCA---------------MGIMASkwlnlrAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLdne 1005
Cdd:PRK13657 60 AAWAGF----GLFNIIAGvlvarhadrlahrrrLAVLTE------YFERIIQLPLAWHSQRGSGRALHTLLRGTDAL--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1006 LTESLRLMTSQFANIVGVCVMCIV--YLPW-FAIAIPFLLVIFVLIADHYqssgreIKRLEAVQRSF--VYNNLNE---- 1076
Cdd:PRK13657 127 FGLWLEFMREHLATLVALVVLLPLalFMNWrLSLVLVVLGIVYTLITTLV------MRKTKDGQAAVeeHYHDLFAhvsd 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1077 VLGGMDTIKAY-RSQERFLAKSDFlINKMNEAGY-------LVVVLQRWVGIfLDMVAIafaLIITLLCVTRAfpisAAS 1148
Cdd:PRK13657 201 AIGNVSVVQSYnRIEAETQALRDI-ADNLLAAQMpvlswwaLASVLNRAAST-ITMLAI---LVLGAALVQKG----QLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1149 VGVLLTYVlqlpGLLNTILRAMTQTENDMN----SAERLVTYATELPLEASYRKPEMTPPESWPSmGEIIFENVDFAYrP 1224
Cdd:PRK13657 272 VGEVVAFV----GFATLLIGRLDQVVAFINqvfmAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVK-GAVEFDDVSFSY-D 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1225 GLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTI 1304
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSI 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1305 RKNLDPFNE-RTDDELWDALVRGGAIakdDLPEVKLQKpdengthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVR 1383
Cdd:PRK13657 426 EDNIRVGRPdATDEEMRAAAERAQAH---DFIERKPDG--------------YDTVVGERGRQLSGGERQRLAIARALLK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1384 QSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE---FD 1446
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFD 554
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
196-799 |
1.33e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 174.58 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 196 LRALLFTFKKQYFMSIVFAILANCTSGFNPMITKRLIEfveekAIFHSMHVNKGIGYAIGACLMMFVNGLTfnHFFHTSQ 275
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIID-----ALLAGGDLSALLLLLLLLLGLALLRALL--SYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 276 LTGVQAKSI--LTKAAMKKM--FNASNYARHcfPNGKVTSFVTTDLARIEFALSFQP--FLAGFPAILAICIVLLIVN-- 347
Cdd:COG1132 85 LARLAQRVVadLRRDLFEHLlrLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLpqLVRSVVTLIGALVVLFVIDwr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 348 LGPIALVGIGiffggffisLFAFKLILGFRIAANIFTDAR------VTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKE 421
Cdd:COG1132 163 LALIVLLVLP---------LLLLVLRLFGRRLRKLFRRVQealaelNGRLQESLSGIRVVKAFGREERELERFREANEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 422 ISKVRKMQLSRNFLIAMAMSLPSIAS-LVTFLAMYKVNKGGRQPGNIFASLSLfqvlsLQMFFLPI-AIGTGIDMI---- 495
Cdd:COG1132 234 RRANLRAARLSALFFPLMELLGNLGLaLVLLVGGLLVLSGSLTVGDLVAFILY-----LLRLFGPLrQLANVLNQLqral 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 496 IGLGRLQSLLEAPED--DPNQMIEMKPSPGfdpklALKMTHCSFEWEDyelndaieeakgeakdegkknkkkrkdtwGKP 573
Cdd:COG1132 309 ASAERIFELLDEPPEipDPPGAVPLPPVRG-----EIEFENVSFSYPG-----------------------------DRP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 574 sastnkakrldnmlkdrdgpedlektsfrGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG---- 649
Cdd:COG1132 355 -----------------------------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdir 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 650 -----DLL-MCGY----PWIQNASVRDNIIFGSP-FNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARI 718
Cdd:COG1132 406 dltleSLRrQIGVvpqdTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 719 NLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDEcLTGMLANKTRILATHQLSLIERASRVIVLgTDGQ-VDIGTVDELKA 797
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVL-DDGRiVEQGTHEELLA 563
|
..
gi 398366407 798 RN 799
Cdd:COG1132 564 RG 565
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
605-796 |
1.94e-45 |
|
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: 165.80 E-value: 1.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCG-YPWIQNASVRDNIIFGSPFNKEKYDEVV 683
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSqFSWIMPGTIKENIIFGVSYDEYRYKSVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 684 RVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTGMLANKTRI 763
Cdd:cd03291 134 KACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRI 213
|
170 180 190
....*....|....*....|....*....|...
gi 398366407 764 LATHQLSLIERASRVIVLGTDGQVDIGTVDELK 796
Cdd:cd03291 214 LVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
196-807 |
1.60e-44 |
|
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: 173.87 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 196 LRALLFTFKKQYFMSIVFAILANCTSGFNPMITKRLIEFVEEKAIFHSMHVnkgigYAIGACLMMFVNGLtfnhffhtsq 275
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWV-----LAIGLLLALLFEGL---------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 276 LTGVQAKsILTKAAmKKMFN--ASNYARH-------CFPNGKVTSFVT--TDLARIEFALS--FQPFLAGFPAILAICIV 342
Cdd:COG2274 212 LRLLRSY-LLLRLG-QRIDLrlSSRFFRHllrlplsFFESRSVGDLASrfRDVESIREFLTgsLLTALLDLLFVLIFLIV 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 343 LLIVNlGPIALVGIGIFFGGFFISLFAFKLILgfRIAANIFTDA--RVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTK 420
Cdd:COG2274 290 LFFYS-PPLALVVLLLIPLYVLLGLLFQPRLR--RLSREESEASakRQSLLVETLRGIETIKALGAESRFRRRWENLLAK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 421 EISKVRKMQLSRNFLIAMAMSLPSIAS-LVTFLAMYKVNKGGRQPGNIFAslslFQVLSLQmFFLPIA--IGTGI---DM 494
Cdd:COG2274 367 YLNARFKLRRLSNLLSTLSGLLQQLATvALLWLGAYLVIDGQLTLGQLIA----FNILSGR-FLAPVAqlIGLLQrfqDA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 495 IIGLGRLQSLLEAPEDDPNQmIEMKPSPGFDPKLALKmtHCSFeweDYelndaieeakgeakdegkknkkkrkdtwgkps 574
Cdd:COG2274 442 KIALERLDDILDLPPEREEG-RSKLSLPRLKGDIELE--NVSF---RY-------------------------------- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 575 astnkakrldnmlkDRDGPEDLektsfrgfKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLL- 652
Cdd:COG2274 484 --------------PGDSPPVL--------DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGiDLRq 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 653 --------MCGY----PWIQNASVRDNIIFGSP-FNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARIN 719
Cdd:COG2274 542 idpaslrrQIGVvlqdVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 720 LARSVYKKKDIYLFDDVLSAVDSRVGKHIMdECLTGMLANKTRILATHQLSLIERASRVIVLgTDGQ-VDIGTVDELKAR 798
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIIL-ENLRRLLKGRTVIIIAHRLSTIRLADRIIVL-DKGRiVEDGTHEELLAR 699
|
....*....
gi 398366407 799 NQTLINLLQ 807
Cdd:COG2274 700 KGLYAELVQ 708
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1211-1442 |
8.83e-41 |
|
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: 150.31 E-value: 8.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1211 GEIIFENVDFAY--RPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRR 1288
Cdd:cd03248 10 GIVKFQNVTFAYptRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1289 KLAIIPQDPVLFRGTIRKNLD-PFNERTDDELWDALVrgGAIAKDDLPEVKlqkpdengtHGkmhkfhLDQAVEEEGSNF 1367
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQ--KAHAHSFISELA---------SG------YDTEVGEKGSQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1368 SLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEV 1442
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1177-1437 |
3.14e-40 |
|
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: 157.45 E-value: 3.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1177 MNSAERLVTYATELPLEASYRKPEMTPPESwpsmgEIIFENVDFAYrPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTI 1256
Cdd:TIGR02857 291 VAAAEALFAVLDAAPRPLAGKAPVTAAPAS-----SLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1257 MSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNL---DPfnERTDDELWDALVRGGAI-AKD 1332
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP--DASDAEIREALERAGLDeFVA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1333 DLPEvklqkpdengthgkmhkfHLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEE 1412
Cdd:TIGR02857 443 ALPQ------------------GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL 504
|
250 260
....*....|....*....|....*
gi 398366407 1413 FGDCTILCIAHRLKTIVNYDRILVL 1437
Cdd:TIGR02857 505 AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1211-1466 |
6.15e-40 |
|
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: 149.62 E-value: 6.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1211 GEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNElTAGKILIDNVDISQLGLFDLRRKL 1290
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDPVLFRGTIRKNLDPFNERTDDELWDALVRGGaiakddLPEVKLQKPDEngthgkmhkfhLDQAVEEEGSNFSLG 1370
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVG------LKSVIEQFPGQ-----------LDFVLVDGGCVLSHG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPWT 1450
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQK 222
|
250
....*....|....*.
gi 398366407 1451 LFSqEDSIFRSMCSRS 1466
Cdd:cd03289 223 LLN-EKSHFKQAISPS 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
989-1425 |
1.63e-39 |
|
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: 155.60 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 989 GRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFA-IAIPFLLVIFVLIADHYQSSGREIKRLEAVQR 1067
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAAlILAAGLLLAGFVAPLVSLRAARAAEQALARLR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1068 SFVYNNLNEVLGGMDTIKAYRSQERFLAKSDF-------LINKMNE-----------AGYLVVVLQRWVGIF------LD 1123
Cdd:TIGR02868 190 GELAAQLTDALDGAAELVASGALPAALAQVEEadreltrAERRAAAatalgaaltllAAGLAVLGALWAGGPavadgrLA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1124 MVAIAfALIITLLCVTRAF-PISAASVgvlltyvlQLPgllntilRAMTqtendmnSAERLVtyatELpLEASYRKPEMT 1202
Cdd:TIGR02868 270 PVTLA-VLVLLPLAAFEAFaALPAAAQ--------QLT-------RVRA-------AAERIV----EV-LDAAGPVAEGS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1203 PPESWPSMGE---IIFENVDFAYrPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDIS 1279
Cdd:TIGR02868 322 APAAGAVGLGkptLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1280 QLGLFDLRRKLAIIPQDPVLFRGTIRKNL---DPfnERTDDELWDALVRGG-AIAKDDLPEvklqkpdenGTHGKMHkfh 1355
Cdd:TIGR02868 401 SLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGlADWLRALPD---------GLDTVLG--- 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1356 ldqaveEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRL 1425
Cdd:TIGR02868 467 ------EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1012-1444 |
1.33e-38 |
|
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: 155.11 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1012 LMTSQFA--NIVgvcVMCIVYLPWFAIAIPFLLVIFVLIA------DHYQssgREIKRLEAVQRSFVYnnlnEVLGGMDT 1083
Cdd:TIGR03797 257 LLSGIFAllNLG---LMFYYSWKLALVAVALALVAIAVTLvlgllqVRKE---RRLLELSGKISGLTV----QLINGISK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1084 IKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFALIITLLCVtraFPISAA--SVGVLLTYVlqlpG 1161
Cdd:TIGR03797 327 LRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAI---SLLGGAglSLGSFLAFN----T 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1162 LLNTILRAMTQTENDMNSAERLV-TYATELP-LEAsyrKPEMTPPESWPS--MGEIIFENVDFAYRPGLPIVLKNLNLNI 1237
Cdd:TIGR03797 400 AFGSFSGAVTQLSNTLISILAVIpLWERAKPiLEA---LPEVDEAKTDPGklSGAIEVDRVTFRYRPDGPLILDDVSLQI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1238 KSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNLDPFNERTDD 1317
Cdd:TIGR03797 477 EPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1318 ELWDALVRGGaIAKD--DLPEvklqkpdengthgKMHKFhldqaVEEEGSNFSLGERQLLALTRALVRQSKILILDEATS 1395
Cdd:TIGR03797 557 EAWEAARMAG-LAEDirAMPM-------------GMHTV-----ISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATS 617
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 1396 SVDYETD-------GKIQ-TRIVeefgdctilcIAHRLKTIVNYDRILVLEKGEVAE 1444
Cdd:TIGR03797 618 ALDNRTQaivseslERLKvTRIV----------IAHRLSTIRNADRIYVLDAGRVVQ 664
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
210-501 |
3.16e-38 |
|
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: 145.31 E-value: 3.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 210 SIVFAILANCTSGFNPMITKRLIEFVEEKAIFHSmhvnKGIGYAIGACLMMFVNGLTFNHFFHTSQLTGVQAKSILTKAA 289
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLW----KGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 290 MKKMFNASNYARHCFPNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLGPIALVGIGIFFGGFFISLFA 369
Cdd:cd18595 78 YRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 370 FKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIASLV 449
Cdd:cd18595 158 ARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 450 TFLAMYKVNkggrqPGNI------FASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRL 501
Cdd:cd18595 238 TFATYVLSD-----PDNVldaekaFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1179-1444 |
1.32e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 150.36 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1179 SAERLvtyaTELpLEAsyrKPEMTPPES---WPSMGEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKST 1255
Cdd:PRK11160 310 SARRI----NEI-TEQ---KPEVTFPTTstaAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKST 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1256 IMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNL---DPfnERTDDELWDALVRggaiakd 1332
Cdd:PRK11160 382 LLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQ------- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1333 dlpeVKLQK--PDENGthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIV 1410
Cdd:PRK11160 453 ----VGLEKllEDDKG---------LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA 519
|
250 260 270
....*....|....*....|....*....|....
gi 398366407 1411 EEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE 1444
Cdd:PRK11160 520 EHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
209-501 |
2.23e-37 |
|
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: 142.70 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 209 MSIVFAILANCTSGFNP-MITKRLIEFVEEKaifhSMHVNKGIGYAIGACLMMFVNGLTFNHFFHTSQLTGVQAKSILTK 287
Cdd:cd18592 1 FSILLLLISLIFGFIGPtILIRKLLEYLEDS----DSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 288 AAMKKMFNASNYARHCfpNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLGPIALVGIGIFFGGFFISL 367
Cdd:cd18592 77 LLYKKILRLRSLGDKS--VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 368 FAFKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIAS 447
Cdd:cd18592 155 FIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIAS 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 448 LVTFLAMykVNKGGR-QPGNIFASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRL 501
Cdd:cd18592 235 VVTFLAH--VALGNDlTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
605-799 |
3.05e-37 |
|
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: 149.14 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL----------MCGY----PWIQNASVRDNIIF 670
Cdd:COG4988 354 DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsdldpaswrrQIAWvpqnPYLFAGTIRENLRL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSP-FNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:COG4988 434 GRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEIL 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 398366407 750 DEcLTGMLANKTRILATHQLSLIERASRVIVLGtDGQ-VDIGTVDELKARN 799
Cdd:COG4988 514 QA-LRRLAKGRTVILITHRLALLAQADRILVLD-DGRiVEQGTHEELLAKN 562
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
924-1444 |
5.70e-37 |
|
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: 150.28 E-value: 5.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 924 NKFKNRPPSFYMGLYSFFVFAAfIFMNGQFTILCAMGIMASKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLD 1003
Cdd:TIGR01193 189 HKMMGTLGIISIGLIIAYIIQQ-ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIID 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1004 NE--------LTESLRLMTSQFANIVGVCVMCIVYLpwfaiAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLN 1075
Cdd:TIGR01193 268 ALastilslfLDMWILVIVGLFLVRQNMLLFLLSLL-----SIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLN 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1076 evlgGMDTIKAYRS-QERFLAKSDFLINKMNEAgyLVVVLQRWVGIFLDmVAIAFALIITLLCVTRAFPISAA-SVGVLL 1153
Cdd:TIGR01193 343 ----GIETIKSLTSeAERYSKIDSEFGDYLNKS--FKYQKADQGQQAIK-AVTKLILNVVILWTGAYLVMRGKlTLGQLI 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1154 TYVLQLPGLLNTI-----LRAMTQTENDMNsaERLvtyaTELPLEASYRKPEMTPPESWPSMGEIIFENVDFAYRPGLPI 1228
Cdd:TIGR01193 416 TFNALLSYFLTPLeniinLQPKLQAARVAN--NRL----NEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNI 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 vLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNL 1308
Cdd:TIGR01193 490 -LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 DPFNER--TDDELWDALvrggaiakdDLPEVKlqKPDENGTHGkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSK 1386
Cdd:TIGR01193 569 LLGAKEnvSQDEIWAAC---------EIAEIK--DDIENMPLG------YQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1387 ILILDEATSSVDYETDGKIQTRIVeEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE 1444
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1219-1442 |
1.43e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.64 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1219 DFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPV 1298
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1299 LFRGTIRKNLD-PFNERTDDELWDAlvrggaiAKDDLPEVKLqkPDENgthgkmhkfhLDQAVEEegsnFSLGERQLLAL 1377
Cdd:COG4619 85 LWGGTVRDNLPfPFQLRERKFDRER-------ALELLERLGL--PPDI----------LDKPVER----LSGGERQRLAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1378 TRALVRQSKILILDEATSSVDYETdgkiqTRIVEEF-------GDCTILCIAH------RLKtivnyDRILVLEKGEV 1442
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPEN-----TRRVEELlreylaeEGRAVLWVSHdpeqieRVA-----DRVLTLEAGRL 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1213-1456 |
2.46e-36 |
|
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: 137.85 E-value: 2.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPV--LFRGTIRKNLD--PFNERTDDELWDALVRgGAIAKDDLPEVKLQKPdengthgkmhkFHLdqaveeegsnfS 1368
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAfgPENLGLPREEIRERVE-EALELVGLEHLADRPP-----------HEL-----------S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1369 LGERQLLALTRALVRQSKILILDEATSSVDYETdgkiQTRIVEEFGD-----CTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRG----RRELLELLKRlnkegKTVIIVTHDLDLVAELaDRVIVLDDGRI 212
|
250
....*....|....
gi 398366407 1443 AEFDTPWTLFSQED 1456
Cdd:COG1122 213 VADGTPREVFSDYE 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1216-1442 |
2.86e-36 |
|
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: 135.42 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQ 1295
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1296 DPVLFRGTIRKNLdpfnertddelwdalvrggaiakddlpevklqkpdengthgkmhkfhldqaveeegsnFSLGERQLL 1375
Cdd:cd03246 84 DDELFSGSIAENI----------------------------------------------------------LSGGQRQRL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1376 ALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE-EFGDCTILCIAHRLKTIVNYDRILVLEKGEV 1442
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
695-1460 |
3.09e-36 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 150.56 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 695 LPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvGKHIMDECLTGMLANKTRI--LATHQLSLI 772
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKGNENRItiIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 773 ERASRVIVL-----GTDGQVDI------------------------------------------GTVDEL-KARN---QT 801
Cdd:PTZ00265 644 RYANTIFVLsnrerGSTVDVDIigedptkdnkennnknnkddnnnnnnnnnnkinnagsyiieqGTHDALmKNKNgiyYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 802 LINLLQFSSQNSEKEDEEQEAVVAGEL---GQLKYESEvkELTELKKKATEmSQTANSGKIVADGHTSSKEE-------- 870
Cdd:PTZ00265 724 MINNQKVSSKKSSNNDNDKDSDMKSSAykdSERGYDPD--EMNGNSKHENE-SASNKKSCKMSDENASENNAggklpflr 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 871 -------RAVNSISLkIYRE---YIKAAVgkwgFIAL---------PLYAILV---VGTtfcsLFSSVWLSYwTENKFkn 928
Cdd:PTZ00265 801 nlfkrkpKAPNNLRI-VYREifsYKKDVT----IIALsilvagglyPVFALLYakyVST----LFDFANLEA-NSNKY-- 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 929 rppSFYMGLYSFFVFAAFIFMNGQFTILcamGIMASKWLNLRAVKRILHTPMSYIDT---TPlGRILNRFTKDTDSLDNE 1005
Cdd:PTZ00265 869 ---SLYILVIAIAMFISETLKNYYNNVI---GEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTG 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1006 LTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIF--VLIADHYQSSGREIKRLEAVQRS--FVYNN-------- 1073
Cdd:PTZ00265 942 LVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFmrVFAIRARLTANKDVEKKEINQPGtvFAYNSddeifkdp 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1074 ---LNEVLGGMDTIKAYRSQERFLA-------------KSDFLINKM-----NEAGYLVVVLQRWVGIFLdmVAIAFALI 1132
Cdd:PTZ00265 1022 sflIQEAFYNMNTVIIYGLEDYFCNliekaidysnkgqKRKTLVNSMlwgfsQSAQLFINSFAYWFGSFL--IRRGTILV 1099
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1133 ITLLCVTRAFPISAASVGVLLTyvlqLPGllntilramtQTENDMNSAERLVTYATELPLEASYRKPEMTPPESWPSMGE 1212
Cdd:PTZ00265 1100 DDFMKSLFTFLFTGSYAGKLMS----LKG----------DSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGK 1165
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAY--RPGLPIvLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNEL------------------------ 1266
Cdd:PTZ00265 1166 IEIMDVNFRYisRPNVPI-YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqg 1244
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1267 ------------------------------TAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNLDPFNERTD 1316
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1317 DELWDALVRGGAIakDDLPEVKLQKPDEN-GTHGKmhkfhldqaveeegsNFSLGERQLLALTRALVRQSKILILDEATS 1395
Cdd:PTZ00265 1325 REDVKRACKFAAI--DEFIESLPNKYDTNvGPYGK---------------SLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1396 SVDYETDGKIQTRIVE--EFGDCTILCIAHRLKTIVNYDRILVLEKGE-----VAEFDTPWTLFSQEDSIFR 1460
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVDikDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYK 1459
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
208-478 |
1.13e-35 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 137.39 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 208 FMSIVFAILANCTSGFNPMITKRLIEFVEEKAIFHSMHVNKGIGYAIGACLMMFVNGLTFNHFFHtsqLTGVQAKSILTK 287
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLN---HTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 288 AAMKKMFNA--SNYARHcfPNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLGP-IALVGIGIFFGGFF 364
Cdd:pfam00664 79 KLFKKILRQpmSFFDTN--SVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWkLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 365 ISLFAFKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPS 444
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*
gi 398366407 445 IA-SLVTFLAMYKVNKGGRQPGNIFASLSLFQVLS 478
Cdd:pfam00664 237 LSyALALWFGAYLVISGELSVGDLVAFLSLFAQLF 271
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1213-1444 |
2.76e-34 |
|
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: 130.13 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfDLRRKLAI 1292
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRGTIRKNLdpfnertddelwdalvrggaiakddlpevklqkpdengthgkmhkfhldqaveeeGSNFSLGER 1372
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------------------------GRRFSGGER 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1373 QLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE 1444
Cdd:cd03247 105 QRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1215-1441 |
1.99e-33 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 128.74 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1215 FENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIP 1294
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1295 QDPvlfRGTIrknldpFNERTDDELWDALVRGGaIAKDDLPEVKLQKPDENGTHGKMHK--FHLdqaveeegsnfSLGER 1372
Cdd:cd03225 82 QNP---DDQF------FGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRspFTL-----------SGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1373 QLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFGDC--TILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRREL-LELLKKLKAEgkTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
206-501 |
2.08e-33 |
|
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: 131.85 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 206 QYFMSIVFAILanctsGF-NPMITKRLIEFVEEKAifhSMHVNKGIGYAIGACLMMFVNGLTFNHFFHTSQLTGVQAKSI 284
Cdd:cd18596 2 QALLAVLSSVL-----SFaPPFFLNRLLRYLEDPG---EDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 285 LTKA----AMKKMFNASNYARHCFPN---------------GKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLI 345
Cdd:cd18596 74 LTQLifekALRRRDKSGSSKSSESKKkdkeededekssasvGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 346 VNLGPIALVGIGIFFGGFFISLFAFKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKV 425
Cdd:cd18596 154 RLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWL 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 426 RKMQLSRNFLIAMAMSLPSIASLVTFLAMYKVNKGGRQPGNIFASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRL 501
Cdd:cd18596 234 RKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1228-1465 |
1.58e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 135.36 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1228 IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSAL-----YRlneltaGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRG 1302
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpYQ------GSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1303 TIRKNLDPFNER-TDDELWDALVRggAIAKDDLPEVklqkpdengTHGkmhkfhLDQAVEEEGSNFSLGERQLLALTRAL 1381
Cdd:PRK11174 438 TLRDNVLLGNPDaSDEQLQQALEN--AWVSEFLPLL---------PQG------LDTPIGDQAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1382 VRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE---FDTpwtlFSQEDSI 1458
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGL 576
|
....*..
gi 398366407 1459 FRSMCSR 1465
Cdd:PRK11174 577 FATLLAH 583
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1230-1395 |
2.88e-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: 123.14 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRG-TIRKNL 1308
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 DpfnERTDDELWDALVRgGAIAKDDLPEVKLqkpdengthgkmhKFHLDQAVEEEGSNFSLGERQLLALTRALVRQSKIL 1388
Cdd:pfam00005 81 R---LGLLLKGLSKREK-DARAEEALEKLGL-------------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 398366407 1389 ILDEATS 1395
Cdd:pfam00005 144 LLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1215-1441 |
3.18e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 123.51 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1215 FENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIP 1294
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1295 QdpvlfrgtirknldpfnertddelwdalvrggaiakddlpevklqkpdengthgkmhkfhldqaveeegsnFSLGERQL 1374
Cdd:cd00267 80 Q-----------------------------------------------------------------------LSGGQRQR 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1375 LALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEF-GDCTILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:cd00267 89 VALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
212-502 |
6.60e-32 |
|
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: 126.98 E-value: 6.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 212 VFAILANCTSGFNPMITKRLIEFVEEKAifhSMHVNKGIGYAIGACLMMFVNGLTFNHFFHTSQLTGVQAKSILTKAAMK 291
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVAYFVPDS---TVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 292 KMFNASNYARHCFPNGKVTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLGPIALVGIGIFFGGFFISLFAFK 371
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 372 LILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIASLVTF 451
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 398366407 452 LaMYKVNKGGRQPGNIFASLSLFQVLSLQM-FFLPIAIGTGIDMIIGLGRLQ 502
Cdd:cd18594 241 V-PYVLTGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRIQ 291
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1215-1454 |
7.40e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 131.95 E-value: 7.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1215 FENVDFAY---RPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---LFDLRR 1288
Cdd:COG1123 263 VRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1289 KLAIIPQDPV--LF-RGTIRknldpfnertdDELWDALVRGGAIAKDDLPE--VKLqkpdengthgkMHKFHLDQAVEE- 1362
Cdd:COG1123 343 RVQMVFQDPYssLNpRMTVG-----------DIIAEPLRLHGLLSRAERRErvAEL-----------LERVGLPPDLADr 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1363 ---EgsnFSLGERQLLALTRALVRQSKILILDEATSSVDYetdgKIQTRIV-------EEFGdCTILCIAHRLkTIVNY- 1431
Cdd:COG1123 401 yphE---LSGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILnllrdlqRELG-LTYLFISHDL-AVVRYi 471
|
250 260
....*....|....*....|....
gi 398366407 1432 -DRILVLEKGEVAEFDTPWTLFSQ 1454
Cdd:COG1123 472 aDRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
326-807 |
1.23e-31 |
|
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: 132.20 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 326 FQPFLAGFPAILAICIVLLIVNLgPIALVgigiffggffisLFAFKLILGF----------RIAANIFTDARVTMMREVL 395
Cdd:COG4987 133 LLPLLVALLVILAAVAFLAFFSP-ALALV------------LALGLLLAGLllpllaarlgRRAGRRLAAARAALRARLT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 396 NNI---KMIKYYTWEDAYEKNIQDIrTKEISKVRKMQLS----RNFLIAMAMSLPSIASLVtfLAMYKVNkGGRQPGN-- 466
Cdd:COG4987 200 DLLqgaAELAAYGALDRALARLDAA-EARLAAAQRRLARlsalAQALLQLAAGLAVVAVLW--LAAPLVA-AGALSGPll 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 467 ---IFASLSLFQVLSLqmffLPIAIGTGIDMIIGLGRLQSLLEAPEDDPNQMIEMKPSPGFDpklaLKMTHCSFEWEDye 543
Cdd:COG4987 276 allVLAALALFEALAP----LPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPS----LELEDVSFRYPG-- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 544 lndaieeakgeakdegkknkkkrkdtwgkpsastnkakrldnmlkdrdGPEDLektsfrgFKDLNFDIKKGEFIMITGPI 623
Cdd:COG4987 346 ------------------------------------------------AGRPV-------LDGLSLTLPPGERVAIVGPS 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 624 GTGKSSLLNAMAGSMRKTDGKVEVNG-DLL---------MCGY----PWIQNASVRDNIIFGSPFNKEkyDEVVRVCS-- 687
Cdd:COG4987 371 GSGKSTLLALLLRFLDPQSGSITLGGvDLRdldeddlrrRIAVvpqrPHLFDTTLRENLRLARPDATD--EELWAALErv 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 688 -LKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTgMLANKTRILAT 766
Cdd:COG4987 449 gLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLIT 527
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 398366407 767 HQLSLIERASRVIVLGTDGQVDIGTVDELKARNQTLINLLQ 807
Cdd:COG4987 528 HRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
604-781 |
6.37e-31 |
|
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: 120.18 E-value: 6.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL----------MCGY----PWIQNASVRDNIi 669
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrdldleslrkNIAYvpqdPFLFSGTIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 670 fgspfnkekydevvrvcslkadldilpagdmteigergitLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:cd03228 97 ----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|..
gi 398366407 750 dECLTGMLANKTRILATHQLSLIERASRVIVL 781
Cdd:cd03228 137 -EALRALAKGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1217-1445 |
7.41e-30 |
|
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: 119.15 E-value: 7.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1217 NVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---LFDLRRKLAII 1293
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1294 PQDPvlfrgtiRKNLDPfNERTDDELWDAL-VRGGAIAKDDLPEVKLQKpdengthgkMHKFHLDQAVEEEGSN-FSLGE 1371
Cdd:cd03257 88 FQDP-------MSSLNP-RMTIGEQIAEPLrIHGKLSKKEARKEAVLLL---------LVGVGLPEEVLNRYPHeLSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAHRLKtIVNY--DRILVLEKGEVAEF 1445
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDllkKLQEELG-LTLLFITHDLG-VVAKiaDRVAVMYAGKIVEE 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
605-799 |
8.36e-30 |
|
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: 119.26 E-value: 8.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DL-------------LMCGYPWIQNASVRDNIIF 670
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhDVrdytlaslrrqigLVSQDVFLFNDTVAENIAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSPfnKEKYDEVVRVCSLKADLDI---LPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvGKH 747
Cdd:cd03251 99 GRP--GATREEVEEAARAANAHEFimeLPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE-SER 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398366407 748 IMDECLTGMLANKTRILATHQLSLIERASRVIVLgTDGQ-VDIGTVDELKARN 799
Cdd:cd03251 176 LVQAALERLMKNRTTFVIAHRLSTIENADRIVVL-EDGKiVERGTHEELLAQG 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
591-807 |
1.51e-29 |
|
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: 118.36 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 591 DGPEDLEktsfrgfkDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGYPWIQ--------- 660
Cdd:cd03252 13 DGPVILD--------NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhDLALADPAWLRrqvgvvlqe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 661 ----NASVRDNIIFGSP-FNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDD 735
Cdd:cd03252 85 nvlfNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 736 VLSAVDSRvGKHIMDECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKARNQTLINLLQ 807
Cdd:cd03252 165 ATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1215-1451 |
4.46e-29 |
|
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: 116.90 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1215 FENVDFAYRPGlpIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNEL-----TAGKILIDNVDISQLGLFD--LR 1287
Cdd:cd03260 3 LRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVleLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQDPVLFRGTIRKNLD----PFNERTDDELwDALVRGgAIAKDDLP-EVKLqkpdengthgKMHKFHLdqavee 1362
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEEL-DERVEE-ALRKAALWdEVKD----------RLHALGL------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1363 egsnfSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:cd03260 143 -----SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGR 217
|
250
....*....|
gi 398366407 1442 VAEFDTPWTL 1451
Cdd:cd03260 218 LVEFGPTEQI 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
605-781 |
5.51e-29 |
|
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: 116.15 E-value: 5.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLM---------CGY----PWIQNASVRDNIIF 670
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtDIRQldpadlrrnIGYvpqdVTLFYGTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSPF-NKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:cd03245 101 GAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLK 180
|
170 180 190
....*....|....*....|....*....|..
gi 398366407 750 DEcLTGMLANKTRILATHQLSLIERASRVIVL 781
Cdd:cd03245 181 ER-LRQLLGDKTLIIITHRPSLLDLVDRIIVM 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1213-1444 |
2.87e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 114.38 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQL---GLFDLRRK 1289
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQD-PVLFRGTIRKNLdpfnertddelwdALV-----RGGAIAKDDLPEVkLqkpDENGTHGKMHKF--HLdqave 1361
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENV-------------ALPlrvtgKSRKEIRRRVREV-L---DLVGLSDKAKALphEL----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1362 eegsnfSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEF---GdCTILcIA-HRLKTIVNYD-RILV 1436
Cdd:COG2884 139 ------SGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEI-MELLEEInrrG-TTVL-IAtHDLELVDRMPkRVLE 209
|
....*...
gi 398366407 1437 LEKGEVAE 1444
Cdd:COG2884 210 LEDGRLVR 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
605-799 |
2.88e-28 |
|
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: 114.63 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLL---------MCGY----PWIQNASVRDNIIF 670
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGiDIRdisrkslrsMIGVvlqdTFLFSGTIMENIRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSPFNKEkyDEVVRVCSLKADLDI---LPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKH 747
Cdd:cd03254 100 GRPNATD--EEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398366407 748 ImDECLTGMLANKTRILATHQLSLIERASRVIVLgTDGQ-VDIGTVDELKARN 799
Cdd:cd03254 178 I-QEALEKLMKGRTSIIIAHRLSTIKNADKILVL-DDGKiIEEGTHDELLAKK 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1213-1448 |
6.05e-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: 6.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfDLRRKLAI 1292
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLF-RGTIRKNLDPFNertddELWDALVRGGAIAKDDLpevklqkpdengthgkMHKFHLDQAVEEEGSNFSLGE 1371
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYFA-----ELYGLFDEELKKRIEEL----------------IELLGLEEFLDRRVGELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVDYETDGKIQtRIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTP 1448
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLR-EILRALKKegKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSL 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1216-1442 |
1.17e-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: 110.99 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQ 1295
Cdd:cd03214 3 ENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1296 dpVLfrgtIRKNLDPFNERTDDELwdalvrggaiakddlpevklqkpdengthgkmhkfhldqaveeegsnfSLGERQLL 1375
Cdd:cd03214 81 --AL----ELLGLAHLADRPFNEL------------------------------------------------SGGERQRV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1376 ALTRALVRQSKILILDEATSSVDY----ETDGKIQtRIVEEFGdCTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIahqiELLELLR-RLARERG-KTVVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
604-799 |
1.34e-27 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 113.02 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG----DLLMCGY----------PWIQNASVRDNII 669
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirDLNLRWLrsqiglvsqePVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 670 FGSpfNKEKYDEVVRVCSLKADLDI---LPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGK 746
Cdd:cd03249 99 YGK--PDATDEEVEEAAKKANIHDFimsLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398366407 747 hIMDECLTGMLANKTRILATHQLSLIERASRVIVLGtDGQ-VDIGTVDELKARN 799
Cdd:cd03249 177 -LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQ-NGQvVEQGTHDELMAQK 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1220-1444 |
1.43e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 119.82 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1220 FAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVL 1299
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1300 FRGTIRKNLdpfnertddelwdALVRggaiakddlPEVKLQKPDENGTHGKMHKFHL------DQAVEEEGSNFSLGERQ 1373
Cdd:PRK10789 401 FSDTVANNI-------------ALGR---------PDATQQEIEHVARLASVHDDILrlpqgyDTEVGERGVMLSGGQKQ 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 1374 LLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE 1444
Cdd:PRK10789 459 RISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
604-799 |
3.49e-27 |
|
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: 111.55 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLL---------MCGY-PwiQ-----NASVRDN 667
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqDIRevtldslrrAIGVvP--QdtvlfNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGSPFNKEkyDEVVRVCsLKADLD--I--LPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSR 743
Cdd:cd03253 95 IRYGRPDATD--EEVIEAA-KAAQIHdkImrFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 744 VGKHIMdECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKARN 799
Cdd:cd03253 172 TEREIQ-AALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1213-1454 |
3.72e-27 |
|
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: 111.52 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVD--FAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDL---R 1287
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQDpvlFrgtirkNLdpFNERTddelwdalVRGGaIAkddLPevkLQkpdengtHGKMHKFHLDQAVEE----- 1362
Cdd:cd03258 82 RRIGMIFQH---F------NL--LSSRT--------VFEN-VA---LP---LE-------IAGVPKAEIEERVLEllelv 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1363 --EG------SNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE---EFGdCTILCIAHRLKTIVNY 1431
Cdd:cd03258 129 glEDkadaypAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinrELG-LTIVLITHEMEVVKRI 207
|
250 260
....*....|....*....|....
gi 398366407 1432 -DRILVLEKGEVAEFDTPWTLFSQ 1454
Cdd:cd03258 208 cDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
605-781 |
4.69e-27 |
|
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: 117.77 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL----------MCGY----PWIQNASVRDNIIF 670
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadadadswrdQIAWvpqhPFLFAGTIAENIRL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSPFNKE-KYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:TIGR02857 419 ARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
170 180 190
....*....|....*....|....*....|..
gi 398366407 750 DEcLTGMLANKTRILATHQLSLIERASRVIVL 781
Cdd:TIGR02857 499 EA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1210-1454 |
4.80e-27 |
|
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: 117.31 E-value: 4.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEII-FENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRL---NELTAGKILIDNVDISQLGLFD 1285
Cdd:COG1123 1 MTPLLeVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 LRRKLAIIPQDPvlfrgtiRKNLDPfnERTDDELWDALVRGGAIAKDDLPEVKLQkpdengthgkMHKFHLDQAVEEEGS 1365
Cdd:COG1123 81 RGRRIGMVFQDP-------MTQLNP--VTVGDQIAEALENLGLSRAEARARVLEL----------LEAVGLERRLDRYPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1366 NFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQ---TRIVEEFGdCTILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILdllRELQRERG-TTVLLITHDLGVVAEIaDRVVVMDDGR 220
|
250
....*....|...
gi 398366407 1442 VAEFDTPWTLFSQ 1454
Cdd:COG1123 221 IVEDGPPEEILAA 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1216-1455 |
2.63e-26 |
|
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: 109.36 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYRPGlpIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQ 1295
Cdd:COG1120 5 ENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1296 DPVL-FRGTIR-----------KNLDPFNERTDDELWDALVRGGaIAkddlpevklqkpdengthgkmhkfHL-DQAVEE 1362
Cdd:COG1120 83 EPPApFGLTVRelvalgryphlGLFGRPSAEDREAVEEALERTG-LE------------------------HLaDRPVDE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1363 egsnFSLGERQLLALTRALVRQSKILILDEATSSVD----YETDGKIQtRIVEEFGdCTILCIAHRLKTIVNY-DRILVL 1437
Cdd:COG1120 138 ----LSGGERQRVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLR-RLARERG-RTVVMVLHDLNLAARYaDRLVLL 211
|
250
....*....|....*...
gi 398366407 1438 EKGEVAEFDTPWTLFSQE 1455
Cdd:COG1120 212 KDGRIVAQGPPEEVLTPE 229
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
911-1186 |
3.87e-26 |
|
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: 110.00 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 911 SLFSSVWLSYWTENKfKNRPPS---FYMGLYSFFVFAAFIFMNGQFTILCAMGIMASKWLNLRAVKRILHTPMSYIDTTP 987
Cdd:cd18559 15 SGPSNLWLLLWFDDP-VNGPQEhgqVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 988 LGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPfLLVIFVLIADHYQSSGREIKRLEAVQR 1067
Cdd:cd18559 94 SGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIP-LGLLYVPVNRVYAASSRQLKRLESVSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1068 SFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINkmNEAGYL-VVVLQRWVGIFLDMVA---IAFALIITLLCVTRAFP 1143
Cdd:cd18559 173 DPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD--NELAYLpSIVYLRALAVRLWCVGpciVLFASFFAYVSRHSLAG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 398366407 1144 ISAASVgvllTYVLQLPGLLNTILRAMTQTENDMNSAERLVTY 1186
Cdd:cd18559 251 LVALKV----FYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1179-1445 |
4.03e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 115.23 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1179 SAERLVTYATELPLEAsyrkPEMTPPEswPSmGEIIFENVDFAYrPGLP-IVLKNLNLNIKSGEKIGICGRTGAGKSTIM 1257
Cdd:COG4618 304 AYRRLNELLAAVPAEP----ERMPLPR--PK-GRLSVENLTVVP-PGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1258 SALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNLDPFNERTDDELWDALVRGGA---IAKddL 1334
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVhemILR--L 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1335 PevklqkpdeNGthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE--E 1412
Cdd:COG4618 454 P---------DG---------YDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlkA 515
|
250 260 270
....*....|....*....|....*....|...
gi 398366407 1413 FGdCTILCIAHRLKTIVNYDRILVLEKGEVAEF 1445
Cdd:COG4618 516 RG-ATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
213-501 |
4.86e-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: 109.95 E-value: 4.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 213 FAILANCTSgfnPMITKRLIEFVEEKAifHSMhvNKGIGYAIGACLMMFVNGLTFNHFFHTSQLTGVQAKSILTKAAMKK 292
Cdd:cd18598 8 LADVLGFAG---PLLLNKLVEFLEDSS--EPL--SDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 293 MFNASNYARHCFPNGKVTSFVTTDLARI-EFALSFQPFLAGfPAILAICIVLL--------IVNLGpIALVgigiffggf 363
Cdd:cd18598 81 ALRVRSSSLSKFSTGEIVNLMSTDADRIvNFCPSFHDLWSL-PLQIIVALYLLyqqvgvafLAGLV-FALV--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 364 fisLFAFKLILGFRIAAN-----IFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKmqlsRNFLIAM 438
Cdd:cd18598 150 ---LIPINKWIAKRIGALsekmmKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKG----RKYLDAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 439 AM----SLPSIASLVTFlAMYkVNKGGR-QPGNIFASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRL 501
Cdd:cd18598 223 CVyfwaTTPVLISILTF-ATY-VLMGNTlTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1213-1441 |
9.30e-26 |
|
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: 105.35 E-value: 9.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLF--DLRRKL 1290
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDPVLFRG-TIRKNLdpfnertddelwdalvrggaiakddlpevklqkpdengTHGkmhkfhldqaveeegsnFSL 1369
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI--------------------------------------ALG-----------------LSG 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:cd03229 104 GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRAllkSLQAQLG-ITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1213-1458 |
1.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.77 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPvlfrgtirknldpfnertDDELWdalvrgGAIAKDDLP---EVKLQKPDENGT--HGKMHKFHLDQAVEEEGSNF 1367
Cdd:PRK13632 88 IFQNP------------------DNQFI------GATVEDDIAfglENKKVPPKKMKDiiDDLAKKVGMEDYLDKEPQNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1368 SLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE--EFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEF 1445
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQ 223
|
250
....*....|...
gi 398366407 1446 DTPWTLFSQEDSI 1458
Cdd:PRK13632 224 GKPKEILNNKEIL 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1068-1446 |
3.20e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 114.36 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1068 SFVYNN-----LNEVLGGMDTIKAYRSQERFLAK---SDFLINKMNEAGYLVVVLQrwVGIFLDMVAIAFA--------L 1131
Cdd:PTZ00265 228 SLLYNNntmsiIEEALVGIRTVVSYCGEKTILKKfnlSEKLYSKYILKANFMESLH--IGMINGFILASYAfgfwygtrI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1132 IITLLcvTRAFP---ISAASVGVLLTYVLQLPGLLNTILRAMTQTendMNSAErlvtyATELPLEASYRKPEM---TPPE 1205
Cdd:PTZ00265 306 IISDL--SNQQPnndFHGGSVISILLGVLISMFMLTIILPNITEY---MKSLE-----ATNSLYEIINRKPLVennDDGK 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1206 SWPSMGEIIFENVDFAY--RPGLPIvLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILI-DNVDISQLG 1282
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYdtRKDVEI-YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDIN 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1283 LFDLRRKLAIIPQDPVLFRGTIRKNL--------------DPFNERTDDELWDALVRGGAIAK--DDLPEVkLQKPDENG 1346
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsNYYNEDGNDSQENKNKRNSCRAKcaGDLNDM-SNTTDSNE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1347 -THGK-------------------MHKF------HLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYE 1400
Cdd:PTZ00265 534 lIEMRknyqtikdsevvdvskkvlIHDFvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1401 TDGKIQTRIVEEFGD---CTILcIAHRLKTIVNYDRILVL---EKGEVAEFD 1446
Cdd:PTZ00265 614 SEYLVQKTINNLKGNenrITII-IAHRLSTIRYANTIFVLsnrERGSTVDVD 664
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
212-501 |
8.46e-25 |
|
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: 106.55 E-value: 8.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 212 VFAILANCTSGFNPMITKRLIEFVEEK-AIFHSMHVNKGI-----------GYAIGACLMM--FVNGLTFNHFFHTSQLT 277
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENtYSSSNSTDKLSVsyvtveeffsnGYVLAVILFLalLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 278 GVQAKSILTKAAMKKMFNASNYarhCFPNGK-----VTSFVTTDLARIEFALSFQPFLAGFPAILAICIVLLIVNLGPIA 352
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSSW---NLSSGSmtigqITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 353 LVGIGIFFGgffisLFAFKLILGFRIAAN-----IFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRK 427
Cdd:cd18591 161 LIGAALILV-----MTPLQYLIARKLSKNqkstlEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLK 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 428 MQLSRNFLIAMAMSLPSIASLVTFLAMYKVNKGGRQPGNIFASLSLFQVLSLQMFFLPIAIGTGIDMIIGLGRL 501
Cdd:cd18591 236 DAVYWSLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1213-1461 |
1.12e-24 |
|
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: 104.69 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVlKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLF-RGTIRKN--LDP---------FNERTDDELwdALVrggaiakdDLPEVKLQK--PDEngthgkmhkfhldq 1358
Cdd:cd03295 80 VIQQIGLFpHMTVEENiaLVPkllkwpkekIRERADELL--ALV--------GLDPAEFADryPHE-------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1359 aveeegsnFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQ---TRIVEEFGDcTILCIAHRL-KTIVNYDRI 1434
Cdd:cd03295 136 --------LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQeefKRLQQELGK-TIVFVTHDIdEAFRLADRI 206
|
250 260
....*....|....*....|....*..
gi 398366407 1435 LVLEKGEVAEFDTPwtlfsqeDSIFRS 1461
Cdd:cd03295 207 AIMKNGEIVQVGTP-------DEILRS 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
605-797 |
3.23e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 109.03 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG----DLLMCGY----------PWIQNASVRDNIIF 670
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltKLQLDSWrsrlavvsqtPFLFSDTVANNIAL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSP-FNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:PRK10789 412 GRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQIL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398366407 750 DEcLTGMLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKA 797
Cdd:PRK10789 492 HN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
891-1445 |
4.18e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 891 KWGFIALplyAILVVGTTFCSLFSSVWLSYWtenkfkNRPpsFYMGLySFFVFAAFIFMNGQFTILCAMGIMAS------ 964
Cdd:COG4178 20 KWKAWGL---LALLLLLTLASVGLNVLLNFW------NRD--FYDAL-QARDAAAFWQQLGVFALLAAISILLAvyqtyl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 965 ---------KWLNLRAVKRILHtpmsyidttplGRI---LNRFTKDTDSLDNELTESLRLMTSQ--------FANIVGVC 1024
Cdd:COG4178 88 rqrlqirwrEWLTERLLDRWLS-----------NRAyyrLQLSGGEIDNPDQRIAEDIRLFTETtlslslglLSSVVTLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1025 VMCIV----------YLPWFAIAIPFLLVIFVLIadhYQSS--------GREIKRLEAVQR----SFVYN--NLNEvlgG 1080
Cdd:COG4178 157 SFIGIlwslsgsltfTLGGYSITIPGYMVWAALI---YAIIgtllthliGRPLIRLNFEQQrreaDFRFAlvRVRE---N 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1081 MDTIKAYR--SQERFLAKSDFlinkmnEAgylvvVLQRWVGIfldmvaIAFALIITLlcVTRAFpisaASVGVLLTYVLQ 1158
Cdd:COG4178 231 AESIALYRgeAAERRRLRRRF------DA-----VIANWRRL------IRRQRNLTF--FTTGY----GQLAVIFPILVA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1159 LP---------GLLNTILRAMTQTENDMN--------------SAERLVTYATELplEASYRKPEMTPPESWPSMGEIIF 1215
Cdd:COG4178 288 APryfageitlGGLMQAASAFGQVQGALSwfvdnyqslaewraTVDRLAGFEEAL--EAADALPEAASRIETSEDGALAL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFaYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILI-DNVDIsqlgLFdlrrklaiIP 1294
Cdd:COG4178 366 EDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----LF--------LP 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1295 QDPVLFRGTIRKNL---DPFNERTDDELWDALVRggaiakddlpeVKLQkpdengthgkmhkfHLDQAVEEE---GSNFS 1368
Cdd:COG4178 433 QRPYLPLGTLREALlypATAEAFSDAELREALEA-----------VGLG--------------HLAERLDEEadwDQVLS 487
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 1369 LGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEF 1445
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQL 564
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
607-814 |
6.88e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.39 E-value: 6.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 607 LNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMrKTDGKVEVNG----DLLMCGY----PWI-QN-----ASVRDNIIFGS 672
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielrELDPESWrkhlSWVgQNpqlphGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 673 P-FNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMdE 751
Cdd:PRK11174 448 PdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM-Q 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 752 CLTGMLANKTRILATHQLSLIERASRVIVLgTDGQ-VDIGTVDELKARNQTLINLLqfsSQNSE 814
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVM-QDGQiVQQGDYAELSQAGGLFATLL---AHRQE 586
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1213-1441 |
1.31e-23 |
|
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: 100.24 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPG---LPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALyrLNELTAGKilidnvdisqlGLFDLRRK 1289
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEKLS-----------GSVSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVLFRGTIRKNLdPFNERTDDELWDALVRGGAIAKD-------DLPEVklqkpdenGthgkmhkfhldqaveE 1362
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENI-LFGKPFDEERYEKVIKACALEPDleilpdgDLTEI--------G---------------E 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1363 EGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIqtriveeFGDC---------TILCIAHRLKTIVNYDR 1433
Cdd:cd03250 124 KGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQ 196
|
....*...
gi 398366407 1434 ILVLEKGE 1441
Cdd:cd03250 197 IVVLDNGR 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1213-1448 |
1.93e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.52 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGlpIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfDLRRKLAI 1292
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRG-TIRKNLDPFnertddelwdALVRG--GAIAKDDLPEVklqkpdengthgkMHKFHLDQAVEEEGSNFSL 1369
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFF----------ARLYGlpRKEARERIDEL-------------LELFGLTDAADRKVGTLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSVDyetdgkIQTR-----IVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:COG1131 135 GMKQRLGLALALLHDPELLILDEPTSGLD------PEARrelweLLRELAAegKTVLLSTHYLEEAERLcDRVAIIDKGR 208
|
....*..
gi 398366407 1442 VAEFDTP 1448
Cdd:COG1131 209 IVADGTP 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
604-781 |
1.97e-23 |
|
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: 99.85 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL----------MCGY----PWIQ--NASVRDN 667
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtklslkelrrKVGLvfqnPDDQffGPTVEEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGSPFNKEKYDEVVrvcslKADLDILPAGDMTEIGERGI-TLSGGQKARINLArSVY-KKKDIYLFDDVLSAVDSRVG 745
Cdd:cd03225 97 VAFGLENLGLPEEEIE-----ERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIA-GVLaMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398366407 746 KHIMDecltgML-----ANKTRILATHQLSLIER-ASRVIVL 781
Cdd:cd03225 171 RELLE-----LLkklkaEGKTIIIVTHDLDLLLElADRVIVL 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1217-1447 |
2.32e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 100.65 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1217 NVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQD 1296
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1297 PVLF---RGTIRKNLD-PFNE----RTDDELWDALVRGGaiakddLP-EVKLQKPDEngthgkmhkfhldqaveeegsnF 1367
Cdd:COG1124 88 PYASlhpRHTVDRILAePLRIhglpDREERIAELLEQVG------LPpSFLDRYPHQ----------------------L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1368 SLGERQLLALTRALVRQSKILILDEATSSVDYETdgkiQTRIVEEFGD------CTILCIAHRLKtIVNY--DRILVLEK 1439
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSV----QAEILNLLKDlreergLTYLFVSHDLA-VVAHlcDRVAVMQN 214
|
....*...
gi 398366407 1440 GEVAEFDT 1447
Cdd:COG1124 215 GRIVEELT 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1213-1448 |
2.64e-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: 100.34 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---LFDLRRK 1289
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDP-----------VL-----FRGTIRKNLDPFNERtddELWDALvrgGAIAKDDLPEVKLQKPDEngthgkmhk 1353
Cdd:cd03256 80 IGMIFQQFnlierlsvlenVLsgrlgRRSTWRSLFGLFPKE---EKQRAL---AALERVGLLDKAYQRADQ--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1354 fhldqaveeegsnFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQ---TRIVEEFGDcTILCIAHRLKTIVN 1430
Cdd:cd03256 145 -------------LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMdllKRINREEGI-TVIVSLHQVDLARE 210
|
250
....*....|....*....
gi 398366407 1431 Y-DRILVLEKGEVAeFDTP 1448
Cdd:cd03256 211 YaDRIVGLKDGRIV-FDGP 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
604-787 |
2.81e-23 |
|
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: 98.06 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLlmcgypwiqnasvrdniifgSPFNKEKYDEv 682
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGaDI--------------------SQWDPNELGD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 683 vRVCSLKADlDILPAGDMTEIgergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvGKHIMDECLTGM-LANKT 761
Cdd:cd03246 77 -HVGYLPQD-DELFSGSIAEN-----ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQAIAALkAAGAT 148
|
170 180
....*....|....*....|....*.
gi 398366407 762 RILATHQLSLIERASRVIVLgTDGQV 787
Cdd:cd03246 149 RIVIAHRPETLASADRILVL-EDGRV 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1213-1456 |
3.51e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.28 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLP---IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDIS--QLGLFDLR 1287
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQDP--VLFRGTIRKNLD--PFN-ERTDDELWDALVRGGAIAKDDLPEVKLQKPdengthgkmhkFHLdqavee 1362
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAfgPINlGLSEEEIENRVKRAMNIVGLDYEDYKDKSP-----------FEL------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1363 egsnfSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKI--QTRIVEEFGDCTILCIAHRLKTIVNY-DRILVLEK 1439
Cdd:PRK13637 146 -----SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIlnKIKELHKEYNMTIILVSHSMEDVAKLaDRIIVMNK 220
|
250
....*....|....*..
gi 398366407 1440 GEVAEFDTPWTLFSQED 1456
Cdd:PRK13637 221 GKCELQGTPREVFKEVE 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1213-1442 |
5.23e-23 |
|
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: 97.47 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGlpIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfDLRRKLAI 1292
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRG-TIRKNLDpfnertddelwdalvrggaiakddlpevklqkpdengthgkmhkfhldqaveeegsnFSLGE 1371
Cdd:cd03230 78 LPEEPSLYENlTVRENLK---------------------------------------------------------LSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVDyetdgkIQTR-----IVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLD------PESRrefweLLRELKKegKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
594-787 |
6.02e-23 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 98.75 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPW-------IQNA-- 662
Cdd:cd03259 4 KGLSKTygSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPErrnigmvFQDYal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 663 ----SVRDNIIFGSPFNKEKYDEVVRVCSLKADLdilpaGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVL 737
Cdd:cd03259 84 fphlTVAENIAFGLKLRGVPKAEIRARVRELLEL-----VGLEGLLNRYPhELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398366407 738 SAVDSRVGKHIMDEcLTGMLAN--KTRILATHQLSLIER-ASRVIVLgTDGQV 787
Cdd:cd03259 159 SALDAKLREELREE-LKELQRElgITTIYVTHDQEEALAlADRIAVM-NEGRI 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
604-798 |
6.54e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.96 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLM---CGY-----------PWIQNASVRDNII 669
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydHHYlhrqvalvgqePVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 670 FGSPF-NKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVgKHI 748
Cdd:TIGR00958 577 YGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-EQL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398366407 749 MDECLTgmLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKAR 798
Cdd:TIGR00958 656 LQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1213-1446 |
1.14e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 97.59 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGlpIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISqlGLFDLRRKLAI 1292
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLF-RGTIRKNLDpFnertddelwdALVRGGaIAKDDLPEVKLQKPDENGTHGKMHKFhldqaVEEegsnFSLGE 1371
Cdd:cd03259 77 VFQDYALFpHLTVAENIA-F----------GLKLRG-VPKAEIRARVRELLELVGLEGLLNRY-----PHE----LSGGQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGDCTI---------LCIAhrlktivnyDRILVLEK 1439
Cdd:cd03259 136 QQRVALARALAREPSLLLLDEPLSALDAKLREELREelkELQRELGITTIyvthdqeeaLALA---------DRIAVMNE 206
|
....*..
gi 398366407 1440 GEVAEFD 1446
Cdd:cd03259 207 GRIVQVG 213
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
250-501 |
1.54e-22 |
|
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: 99.60 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 250 IGYAIGACLMMFVNGLTFNHFFHTSQLTGVQAKSILTKAAMKKMFNASNYARHCFPNGKVTSFVTTDLARIEFALSFQPF 329
Cdd:cd18593 40 YLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 330 LAGFPAILAICIVLLIVNLGPIALVGIGIFFGGFFISLFAFKLILGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDA 409
Cdd:cd18593 120 LWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 410 YEKNIQDIRTKEISKVRKmqlsRNFLIAMAMSLPSIAS----LVTFLAMYKVNKgGRQPGNIFASLSLFQVLSLQM-FFL 484
Cdd:cd18593 200 FAKLVDDLRRKEIKKVRR----TSFLRALNMGLFFVSSklilFLTFLAYILLGN-ILTAERVFVTMALYNAVRLTMtLFF 274
|
250
....*....|....*..
gi 398366407 485 PIAIGTGIDMIIGLGRL 501
Cdd:cd18593 275 PFAIQFGSELSVSIRRI 291
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
604-786 |
1.58e-22 |
|
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: 95.39 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGdllmCGYPWIQNASVRDNIIFgspfnkekydevv 683
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG----KDIAKLPLEELRRRIGY------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 684 rvcslkadldiLPagdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvGKHIMDECLTGMLA-NKTR 762
Cdd:cd00267 78 -----------VP------------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELLRELAEeGRTV 133
|
170 180
....*....|....*....|....
gi 398366407 763 ILATHQLSLIERASRVIVLGTDGQ 786
Cdd:cd00267 134 IIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
605-787 |
2.24e-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: 97.18 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMC-------------------GYPWIQNASVR 665
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelaafrrrhigfvfqSFNLLPDLTAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 DNIIFGSPFNKEKYDEVVRVCS-------LKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLS 738
Cdd:cd03255 101 ENVELPLLLAGVPKKERRERAEellervgLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADEPTG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 398366407 739 AVDSRVGKHIMDEcLTGM--LANKTRILATHQLSLIERASRVIVLgTDGQV 787
Cdd:cd03255 170 NLDSETGKEVMEL-LRELnkEAGTTIVVVTHDPELAEYADRIIEL-RDGKI 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1216-1442 |
2.43e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 96.56 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYRPGlPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLglfDLRRKLAIIPQ 1295
Cdd:cd03226 3 ENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1296 DP--VLFRGTIRKNLDPFNERTDDELWDAlvrggaiakddlpevklqkpdengtHGKMHKFHLDQAVEEEGSNFSLGERQ 1373
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQA-------------------------ETVLKDLDLYALKERHPLSLSGGQKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1374 LLALTRALVRQSKILILDEATSSVDYETdgkiQTRIVEEFGDC-----TILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:cd03226 134 RLAIAAALLSGKDLLIFDEPTSGLDYKN----MERVGELIRELaaqgkAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1213-1442 |
2.82e-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: 96.79 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIV--LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDL---- 1286
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1287 RRKLAIIPQDPVLFRG-TIRKNLD-PF----NERTDDELWdalvrggaiAKDDLPEVKLQKpdengthgKMHKFhldqav 1360
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVElPLllagVPKKERRER---------AEELLERVGLGD--------RLNHY------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1361 eeeGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQ---TRIVEEFGdCTILCIAHRLKtIVNY-DRILV 1436
Cdd:cd03255 138 ---PSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMellRELNKEAG-TTIVVVTHDPE-LAEYaDRIIE 212
|
....*.
gi 398366407 1437 LEKGEV 1442
Cdd:cd03255 213 LRDGKI 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1213-1458 |
1.03e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.74 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPV-LFRGTIRKNLDPFNERTDDELWDALVRggaIAKDDLPEVKLqkpdengthgkmhkfhLDQAVEEEGSnFSLGE 1371
Cdd:PRK13648 88 VFQNPDnQFVGSIVKYDVAFGLENHAVPYDEMHR---RVSEALKQVDM----------------LERADYEPNA-LSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRI--VEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTPW 1449
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVrkVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
....*....
gi 398366407 1450 TLFSQEDSI 1458
Cdd:PRK13648 228 EIFDHAEEL 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
604-795 |
2.06e-21 |
|
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: 94.71 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL----------MCGY----PWIQ--NASVRDN 667
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkknlrelrrKVGLvfqnPDDQlfAPTVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGsPFN----KEKYDEVVRvcslkadlDILPAGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDS 742
Cdd:COG1122 97 VAFG-PENlglpREEIRERVE--------EALELVGLEHLADRPPhELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 743 RVGKHIMDecltgMLA-----NKTRILATHQLSLIER-ASRVIVLGtDGQ-VDIGTVDEL 795
Cdd:COG1122 168 RGRRELLE-----LLKrlnkeGKTVIIVTHDLDLVAElADRVIVLD-DGRiVADGTPREV 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1210-1459 |
2.18e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.45 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEIIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISqlglfDL--- 1286
Cdd:COG3839 1 MASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLppk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1287 RRKLAIIPQDPVLF-RGTIRKNLDpF---NERTDDELWDALVRggAIAK----DDLpevkLQ-KPDEngthgkmhkfhLd 1357
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIA-FplkLRKVPKAEIDRRVR--EAAEllglEDL----LDrKPKQ-----------L- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1358 qaveeegsnfSLGERQLLALTRALVRQSKILILDEATSSVDYETdgKIQTRIveefgdctilCIA---HRLKTIVNY--- 1431
Cdd:COG3839 135 ----------SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKL--RVEMRA----------EIKrlhRRLGTTTIYvth 192
|
250 260 270
....*....|....*....|....*....|....*..
gi 398366407 1432 ---------DRILVLEKGEVAEFDTPWTLFSQEDSIF 1459
Cdd:COG3839 193 dqveamtlaDRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1208-1455 |
2.74e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 94.77 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1208 PSMGEIIFENVDFAYRpGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLglfdlR 1287
Cdd:COG1121 2 MMMPAIELENLTVSYG-GRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQdpvlfRGTIRKNLdPFNertddeLWDaLVRGGAiakddLPEVKLQKPdengtHGKMHKFHLDQAVEEEG--- 1364
Cdd:COG1121 75 RRIGYVPQ-----RAEVDWDF-PIT------VRD-VVLMGR-----YGRRGLFRR-----PSRADREAVDEALERVGled 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1365 ------SNFSLGERQ--LLAltRALVRQSKILILDEATSSVDYETdgkiQTRIVEEFGD-----CTILCIAHRLKTIVNY 1431
Cdd:COG1121 132 ladrpiGELSGGQQQrvLLA--RALAQDPDLLLLDEPFAGVDAAT----EEALYELLRElrregKTILVVTHDLGAVREY 205
|
250 260
....*....|....*....|....*
gi 398366407 1432 -DRILVLEKGEVAeFDTPWTLFSQE 1455
Cdd:COG1121 206 fDRVLLLNRGLVA-HGPPEEVLTPE 229
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
605-781 |
2.86e-21 |
|
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: 94.07 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL-------------MCGY-PWIQNASVRDNIIF 670
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqyehkylhskvsLVGQePVLFARSLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSPfnkEKYDEVVRVCSLKADLD----ILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvGK 746
Cdd:cd03248 111 GLQ---SCSFECVKEAAQKAHAHsfisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SE 186
|
170 180 190
....*....|....*....|....*....|....*
gi 398366407 747 HIMDECLTGMLANKTRILATHQLSLIERASRVIVL 781
Cdd:cd03248 187 QQVQQALYDWPERRTVLVIAHRLSTVERADQILVL 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1229-1448 |
4.14e-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: 93.65 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD-LRRKLAIIPQDPVLFRG-TIRK 1306
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1307 NLdpfnertddeLWDALVRGGAIAKDDLPEVklqkpdengthgkmhkFH----LDQAVEEEGSNFSLGERQLLALTRALV 1382
Cdd:cd03224 95 NL----------LLGAYARRRAKRKARLERV----------------YElfprLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1383 RQSKILILDEATSsvdyetdGkIQTRIVEEFGDC---------TILCI---AHRLKTIVnyDRILVLEKGEVAEFDTP 1448
Cdd:cd03224 149 SRPKLLLLDEPSE-------G-LAPKIVEEIFEAirelrdegvTILLVeqnARFALEIA--DRAYVLERGRVVLEGTA 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1215-1443 |
4.99e-21 |
|
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: 92.98 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1215 FENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISqlglfDLRRKLAIIP 1294
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1295 Q-------------DPVLFRGTIRKNLDPFNERTDDELWD-ALVRGGAiakddlpevklqkpdengthGKMHKFHLDQAv 1360
Cdd:cd03235 75 QrrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDeALERVGL--------------------SELADRQIGEL- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1361 eeegsnfSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFGD--CTILCIAHRLKTIVNY-DRILVL 1437
Cdd:cd03235 134 -------SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI-YELLRELRRegMTILVVTHDLGLVLEYfDRVLLL 205
|
....*.
gi 398366407 1438 EKGEVA 1443
Cdd:cd03235 206 NRTVVA 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
605-781 |
6.53e-21 |
|
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: 92.60 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-----DLLMCGY-------PWIQNASVRD------ 666
Cdd:cd03235 16 EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekERKRIGYvpqrrsiDRDFPISVRDvvlmgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 667 --NIIFGSPFNKEKYDEVvrvcslkadLDILPAGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSR 743
Cdd:cd03235 96 ygHKGLFRRLSKADKAKV---------DEALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398366407 744 VGKHIMDecltgMLA-----NKTRILATHQLSLIER-ASRVIVL 781
Cdd:cd03235 167 TQEDIYE-----LLRelrreGMTILVVTHDLGLVLEyFDRVLLL 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1208-1444 |
8.80e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 93.62 E-value: 8.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1208 PSMGEIIFENVDFAYRP--GLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGlfd 1285
Cdd:COG1116 3 AAAPALELRGVSKRFPTggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 lrRKLAIIPQDPVLF--RgTIRKNLdpfnertddELwdALVRGG-------AIAKDDLPEVKLQkpdengthGKMHKF-H 1355
Cdd:COG1116 80 --PDRGVVFQEPALLpwL-TVLDNV---------AL--GLELRGvpkaerrERARELLELVGLA--------GFEDAYpH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1356 -LdqaveeegsnfSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAH------RL 1425
Cdd:COG1116 138 qL-----------SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDellRLWQETG-KTVLFVTHdvdeavFL 205
|
250 260
....*....|....*....|.
gi 398366407 1426 KtivnyDRILVLEK--GEVAE 1444
Cdd:COG1116 206 A-----DRVVVLSArpGRIVE 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
578-794 |
1.04e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 578 NKAKRLDNMLKDRDGPEdleKTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDL-----L 652
Cdd:COG1134 19 EPSRSLKELLLRRRRTR---REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsalleL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 653 MCGYpwIQNASVRDNIIFGSPFN-------KEKYDEVVrvcslkadldilpagDMTEIGE------RgiTLSGGQKARIN 719
Cdd:COG1134 96 GAGF--HPELTGRENIYLNGRLLglsrkeiDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 720 LARSVYKKKDIYLFDDVLSAVDsrvgKHIMDECLTGMLA----NKTRILATHQLSLIER-ASRVIVLGtDGQV-DIGTVD 793
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGD----AAFQKKCLARIRElresGRTVIFVSHSMGAVRRlCDRAIWLE-KGRLvMDGDPE 231
|
.
gi 398366407 794 E 794
Cdd:COG1134 232 E 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1213-1454 |
1.19e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.14 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVD--FAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTimsaLYR-LNEL---TAGKILIDNVDISQL---GL 1283
Cdd:COG1135 2 IELENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRcINLLerpTSGSVLVDGVDLTALserEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1284 FDLRRKLAIIPQDpvlFrgtirkNLdpFNERTddelwdalVRGGaIAkddLPevkLQkpdengtHGKMHKFHLDQAVEE- 1362
Cdd:COG1135 78 RAARRKIGMIFQH---F------NL--LSSRT--------VAEN-VA---LP---LE-------IAGVPKAEIRKRVAEl 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1363 ------EG------SNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAHRL-- 1425
Cdd:COG1135 125 lelvglSDkadaypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDllkDINRELG-LTIVLITHEMdv 203
|
250 260 270
....*....|....*....|....*....|
gi 398366407 1426 -KTIVnyDRILVLEKGEVAEFDTPWTLFSQ 1454
Cdd:COG1135 204 vRRIC--DRVAVLENGRIVEQGPVLDVFAN 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
604-782 |
1.39e-20 |
|
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: 91.76 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL-----MCGY--------PWiqnASVRDNIIF 670
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVtgpgpDRGYvfqqdallPW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSPFN-------KEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSR 743
Cdd:cd03293 97 GLELQgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398366407 744 VGKHIMDEcLTGMLA--NKTRILATHQLS-LIERASRVIVLG 782
Cdd:cd03293 166 TREQLQEE-LLDIWRetGKTVLLVTHDIDeAVFLADRVVVLS 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1213-1461 |
1.44e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 92.18 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---LFDLRRK 1289
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVLFRG-TIRKNLD-PFNERTddELWDALVRggAIAKDDLPEVklqkpdenGTHGKMHKFhldqaveeeGSNF 1367
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHT--RLSEEEIR--EIVLEKLEAV--------GLRGAEDLY---------PAEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1368 SLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAHRLKTIVNY-DRILVLEKGEVA 1443
Cdd:cd03261 138 SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDlirSLKKELG-LTSIMVTHDLDTAFAIaDRIAVLYDGKIV 216
|
250
....*....|....*...
gi 398366407 1444 EFDTPWTLFSQEDSIFRS 1461
Cdd:cd03261 217 AEGTPEELRASDDPLVRQ 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1213-1453 |
1.57e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.51 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG-LFDLRRKLA 1291
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1292 IIPQDP-VLFRG-TIRKNLdpfnertddelwdalvrggAIAKDD--LPEVKLQKpdengthgkmhkfHLDQAVEEEG--- 1364
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL-------------------AFGPENlcLPPIEIRK-------------RVDRALAEIGlek 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1365 ------SNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRI--VEEFGDcTILCIAHRLKTIVNYDRILV 1436
Cdd:PRK13644 129 yrhrspKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIkkLHEKGK-TIVYITHNLEELHDADRIIV 207
|
250
....*....|....*..
gi 398366407 1437 LEKGEVAEFDTPWTLFS 1453
Cdd:PRK13644 208 MDRGKIVLEGEPENVLS 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
605-794 |
2.66e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 91.69 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPWI----QN--------ASVRD------ 666
Cdd:COG1121 23 EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIgyvpQRaevdwdfpITVRDvvlmgr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 667 --NIIFGSPFNKEKYDEVVRVcslkadLDILpagDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSR 743
Cdd:COG1121 103 ygRRGLFRRPSRADREAVDEA------LERV---GLEDLADRPIgELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 744 VGKHIMDecltgMLA-----NKTRILATHQLSLIER-ASRVIVLGtDGQVDIGTVDE 794
Cdd:COG1121 174 TEEALYE-----LLRelrreGKTILVVTHDLGAVREyFDRVLLLN-RGLVAHGPPEE 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1213-1449 |
4.85e-20 |
|
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: 90.22 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLP--IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGlfdlrRKL 1290
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDPVLF--RgTIRKNLdpfnertddELwdALVRGGAIAKDDLPEVklqkpdengtHGKMHKFHLDQAVEEEGSNFS 1368
Cdd:cd03293 76 GYVFQQDALLpwL-TVLDNV---------AL--GLELQGVPKAEARERA----------EELLELVGLSGFENAYPHQLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1369 LGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGDcTILCIAHRLKTIVnY--DRILVLEKGE-- 1441
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEellDIWRETGK-TVLLVTHDIDEAV-FlaDRVVVLSARPgr 211
|
....*....
gi 398366407 1442 -VAEFDTPW 1449
Cdd:cd03293 212 iVAEVEVDL 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
594-808 |
7.47e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 90.25 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKtSFRG---FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG---------DLLM----CGYP 657
Cdd:cd03261 4 RGLTK-SFGGrtvLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaELYRlrrrMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 658 WIQNA-----SVRDNIIFG----SPFNKEKYDEVVRVC----SLKADLDILPAgdmteigergiTLSGGQKARINLARSV 724
Cdd:cd03261 83 FQSGAlfdslTVFENVAFPlrehTRLSEEEIREIVLEKleavGLRGAEDLYPA-----------ELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 725 YKKKDIYLFDDVLSAVDSrVGKHIMDEC---LTGMLaNKTRILATHQLSLIER-ASRVIVLGtDGQ-VDIGTVDELKARN 799
Cdd:cd03261 152 ALDPELLLYDEPTAGLDP-IASGVIDDLirsLKKEL-GLTSIMVTHDLDTAFAiADRIAVLY-DGKiVAEGTPEELRASD 228
|
....*....
gi 398366407 800 QTLINllQF 808
Cdd:cd03261 229 DPLVR--QF 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1213-1442 |
9.76e-20 |
|
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: 89.39 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQL---GLFDLRRK 1289
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDpvlFRgtIRKNLDPFnertdDELWDALVRGGAIAKDDLPEVKlQKPDENGTHGKMHKFhldqaveeeGSNFSL 1369
Cdd:cd03292 80 IGVVFQD---FR--LLPDRNVY-----ENVAFALEVTGVPPREIRKRVP-AALELVGLSHKHRAL---------PAELSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFGD--CTILCIAHRlKTIVN--YDRILVLEKGEV 1442
Cdd:cd03292 140 GEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKagTTVVVATHA-KELVDttRHRVIALERGKL 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1210-1460 |
9.98e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.23 E-value: 9.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEII-FENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRR 1288
Cdd:PRK13635 2 KEEIIrVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1289 KLAIIPQDP-VLFRGTIrknldpfnerTDDELWDALVRGGaIAKDDLPEvklqkpdenGTHGKMHKFHLDQAVEEEGSNF 1367
Cdd:PRK13635 82 QVGMVFQNPdNQFVGAT----------VQDDVAFGLENIG-VPREEMVE---------RVDQALRQVGMEDFLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1368 SLGERQLLALTRALVRQSKILILDEATSSVDYEtdGKIQT----RIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVA 1443
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPR--GRREVletvRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
250
....*....|....*..
gi 398366407 1444 EFDTPWTLFSQEDSIFR 1460
Cdd:PRK13635 220 EEGTPEEIFKSGHMLQE 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
594-782 |
1.14e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 89.08 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKTsfRG----FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG------------DLLMCGY- 656
Cdd:COG4133 6 ENLSCR--RGerllFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 657 -PWIQNASVRDNIIF-----GSPFNKEKYDEVVRVCSLKADLDiLPAGdmteigergiTLSGGQKARINLARSVYKKKDI 730
Cdd:COG4133 84 dGLKPELTVRENLRFwaalyGLRADREAIDEALEAVGLAGLAD-LPVR----------QLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 731 YLFDDVLSAVD----SRVGKHIMDECLTGMLAnktrILATHQLSLIERAsRVIVLG 782
Cdd:COG4133 153 WLLDEPFTALDaagvALLAELIAAHLARGGAV----LLTTHQPLELAAA-RVLDLG 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
604-735 |
1.68e-19 |
|
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: 86.55 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGYPWIQ--------------NASVRDNI 668
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqDLTDDERKSLRkeigyvfqdpqlfpRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 669 IFGSPFNKEKYDEV-VRVCSLKADLDILPAGDmTEIGERGITLSGGQKARINLARSVYKKKDIYLFDD 735
Cdd:pfam00005 81 RLGLLLKGLSKREKdARAEEALEKLGLGDLAD-RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
605-787 |
2.07e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 88.08 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG------DLLMCGYPWIQN-------ASVRDNIIFG 671
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakERRKSIGYVMQDvdyqlftDSVREELLLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 672 spfNKEKYDEVVRVCSLKADLDILPAGDmteigERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVD----SRVGKH 747
Cdd:cd03226 97 ---LKELDAGNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknmERVGEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398366407 748 IMDECLTGmlanKTRILATHQLSLIER-ASRVIVLGTDGQV 787
Cdd:cd03226 169 IRELAAQG----KAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1216-1443 |
2.27e-19 |
|
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: 88.89 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDL-RRKLAIIP 1294
Cdd:COG0410 7 ENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1295 QDPVLFRG-TIRKNLdpfnertddELWDALVRGGAIAKDDLPEV-----KLQKpdengthgkmhkfHLDQAveeeGSNFS 1368
Cdd:COG0410 85 EGRRIFPSlTVEENL---------LLGAYARRDRAEVRADLERVyelfpRLKE-------------RRRQR----AGTLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1369 LGERQLLALTRALVRQSKILILDEATSsvdyetdGkIQTRIVEEFGDC---------TILCI---AHRLKTIVnyDRILV 1436
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPSL-------G-LAPLIVEEIFEIirrlnregvTILLVeqnARFALEIA--DRAYV 208
|
....*..
gi 398366407 1437 LEKGEVA 1443
Cdd:COG0410 209 LERGRIV 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1228-1398 |
3.08e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 87.53 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1228 IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfDLRRKLAIIPQDPVLFRG-TIRK 1306
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLGHADGLKPElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1307 NLDpfnertddeLWdALVRGGAIAKDDLPEVklqkpdengthgkMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQSK 1386
Cdd:COG4133 95 NLR---------FW-AALYGLRADREAIDEA-------------LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170
....*....|..
gi 398366407 1387 ILILDEATSSVD 1398
Cdd:COG4133 152 LWLLDEPFTALD 163
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
594-798 |
3.25e-19 |
|
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: 88.76 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPWIQNA--------- 662
Cdd:COG4555 5 ENLSKKygKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQigvlpderg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 663 -----SVRDNIIFGSPFNKEKYDEVVRVCSlkadlDILPAGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDV 736
Cdd:COG4555 85 lydrlTVRENIRYFAELYGLFDEELKKRIE-----ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 737 LSAVDSRVGKHIMDECLTGMLANKTRILATHQLSLIER-ASRVIVLgTDGQ-VDIGTVDELKAR 798
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVIL-HKGKvVAQGSLDELREE 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
605-787 |
3.71e-19 |
|
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: 87.70 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-----------DLLMCG-----YPwiqNASVRDNI 668
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFqnyalYP---HMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 669 IFGSPFNKEKYDE-------VVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVD 741
Cdd:cd03301 94 AFGLKLRKVPKDEidervreVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398366407 742 SRVGKHIMDEcLTGMLAN--KTRILATH-QLSLIERASRVIVLgTDGQV 787
Cdd:cd03301 163 AKLRVQMRAE-LKRLQQRlgTTTIYVTHdQVEAMTMADRIAVM-NDGQI 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
604-782 |
7.32e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.84 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG----------------DLLMcgyPWiqnASVRDN 667
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpdrgvvfqePALL---PW---LTVLDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGSPFN-------KEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAV 740
Cdd:COG1116 101 VALGLELRgvpkaerRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398366407 741 DSRVgKHIMDECLTGMLA--NKTRILATHQLS----LierASRVIVLG 782
Cdd:COG1116 170 DALT-RERLQDELLRLWQetGKTVLFVTHDVDeavfL---ADRVVVLS 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
601-781 |
1.33e-18 |
|
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: 86.43 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 601 FRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD---LLMCGYPWIQNASVRDNIIF-GS---- 672
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssLLGLGGGFNPELTGRENIYLnGRllgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 673 --PFNKEKYDEVVRVCSLKADLDiLPAGdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSrvgkHIMD 750
Cdd:cd03220 115 srKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDA----AFQE 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 398366407 751 EC---LTGMLAN-KTRILATHQLSLIER-ASRVIVL 781
Cdd:cd03220 180 KCqrrLRELLKQgKTVILVSHDPSSIKRlCDRALVL 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1229-1453 |
1.40e-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: 86.62 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISqlGLFDLRRKLAIIPQDPVLF-RGTIRKN 1307
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 LDpfnertddelwdalvRGGAIAKDDLPEVKlQKPDEngTHGKMHKFHLdqaVEEEGSNFSLGERQLLALTRALVRQSKI 1387
Cdd:cd03299 92 IA---------------YGLKKRKVDKKEIE-RKVLE--IAEMLGIDHL---LNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1388 LILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAHRLKTI-VNYDRILVLEKGEVAEFDTPWTLFS 1453
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREelkKIRKEFG-VTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
604-787 |
1.40e-18 |
|
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: 84.79 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLmcgypwiqnasvrdniifgspfNKEKYDEVV 683
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL----------------------ASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 684 RVCSlkadldILP----AGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVD----SRVGKHIMDECLT 754
Cdd:cd03214 73 RKIA------YVPqaleLLGLAHLADRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIELLELLRRLARE 146
|
170 180 190
....*....|....*....|....*....|....
gi 398366407 755 GmlaNKTRILATHQLSLIER-ASRVIVLGtDGQV 787
Cdd:cd03214 147 R---GKTVVMVLHDLNLAARyADRVILLK-DGRI 176
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
941-1470 |
1.61e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 92.35 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 941 FVFAAFIFMNGQFTILCAMGIMASKW---LNLRA--VKRILHTPMSYIDTT----PLGRILNRFTKDTDSLdNELTESLR 1011
Cdd:PLN03232 341 YVYAFLIFFGVTFGVLCESQYFQNVGrvgFRLRStlVAAIFHKSLRLTHEArknfASGKVTNMITTDANAL-QQIAEQLH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1012 -LMTSQFANIVGvcvMCIVYLPWFAIAIPFLLVIFVLIAdhYQS-SGREIKRL--EAVQRSFVYNNL-NEVLGGMDTIKA 1086
Cdd:PLN03232 420 gLWSAPFRIIVS---MVLLYQQLGVASLFGSLILFLLIP--LQTlIVRKMRKLtkEGLQWTDKRVGIiNEILASMDTVKC 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1087 YRSQERFLAKSDFLINK---MNEAGYLVVVLQRWV--GIFLDMVAIAFALIITL---LCVTRAFpiSAASVGVLLTYVLQ 1158
Cdd:PLN03232 495 YAWEKSFESRIQGIRNEelsWFRKAQLLSAFNSFIlnSIPVVVTLVSFGVFVLLggdLTPARAF--TSLSLFAVLRSPLN 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1159 -LPGLLNTILRA---MTQTENDMNSAERLVtyATELPLEasyrkpemtppeswPSMGEIIFENVDFAYRPGLP-IVLKNL 1233
Cdd:PLN03232 573 mLPNLLSQVVNAnvsLQRIEELLLSEERIL--AQNPPLQ--------------PGAPAISIKNGYFSWDSKTSkPTLSDI 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1234 NLNIKSGEKIGICGRTGAGKSTIMSALyrLNELTAgkilidnvdiSQLGLFDLRRKLAIIPQDPVLFRGTIRKNLdPFNE 1313
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSH----------AETSSVVIRGSVAYVPQVSWIFNATVRENI-LFGS 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1314 RTDDELWDALVRGGAIAKD-DLpevklqKPDENGTHgkmhkfhldqaVEEEGSNFSLGERQLLALTRALVRQSKILILDE 1392
Cdd:PLN03232 704 DFESERYWRAIDVTALQHDlDL------LPGRDLTE-----------IGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1393 ATSSVDYETDGKI-QTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTpWTLFSQEDSIFRSMCSRSGIVE 1470
Cdd:PLN03232 767 PLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGT-FAELSKSGSLFKKLMENAGKMD 844
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1213-1439 |
1.74e-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: 84.13 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAyRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDnvdisqlglfdLRRKLAI 1292
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-----------EGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRGTIRknldpfnertdDEL---WDalvrggaiakddlpevklqkpdengthgkmhkfhldqaveeegSNFSL 1369
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypWD-------------------------------------------DVLSG 94
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFgdCTILCIAHRlKTIVNY-DRILVLEK 1439
Cdd:cd03223 95 GEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR-PSLWKFhDRVLDLDG 162
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
602-823 |
1.83e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.18 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG----DLLMCGY----------PWIQNASVRDN 667
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirTVTRASLrrniavvfqdAGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGSPFNKEkyDEVVRVCSLKADLDIL---PAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDS-- 742
Cdd:PRK13657 429 IRVGRPDATD--EEMRAAAERAQAHDFIerkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVet 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 743 --RVgKHIMDECLTGmlaNKTRILAtHQLSLIERASRVIVLGTDGQVDIGTVDELKARNQTLINLLQFSSQNSEKEDEEQ 820
Cdd:PRK13657 507 eaKV-KAALDELMKG---RTTFIIA-HRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQEDERRKQ 581
|
...
gi 398366407 821 EAV 823
Cdd:PRK13657 582 PAA 584
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
602-769 |
3.89e-18 |
|
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: 89.73 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL-----------MCGYPwiQNA-----SVR 665
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVssldqdevrrrVSVCA--QDAhlfdtTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 DNIIFGSP-FNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRV 744
Cdd:TIGR02868 427 ENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
170 180
....*....|....*....|....*
gi 398366407 745 GKHIMDECLTGMlANKTRILATHQL 769
Cdd:TIGR02868 507 ADELLEDLLAAL-SGRTVVLITHHL 530
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1210-1458 |
4.00e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEII-FENVDFAYRPGLP-IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLR 1287
Cdd:PRK13650 1 MSNIIeVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQDPvlfrgtirknldpfnertDDELWdalvrgGAIAKDDlpeVKLQKPDENGTHGKMhKFHLDQAVE------ 1361
Cdd:PRK13650 81 HKIGMVFQNP------------------DNQFV------GATVEDD---VAFGLENKGIPHEEM-KERVNEALElvgmqd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1362 ---EEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYEtdGK---IQT--RIVEEFGdCTILCIAHRLKTIVNYDR 1433
Cdd:PRK13650 133 fkeREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE--GRlelIKTikGIRDDYQ-MTVISITHDLDEVALSDR 209
|
250 260
....*....|....*....|....*
gi 398366407 1434 ILVLEKGEVAEFDTPWTLFSQEDSI 1458
Cdd:PRK13650 210 VLVMKNGQVESTSTPRELFSRGNDL 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
595-787 |
4.22e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 84.65 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 595 DLEKtSFRGFK-DLNFDIKkGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL------MC--------GYPWI 659
Cdd:cd03297 5 DIEK-RLPDFTlKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINlppqqrkiGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 660 QNA-----SVRDNIIFGSPFNKEKYDEVvRVCSLKADLDIlpagdmTEIGERGI-TLSGGQKARINLARSVYKKKDIYLF 733
Cdd:cd03297 83 QYAlfphlNVRENLAFGLKRKRNREDRI-SVDELLDLLGL------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 734 DDVLSAVDSRVGKHIMDEcLTGMLA--NKTRILATHQLSLIERASRVIVLGTDGQV 787
Cdd:cd03297 156 DEPFSALDRALRLQLLPE-LKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
594-787 |
4.39e-18 |
|
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: 83.22 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGdllmcGYPWIQNASVRDNI--I 669
Cdd:cd03230 4 RNLSKRygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-----KDIKKEPEEVKRRIgyL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 670 FGSPFNkekYDevvrvcslkadldilpagDMTeiGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:cd03230 79 PEEPSL---YE------------------NLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 398366407 750 DECLTGMLANKTRILATHQLSLIER-ASRVIVLGtDGQV 787
Cdd:cd03230 136 ELLRELKKEGKTILLSSHILEEAERlCDRVAILN-NGRI 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1213-1444 |
5.41e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.16 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIV--LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQL---GLFDLR 1287
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQ-----------DPVLF--------RGTIRKNLdpfnertdDELWDaLVrGGAIAKDDLPevklqkpdength 1348
Cdd:PRK11153 82 RQIGMIFQhfnllssrtvfDNVALplelagtpKAEIKARV--------TELLE-LV-GLSDKADRYP------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1349 gkmhkfhldqaveeegSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAHRL 1425
Cdd:PRK11153 139 ----------------AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEllkDINRELG-LTIVLITHEM 201
|
250 260
....*....|....*....|..
gi 398366407 1426 ---KTIVnyDRILVLEKGEVAE 1444
Cdd:PRK11153 202 dvvKRIC--DRVAVIDAGRLVE 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1229-1443 |
5.59e-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: 82.48 E-value: 5.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD-LRRKLAIIPQdpvlfrgtirkn 1307
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 ldpfnertddelwdalvrggaiakddlpevklqkpdengthgkmhkfhldqaveeegsnFSLGERQLLALTRALVRQSKI 1387
Cdd:cd03216 83 -----------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 1388 LILDEATSSVdyeTDGKIQT--RIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGEVA 1443
Cdd:cd03216 104 LILDEPTAAL---TPAEVERlfKVIRRLRAqgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1229-1447 |
5.82e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD-LRRKLAIIPQDPVLFRG-TIRK 1306
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1307 NLdpF--NERTddelwdalvRGGAIakddlpevklqkpDENGTHGK----MHKFHLDQAVEEEGSNFSLGERQLLALTRA 1380
Cdd:COG1129 99 NI--FlgREPR---------RGGLI-------------DWRAMRRRarelLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1381 LVRQSKILILDEATSSVdyeTDGKIQT--RIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGE-VAEFDT 1447
Cdd:COG1129 155 LSRDARVLILDEPTASL---TEREVERlfRIIRRLKAqgVAIIYISHRLDEVFEIaDRVTVLRDGRlVGTGPV 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
594-787 |
7.68e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.32 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT------SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCG----------- 655
Cdd:COG1136 8 RNLTKSygtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqDISSLSerelarlrrrh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 656 -------YPWIQNASVRDNI-----IFGSPFN--KEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLA 721
Cdd:COG1136 88 igfvfqfFNLLPELTALENValpllLAGVSRKerRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 722 RSVYKKKDIYLFDDVLSAVDSRVGKHIMdECLTGMLA--NKTRILATHQLSLIERASRVIVLgTDGQV 787
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVL-ELLRELNRelGTTIVMVTHDPELAARADRVIRL-RDGRI 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
581-798 |
7.88e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 89.04 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 581 KRLDNMLKDRDGPED------------LEKTSFR--G-----FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKT 641
Cdd:COG4618 306 RRLNELLAAVPAEPErmplprpkgrlsVENLTVVppGskrpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 642 DGKVEVNG--------DLL--MCGY-PwiQN-----ASVRDNIifgSPFNKEKYDEVVRVCSLkADLD--I--LPAGDMT 701
Cdd:COG4618 386 AGSVRLDGadlsqwdrEELgrHIGYlP--QDvelfdGTIAENI---ARFGDADPEKVVAAAKL-AGVHemIlrLPDGYDT 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 702 EIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvGkhimDECLTGMLAN-----KTRILATHQLSLIERAS 776
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE-G----EAALAAAIRAlkargATVVVITHRPSLLAAVD 534
|
250 260
....*....|....*....|...
gi 398366407 777 RVIVLGtDGQVD-IGTVDELKAR 798
Cdd:COG4618 535 KLLVLR-DGRVQaFGPRDEVLAR 556
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1230-1448 |
9.23e-18 |
|
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: 88.59 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNElTAGKILIDNVDISQLG---LFDLRRKLAIIPQDPvlF-----R 1301
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FgslspR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1302 GTI-----------RKNLDPfNERtddelwDALVRggaiakDDLPEVKLqKPDengthgKMHKF-HldqaveeEgsnFSL 1369
Cdd:COG4172 379 MTVgqiiaeglrvhGPGLSA-AER------RARVA------EALEEVGL-DPA------ARHRYpH-------E---FSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSVDYetdgKIQTRIVE-------EFGdCTILCIAHRLKtIVNY--DRILVLEKG 1440
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDV----SVQAQILDllrdlqrEHG-LAYLFISHDLA-VVRAlaHRVMVMKDG 502
|
250
....*....|....*
gi 398366407 1441 EVAE-------FDTP 1448
Cdd:COG4172 503 KVVEqgpteqvFDAP 517
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
216-488 |
1.05e-17 |
|
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: 85.34 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 216 LANCTSGFN-PMITKRLIEFVEEKAIFHSMHVNKGIGYAIGACLmmfvNGLTFNHFFHTSQLTGVQAKSILTKAAMKKMF 294
Cdd:cd18559 7 LVLCNHVFSgPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAIL----QGITVFQYSMAVSIGGIFASRAVHLDLYHKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 295 NASNYARHCFPNGKVTSFVTTDLARI-EFALSFQPFLAGfPAILAICIVLLIVNLGPIALVGIGIFFGGFFISLFAFKLI 373
Cdd:cd18559 83 RSPISFFERTPSGELVNLFSKDLDRVdSMAPQVIKMWMG-PLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 374 LGFRIAANIFTDARVTMMREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLSRNFLIAMAMSLPSIASLVTFLA 453
Cdd:cd18559 162 RQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFA 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 398366407 454 MYKVNKGGRQPG-NIFASLSLFQVLSLQMFFLPIAI 488
Cdd:cd18559 242 YVSRHSLAGLVAlKVFYSLALTTYLNWPLNMSPEVI 277
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
930-1186 |
1.33e-17 |
|
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: 85.62 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 930 PPSFYMGLYSFFVFAAFIFMNGQFT--ILCAMGIMASKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELT 1007
Cdd:cd18600 66 FTSSYYVFYIYVGVADSLLAMGFFRglPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1008 ESLRLMTSQFANIVGVCVMCIVYLPWFAIAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAY 1087
Cdd:cd18600 146 LTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1088 RSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMVAIAFALIITLLCV-TRAFpiSAASVGVLLTYVLQLPGLLNTI 1166
Cdd:cd18600 226 GRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIgTTGD--GEGRVGIILTLAMNIMSTLQWA 303
|
250 260
....*....|....*....|
gi 398366407 1167 LRAMTQTENDMNSAERLVTY 1186
Cdd:cd18600 304 VNTSIDVDSLMRSVSRIFKF 323
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1201-1454 |
1.59e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.93 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1201 MTPPeswPSMGEIIFE--NVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNEL-----TAGKILI 1273
Cdd:COG1117 1 MTAP---ASTLEPKIEvrNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1274 DNVDI--SQLGLFDLRRKLAIIPQDPVLFRGTIRKN------LDPFNERTD-DE----------LWDalvrggaiakddl 1334
Cdd:COG1117 76 DGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNvayglrLHGIKSKSElDEiveeslrkaaLWD------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1335 pEVK--LQKPdengthgkmhkfhldqaveeeGSNFSLGERQLLALTRALVRQSKILILDEATSSVDyetdgKIQTRIVEE 1412
Cdd:COG1117 143 -EVKdrLKKS---------------------ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD-----PISTAKIEE 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1413 F-----GDCTILCIAH------RLKtivnyDRILVLEKGEVAEFDTPWTLFSQ 1454
Cdd:COG1117 196 LilelkKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPTEQIFTN 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1212-1458 |
1.67e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 84.69 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1212 EIIFENVDFAYRPGLP---IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDIS----QLGLF 1284
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1285 DLRRKLAIIPQDP--VLFRGTIRKNL--DPFNERTDDElwDALVRggaiAKDDLPEVKLqkPDEngthgkmhkfHLDQav 1360
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETVEKDIcfGPMNFGVSEE--DAKQK----AREMIELVGL--PEE----------LLAR-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1361 eeegSNFSL--GERQLLALTRALVRQSKILILDEATSSVdyetDGKIQTRIVEEF------GDCTILCIAHRLKTIVNY- 1431
Cdd:PRK13634 142 ----SPFELsgGQMRRVAIAGVLAMEPEVLVLDEPTAGL----DPKGRKEMMEMFyklhkeKGLTTVLVTHSMEDAARYa 213
|
250 260
....*....|....*....|....*..
gi 398366407 1432 DRILVLEKGEVAEFDTPWTLFSQEDSI 1458
Cdd:PRK13634 214 DQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1209-1454 |
1.82e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.92 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1209 SMGEIIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISqlglfDL-- 1286
Cdd:COG3842 2 AMPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1287 -RRKLAIIPQDPVLF-------------------RGTIRknldpfnERTDDELwdALVRggaiakddLPEVKLQKPDEng 1346
Cdd:COG3842 75 eKRNVGMVFQDYALFphltvaenvafglrmrgvpKAEIR-------ARVAELL--ELVG--------LEGLADRYPHQ-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1347 thgkmhkfhLdqaveeegsnfSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAH 1423
Cdd:COG3842 136 ---------L-----------SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREelrRLQRELG-ITFIYVTH 194
|
250 260 270
....*....|....*....|....*....|....*..
gi 398366407 1424 ------RLKtivnyDRILVLEKGEVAEFDTPWTLFSQ 1454
Cdd:COG3842 195 dqeealALA-----DRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
605-799 |
2.05e-17 |
|
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: 87.95 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DL--------------------LMcgypwiqNAS 663
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqDIrdvtqaslraaigivpqdtvLF-------NDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 664 VRDNIIFGSPFNKEkyDEVVRVCSLkADLD--I--LPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSA 739
Cdd:COG5265 448 IAYNIAYGRPDASE--EEVEAAARA-AQIHdfIesLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 740 VDSRVGKHIMDEcLTGMLANKTRILATHQLSLIERASRVIVLGtDGQ-VDIGTVDELKARN 799
Cdd:COG5265 525 LDSRTERAIQAA-LREVARGRTTLVIAHRLSTIVDADEILVLE-AGRiVERGTHAELLAQG 583
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
605-781 |
2.31e-17 |
|
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: 81.46 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPWIQ-----------------NASVRDN 667
Cdd:cd03229 17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplrrrigmvfqdfalfpHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGspfnkekydevvrvcslkadldilpagdmteigergitLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKH 747
Cdd:cd03229 97 IALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 398366407 748 IMDEcLTGMLAN--KTRILATHQLSLIER-ASRVIVL 781
Cdd:cd03229 139 VRAL-LKSLQAQlgITVVLVTHDLDEAARlADRVVVL 174
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1210-1455 |
3.05e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEIIFENVDFAYRpGLPIVlKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD-LRR 1288
Cdd:PRK10895 1 MATLTAKNLAKAYK-GRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1289 KLAIIPQDPVLFRGTirknldpfnertddELWDALVRGGAIAKDDLPEVKLQKPDEngthgKMHKFHLDQAVEEEGSNFS 1368
Cdd:PRK10895 79 GIGYLPQEASIFRRL--------------SVYDNLMAVLQIRDDLSAEQREDRANE-----LMEEFHIEHLRDSMGQSLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1369 LGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQtRIVEEFGD--CTILCIAHRLK-TIVNYDRILVLEKGEVAEF 1445
Cdd:PRK10895 140 GGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK-RIIEHLRDsgLGVLITDHNVReTLAVCERAYIVSQGHLIAH 218
|
250
....*....|
gi 398366407 1446 DTPWTLFSQE 1455
Cdd:PRK10895 219 GTPTEILQDE 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1229-1443 |
3.19e-17 |
|
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: 82.03 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQlGLFDLRRKLAIIPQDPVLF-RGTIRKN 1307
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYdRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 LDPFnertddelwdALVRG--GAIAKDDLPEVklqkpdengthgkMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQS 1385
Cdd:cd03266 99 LEYF----------AGLYGlkGDELTARLEEL-------------ADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1386 KILILDEATSSVDYetdgkIQTRIVEEF------GDCTILCIAHRLKTIVNY-DRILVLEKGEVA 1443
Cdd:cd03266 156 PVLLLDEPTTGLDV-----MATRALREFirqlraLGKCILFSTHIMQEVERLcDRVVVLHRGRVV 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1213-1448 |
4.26e-17 |
|
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: 81.78 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQlGLFDLRRKLAI 1292
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRG-TIRKNLdpfnertddELWdALVRGgaIAKDDLPEVKLQKPDENGTHGKMHKfhldqaveeEGSNFSLGE 1371
Cdd:cd03263 80 CPQFDALFDElTVREHL---------RFY-ARLKG--LPKSEIKEEVELLLRVLGLTDKANK---------RARTLSGGM 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTP 1448
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSP 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1229-1442 |
5.12e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 81.42 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG--LFDLRRKLAIIPQDPVLF-RGTIR 1305
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKknINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1306 KNLdpfnerTDDELWdalVRGgaIAKDDLPEVKLQKPDENGTHGKMHKFhldqaveeeGSNFSLGERQLLALTRALVRQS 1385
Cdd:cd03262 95 ENI------TLAPIK---VKG--MSKAEAEERALELLEKVGLADKADAY---------PAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1386 KILILDEATSSVDYETDG---KIQTRIVEEfgDCTILCIAHRL---KTIVnyDRILVLEKGEV 1442
Cdd:cd03262 155 KVMLFDEPTSALDPELVGevlDVMKDLAEE--GMTMVVVTHEMgfaREVA--DRVIFMDDGRI 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1216-1442 |
8.27e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.06 E-value: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYRPGLP---IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:COG1101 5 KNLSKTFNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVL---FRGTIRKNLdpfnertddELwdALVRGG------AIAKDDLPEVK--LQKPD---ENgthgkmhkfHLDQ 1358
Cdd:COG1101 85 VFQDPMMgtaPSMTIEENL---------AL--AYRRGKrrglrrGLTKKRRELFRelLATLGlglEN---------RLDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1359 AVEeegsNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAHRLKTIVNY-DRI 1434
Cdd:COG1101 145 KVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLElteKIVEENN-LTTLMVTHNMEQALDYgNRL 219
|
....*...
gi 398366407 1435 LVLEKGEV 1442
Cdd:COG1101 220 IMMHEGRI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
594-795 |
1.07e-16 |
|
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: 81.23 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD-------------LLMCGYPW 658
Cdd:cd03296 6 RNVSKRfgDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernvgFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 659 IQNASVRDNIIFG-----------SPFNKEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKK 727
Cdd:cd03296 86 FRHMTVFDNVAFGlrvkprserppEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 728 KDIYLFDDVLSAVDSRVGKH-------IMDEcltgmlANKTRILATH-QLSLIERASRVIVLgTDGQVD-IGTVDEL 795
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKElrrwlrrLHDE------LHVTTVFVTHdQEEALEVADRVVVM-NKGRIEqVGTPDEV 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1229-1455 |
1.10e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALyrLNELTA--GKILIDNVDISQLGLFDLRRKLAIIPQDPVL-Frgtir 1305
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL--SGELSPdsGEVRLNGRPLADWSPAELARRRAVLPQHSSLsF----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1306 knldPFNERtddelwdALVRGGAIakddlPEVKLQKPDENgthgkmhkfHLDQAVEE------EGSNF---SLGERQLLA 1376
Cdd:PRK13548 90 ----PFTVE-------EVVAMGRA-----PHGLSRAEDDA---------LVAAALAQvdlahlAGRDYpqlSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1377 LTRALVR------QSKILILDEATSSVDyetdgkIQ-----TRIVEEF---GDCTILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:PRK13548 145 LARVLAQlwepdgPPRWLLLDEPTSALD------LAhqhhvLRLARQLaheRGLAVIVVLHDLNLAARYaDRIVLLHQGR 218
|
250
....*....|....
gi 398366407 1442 VAEFDTPWTLFSQE 1455
Cdd:PRK13548 219 LVADGTPAEVLTPE 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
594-795 |
1.36e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.20 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDL-------------------L 652
Cdd:COG3839 7 ENVSKSygGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdlppkdrniamvfqsyaL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 653 mcgYPwiqNASVRDNIIFGSPFNK-------EKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVY 725
Cdd:COG3839 87 ---YP---HMTVYENIAFPLKLRKvpkaeidRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 726 KKKDIYLFDDVLSAVD--SRVgkhIMDECLTGMLA--NKTRILATH-Q---LSLierASRVIVLgTDGQV-DIGTVDEL 795
Cdd:COG3839 150 REPKVFLLDEPLSNLDakLRV---EMRAEIKRLHRrlGTTTIYVTHdQveaMTL---ADRIAVM-NDGRIqQVGTPEEL 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1213-1448 |
1.39e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 80.79 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---LFDLRRK 1289
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAiipqdpVLFRG-------TIRKNLD-PFNERTDdeLWDALVRggAIAKDDLPEVKLQkpdenGTHGKMhkfhldqave 1361
Cdd:COG1127 84 IG------MLFQGgalfdslTVFENVAfPLREHTD--LSEAEIR--ELVLEKLELVGLP-----GAADKM---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1362 eeGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAHRLKTIVNY-DRILVL 1437
Cdd:COG1127 139 --PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDElirELRDELG-LTSVVVTHDLDSAFAIaDRVAVL 215
|
250
....*....|.
gi 398366407 1438 EKGEVAEFDTP 1448
Cdd:COG1127 216 ADGKIIAEGTP 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1213-1456 |
3.11e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.03 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLP---IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDI----SQLGLFD 1285
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 LRRKLAIIPQDP--VLFRGTIRKNLD--PFN-ERTDDELWDALVRGgaIAKDDLPEVKLQKpdengthgkmhkfhldqav 1360
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPKNfGFSEDEAKEKALKW--LKKVGLSEDLISK------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1361 eeegSNFSL--GERQLLALTRALVRQSKILILDEATSSVDYETdgkiQTRIVEEFGDC-----TILCIAHRLKTIVNY-D 1432
Cdd:PRK13641 142 ----SPFELsgGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEYaD 213
|
250 260
....*....|....*....|....
gi 398366407 1433 RILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:PRK13641 214 DVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
604-787 |
5.46e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.56 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DL-----------------------LmcgypwI 659
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqDLsrlkrreipylrrrigvvfqdfrL------L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 660 QNASVRDNIIFG---SPFNKEKYDEVVRvcslkadlDILpagDMTEIGERG----ITLSGGQKARINLARSVYKKKDIYL 732
Cdd:COG2884 92 PDRTVYENVALPlrvTGKSRKEIRRRVR--------EVL---DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 733 FDDVLSAVDSRVGKHIMDecltgML-----ANKTRILATHQLSLIERA-SRVIVLgTDGQV 787
Cdd:COG2884 161 ADEPTGNLDPETSWEIME-----LLeeinrRGTTVLIATHDLELVDRMpKRVLEL-EDGRL 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1229-1443 |
5.53e-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: 77.98 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSAL--YRLNELTAGKILIDNVDISqlgLFDLRRKLAIIPQDPVLF-RGTIR 1305
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHpTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1306 KNLDpFNertddelwdALVRGgaiakddlpevklqkpdengthgkmhkfhldqaveeegsnFSLGERQLLALTRALVRQS 1385
Cdd:cd03213 101 ETLM-FA---------AKLRG----------------------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 1386 KILILDEATSSVDYETDGKI-QTRIVEEFGDCTILCIAHRLKTIV--NYDRILVLEKGEVA 1443
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVmSLLRRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
605-796 |
6.06e-16 |
|
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: 78.32 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLL--------MCGY-------PWiqNASVRDNI 668
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySIRtdrkaarqSLGYcpqfdalFD--ELTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 669 IFGSPF---NKEKYDEVV----RVCSLKADLDilpagdmTEIGergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVD 741
Cdd:cd03263 97 RFYARLkglPKSEIKEEVelllRVLGLTDKAN-------KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 742 SRvGKHIMDECLTGMLANKTRILATHQLSLIER-ASRVIVLgTDGQV-DIGTVDELK 796
Cdd:cd03263 166 PA-SRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIM-SDGKLrCIGSPQELK 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
940-1183 |
7.39e-16 |
|
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: 79.90 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 940 FFVFAAFIFMNGQFTILCAMGIMaskwLNLR--AVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQF 1017
Cdd:cd07346 49 ALLRALLSYLRRYLAARLGQRVV----FDLRrdLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1018 ANIVGVCVMCIVYLPWFAIAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKS 1097
Cdd:cd07346 125 LTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1098 DFLINKMNEAGYLVVVLQRWVGIFLDMV-AIAFALII---------------TLLcvtrAFpisAASVGVLLTYVLQLPG 1161
Cdd:cd07346 205 REANRDLRDANLRAARLSALFSPLIGLLtALGTALVLlyggylvlqgsltigELV----AF---LAYLGMLFGPIQRLAN 277
|
250 260
....*....|....*....|..
gi 398366407 1162 LLNTILRAMTqtendmnSAERL 1183
Cdd:cd07346 278 LYNQLQQALA-------SLERI 292
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1229-1456 |
7.89e-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: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKST---IMSALYRLNEltaGKILIDNVDISQLGLFDlRRKLAII--PQDPVLFRG- 1302
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTtfyMIVGLVKPDS---GKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1303 TIRKNLDPFNERTDDElwdalvrgGAIAKDDLPEVklqkpdengthgkMHKFHLDQAVEEEGSNFSLGERQLLALTRALV 1382
Cdd:cd03218 91 TVEENILAVLEIRGLS--------KKEREEKLEEL-------------LEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 1383 RQSKILILDEATSSVDYETDGKIQtRIVEEFGDCTI--LCIAHRLK-TIVNYDRILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQ-KIIKILKDRGIgvLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1213-1459 |
8.61e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 78.43 E-value: 8.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFdlRRKLAI 1292
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFrgtirKNLDpfnertddeLWDALVRGGAIAKDDLPEVKlQKPDEngthgKMHKFHLDQAVEEEGSNFSLGER 1372
Cdd:cd03300 77 VFQNYALF-----PHLT---------VFENIAFGLRLKKLPKAEIK-ERVAE-----ALDLVQLEGYANRKPSQLSGGQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1373 QLLALTRALVRQSKILILDEATSSVDYETDGKIQ---TRIVEEFGdCTILCIAH-RLKTIVNYDRILVLEKGEVAEFDTP 1448
Cdd:cd03300 137 QRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELG-ITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTP 215
|
250
....*....|.
gi 398366407 1449 WTLFSQEDSIF 1459
Cdd:cd03300 216 EEIYEEPANRF 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1210-1458 |
1.17e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.12 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEIIFENVDFAYR-PGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDN--VDISQLGLFDL 1286
Cdd:PRK13636 1 MEDYILKVEELNYNySDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1287 RRKLAIIPQDPvlfrgtirknldpfnertDDELWDALVRG----GAIAKdDLPEVKLQKPDENGthgkMHKFHLDQAVEE 1362
Cdd:PRK13636 81 RESVGMVFQDP------------------DNQLFSASVYQdvsfGAVNL-KLPEDEVRKRVDNA----LKRTGIEHLKDK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1363 EGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE--EFGDCTILCIAHRLKTIVNY-DRILVLEK 1439
Cdd:PRK13636 138 PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYcDNVFVMKE 217
|
250
....*....|....*....
gi 398366407 1440 GEVAEFDTPWTLFSQEDSI 1458
Cdd:PRK13636 218 GRVILQGNPKEVFAEKEML 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1213-1458 |
1.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.07 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTI---MSALYRLNELTAGKILIDNVDISQLGLFDLRRK 1289
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPvlfrgtirknldpfnertDDELWdalvrgGAIAKDDL---------PEVKLQKPdengTHGKMHKFHLDQAV 1360
Cdd:PRK13640 86 VGIVFQNP------------------DNQFV------GATVGDDVafglenravPRPEMIKI----VRDVLADVGMLDYI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1361 EEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE--EFGDCTILCIAHRLKTIVNYDRILVLE 1438
Cdd:PRK13640 138 DSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLD 217
|
250 260
....*....|....*....|
gi 398366407 1439 KGEVAEFDTPWTLFSQEDSI 1458
Cdd:PRK13640 218 DGKLLAQGSPVEIFSKVEML 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1213-1454 |
1.62e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.59 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPG----LPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG-LFDLR 1287
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQDPvlfrgtirknldpfnertDDELWDALVRGG-AIAKDDL---PEVKLQKPDENGTHGKMHKF-----HLdq 1358
Cdd:PRK13633 85 NKAGMVFQNP------------------DNQIVATIVEEDvAFGPENLgipPEEIRERVDESLKKVGMYEYrrhapHL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1359 aveeegsnFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE---EFGdCTILCIAHRLKTIVNYDRIL 1435
Cdd:PRK13633 145 --------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnkKYG-ITIILITHYMEEAVEADRII 215
|
250
....*....|....*....
gi 398366407 1436 VLEKGEVAEFDTPWTLFSQ 1454
Cdd:PRK13633 216 VMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1217-1443 |
1.90e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 76.95 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1217 NVDFAYRpglpivLKNLNLNIK---SGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNV--DISQLGLF--DLRRK 1289
Cdd:cd03297 3 CVDIEKR------LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINlpPQQRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVLF-RGTIRKNLdpfnertddelwdalVRGgaiAKDDLPEVKLQKPDEngthgKMHKFHLDQAVEEEGSNFS 1368
Cdd:cd03297 77 IGLVFQQYALFpHLNVRENL---------------AFG---LKRKRNREDRISVDE-----LLDLLGLDHLLNRYPAQLS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1369 LGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQ---TRIVEEFGDCTILcIAHRLKTIVNY-DRILVLEKGEVA 1443
Cdd:cd03297 134 GGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLpelKQIKKNLNIPVIF-VTHDLSEAEYLaDRIVVMEDGRLQ 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1212-1455 |
2.12e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1212 EIIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLA 1291
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1292 IIPQDPVLFRG-TIRKNL----DPFNertddELWdalvrgGAIAKDDlpEVKLQKpdengthgKMHKFHLDQAVEEEGSN 1366
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVaygrSPWL-----SLW------GRLSAED--NARVNQ--------AMEQTRINHLADRRLTD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1367 FSLGERQLLALTRALVRQSKILILDEATSSVD-------------YETDGKiqtriveefgdcTILCIAHRLKTIVNY-D 1432
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqvelmrlmreLNTQGK------------TVVTVLHDLNQASRYcD 206
|
250 260
....*....|....*....|...
gi 398366407 1433 RILVLEKGEVAEFDTPWTLFSQE 1455
Cdd:PRK11231 207 HLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1213-1457 |
2.60e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.10 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrPGLPivlKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDlrRKLAI 1292
Cdd:COG3840 2 LRLDDLTYRY-GDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRG-TIRKN----LDPfNERTDDELWDALVRggAIAKDDLPEVKLQKPDEngthgkmhkfhldqaveeegsnF 1367
Cdd:COG3840 76 LFQENNLFPHlTVAQNiglgLRP-GLKLTAEQRAQVEQ--ALERVGLAGLLDRLPGQ----------------------L 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1368 SLGERQLLALTRALVRQSKILILDEATSSVD----YETDGKIQTrIVEEFGdCTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:COG3840 131 SGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDE-LCRERG-LTVLMVTHDPEDAARIaDRVLLVADGRI 208
|
250
....*....|....*
gi 398366407 1443 AEFDTPWTLFSQEDS 1457
Cdd:COG3840 209 AADGPTAALLDGEPP 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
594-795 |
2.63e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.04 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLM---------CGYPWiQNA 662
Cdd:COG1118 6 RNISKRfgSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnlpprerrVGFVF-QHY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 663 ------SVRDNIIFG---SPFNKEKYDEVVRvcSLkadLDILpagDMTEIGERGIT-LSGGQKARINLARSVYKKKDIYL 732
Cdd:COG1118 85 alfphmTVAENIAFGlrvRPPSKAEIRARVE--EL---LELV---QLEGLADRYPSqLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 733 FDDVLSAVDSRVGKHIMDEcLTGMLA--NKTRILATH-QLSLIERASRVIVLGtDGQVD-IGTVDEL 795
Cdd:COG1118 157 LDEPFGALDAKVRKELRRW-LRRLHDelGGTTVFVTHdQEEALELADRVVVMN-QGRIEqVGTPDEV 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1220-1440 |
3.30e-15 |
|
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: 76.22 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1220 FAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRK----LAIIPQ 1295
Cdd:cd03290 8 FSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1296 DPVLFRGTIRKNL---DPFNERTDDELWDALVRGGAIakDDLPevklqkpdengthgkmhkfHLDQA-VEEEGSNFSLGE 1371
Cdd:cd03290 87 KPWLLNATVEENItfgSPFNKQRYKAVTDACSLQPDI--DLLP-------------------FGDQTeIGERGINLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVD-YETDGKIQTRIVEEFGD--CTILCIAHRLKTIVNYDRILVLEKG 1440
Cdd:cd03290 146 RQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
595-846 |
3.87e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.36 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 595 DLEKTSFR-------GFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPW--------- 658
Cdd:PRK13635 7 RVEHISFRypdaatyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdvrrqvgmv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 659 IQN-------ASVRDNIIFGSPFNKEKYDEVVRvcSLKADLDILpagDMTEIGERG-ITLSGGQKARINLARSVYKKKDI 730
Cdd:PRK13635 87 FQNpdnqfvgATVQDDVAFGLENIGVPREEMVE--RVDQALRQV---GMEDFLNREpHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 731 YLFDDVLSAVDSRvGKHIMDECLTGMLANK--TRILATHQLSLIERASRVIVLgTDGQV-DIGTVDELKARNQTLINL-- 805
Cdd:PRK13635 162 IILDEATSMLDPR-GRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVM-NKGEIlEEGTPEEIFKSGHMLQEIgl 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 398366407 806 -LQFSSQNSEKEDEEQEAVVAGELGQlkyESEVKELTELKKK 846
Cdd:PRK13635 240 dVPFSVKLKELLKRNGILLPNTYLTM---ESLVDELWTLHSK 278
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1229-1444 |
4.76e-15 |
|
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: 76.32 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGlFDLRRKLAIIP--QDPVLFRG-TIR 1305
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1306 KNLD-PFNERTDDELWDALVRGgaiAKDDLPEvklqKPDENgthgkMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQ 1384
Cdd:cd03219 94 ENVMvAAQARTGSGLLLARARR---EEREARE----RAEEL-----LERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1385 SKILILDEATSSV-DYETD--GKIQTRIVEEfgDCTILCIAHRLKTIVNY-DRILVLEKGEV-AE 1444
Cdd:cd03219 162 PKLLLLDEPAAGLnPEETEelAELIRELRER--GITVLLVEHDMDVVMSLaDRVTVLDQGRViAE 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
600-751 |
4.78e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 76.12 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 600 SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-------------DLLMCGYPWIQNASVRD 666
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphkrpvNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 667 NIIFGSPFNKEKYDEVVRvcSLKADLDILpagDMTEIGERGIT-LSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVG 745
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKE--RVAEALDLV---QLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLR 166
|
....*.
gi 398366407 746 KHIMDE 751
Cdd:cd03300 167 KDMQLE 172
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
605-787 |
8.18e-15 |
|
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: 75.22 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGY-------------PWIQNASVRDNIif 670
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvDISKIGLhdlrsrisiipqdPVLFSGTIRSNL-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 gSPFNkEKYDE----VVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGK 746
Cdd:cd03244 99 -DPFG-EYSDEelwqALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 398366407 747 HIMdECLTGMLANKTRILATHQLSLIERASRVIVLGtDGQV 787
Cdd:cd03244 177 LIQ-KTIREAFKDCTVLTIAHRLDTIIDSDRILVLD-KGRV 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1219-1437 |
8.95e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.14 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1219 DFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPV 1298
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1299 LFRGTIRKNLD-PFNERTDDELWDALVRGgaIAKDDLPEVKLQKPdengthgkmhkfhldqaVEEegsnFSLGERQLLAL 1377
Cdd:PRK10247 92 LFGDTVYDNLIfPWQIRNQQPDPAIFLDD--LERFALPDTILTKN-----------------IAE----LSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1378 TRALVRQSKILILDEATSSVDYETDGK---IQTRIVEEFGdCTILCIAHRLKTIVNYDRILVL 1437
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNvneIIHRYVREQN-IAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1223-1448 |
9.38e-15 |
|
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: 76.14 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1223 RPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---LFDLRRK--------LA 1291
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1292 IIPQDPVL--------FRGTIRKNldpfNERTDDElwdalvrggAIAKDDLPEVKLQKPDEngthgkmhkfhldqaveee 1363
Cdd:cd03294 113 LLPHRTVLenvafgleVQGVPRAE----REERAAE---------ALELVGLEGWEHKYPDE------------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1364 gsnFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGDcTILCIAHRLKTIVNY-DRILVLEK 1439
Cdd:cd03294 161 ---LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDellRLQAELQK-TIVFITHDLDEALRLgDRIAIMKD 236
|
....*....
gi 398366407 1440 GEVAEFDTP 1448
Cdd:cd03294 237 GRLVQVGTP 245
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
594-787 |
1.08e-14 |
|
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: 74.85 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT------SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL------MCGYPW--I 659
Cdd:cd03257 5 KNLSVSfptgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrrLRKIRRkeI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 660 ----QNA--------SVRDNI-----IFGSPFNKEKYDEV-----VRVCSLKADLDILPAgdmteigergiTLSGGQKAR 717
Cdd:cd03257 85 qmvfQDPmsslnprmTIGEQIaeplrIHGKLSKKEARKEAvllllVGVGLPEEVLNRYPH-----------ELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 718 INLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDE--CLTGMLaNKTRILATHQLSLIER-ASRVIVLgTDGQV 787
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLlkKLQEEL-GLTLLFITHDLGVVAKiADRVAVM-YAGKI 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1229-1448 |
1.24e-14 |
|
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: 75.46 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDL-RRKLAIIPQDPVLFRG-TIRK 1306
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1307 NLD-PFNERTDDELWDALVRGGAIAKDDlPEVkLQKPDENgthgkMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQS 1385
Cdd:COG0411 99 NVLvAAHARLGRGLLAALLRLPRARREE-REA-RERAEEL-----LERVGLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1386 KILILDEATSSVDY-ETDGKIQT--RIVEEFGdCTILCIAHRLKTIVNY-DRILVLEKGEV-AEfDTP 1448
Cdd:COG0411 172 KLLLLDEPAAGLNPeETEELAELirRLRDERG-ITILLIEHDMDLVMGLaDRIVVLDFGRViAE-GTP 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1229-1442 |
1.36e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVL-----FRGT 1303
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfefdVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1304 IRKNLDPFNERTDDelWDalvrggaiakddlpevklqKPDENGTHGKMHKFHLDQAVEEEGSNFSLGERQLLALTRALVR 1383
Cdd:PRK09536 98 VEMGRTPHRSRFDT--WT-------------------ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1384 QSKILILDEATSSVDyeTDGKIQT-----RIVEEfgDCTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:PRK09536 157 ATPVLLLDEPTASLD--INHQVRTlelvrRLVDD--GKTAVAAIHDLDLAARYcDELVLLADGRV 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
604-787 |
1.52e-14 |
|
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: 73.12 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLmcgypwiqnASVRDNIifgspfnkEKYdevv 683
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV---------SDLEKAL--------SSL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 684 rVCSLKADLDILPAGDMTEIGERgitLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMdECLTGMLANKTRI 763
Cdd:cd03247 77 -ISVLNQRPYLFDTTLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFEVLKDKTLI 151
|
170 180
....*....|....*....|....
gi 398366407 764 LATHQLSLIERASRVIVLgTDGQV 787
Cdd:cd03247 152 WITHHLTGIEHMDKILFL-ENGKI 174
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1223-1448 |
1.69e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.38 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1223 RPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---LFDLRRK--------LA 1291
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1292 IIPQDPVLFRGTIRKNLD--PFNERTDDELwdalvrggaiakDDLPEVKLqkpdENGTHGkmhkfHLDQaveeegsnFSL 1369
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAgiNAEERREKAL------------DALRQVGL----ENYAHS-----YPDE--------LSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIV--EEFGDCTILCIAHRLKTIVNY-DRILVLEKGEVAEFD 1446
Cdd:PRK10070 168 GMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVklQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVG 247
|
..
gi 398366407 1447 TP 1448
Cdd:PRK10070 248 TP 249
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
606-787 |
1.98e-14 |
|
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: 73.98 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLmCGYP-------------------WIQNASVRD 666
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRgraipylrrkigvvfqdfrLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 667 NIIF-----GSPFN--KEKYDEVVRVCSLKADLDILPAGdmteigergitLSGGQKARINLARSVYKKKDIYLFDDVLSA 739
Cdd:cd03292 98 NVAFalevtGVPPReiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398366407 740 VDSRVGKHIMDECLTGMLANKTRILATHQLSLIERAS-RVIVLGtDGQV 787
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhRVIALE-RGKL 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
576-795 |
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 398366407 576 STNKAKRLDNMLKDRDGPEDLEKTS-FRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG----- 649
Cdd:cd03294 11 GKNPQKAFKLLAKGKSKEEILKKTGqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 650 ----DL----------------LMcgyPwiqNASVRDNIIFG-------SPFNKEKYDEVVRVCSLKADLDILPagdmte 702
Cdd:cd03294 91 msrkELrelrrkkismvfqsfaLL---P---HRTVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 703 iGErgitLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLT--GMLaNKTRILATHQLsliERASRV-- 778
Cdd:cd03294 159 -DE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAEL-QKTIVFITHDL---DEALRLgd 229
|
250
....*....|....*....
gi 398366407 779 -IVLGTDGQ-VDIGTVDEL 795
Cdd:cd03294 230 rIAIMKDGRlVQVGTPEEI 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1229-1398 |
2.88e-14 |
|
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: 73.62 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDN----VDISQLG---LFDLRRK--------LAII 1293
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQASpreILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1294 PQ--------DPVLFRGTIRKnldpfnertddelwDALVRGGAI-AKDDLPEvklqkpdengthgkmHKFHLDQAveeeg 1364
Cdd:COG4778 106 PRvsaldvvaEPLLERGVDRE--------------EARARARELlARLNLPE---------------RLWDLPPA----- 151
|
170 180 190
....*....|....*....|....*....|....
gi 398366407 1365 sNFSLGERQLLALTRALVRQSKILILDEATSSVD 1398
Cdd:COG4778 152 -TFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
934-1182 |
2.90e-14 |
|
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: 75.12 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 934 YMGLYSFFVFAAFIFMNGQFTILCAMGIMASKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLM 1013
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1014 TSQFANIVGVCVMcIVYLPW-----FAIAIPFLLVIFVLiadhYQSSGREIKRLEAVQRSFVYNNLNEVLGGMDTIKAYR 1088
Cdd:cd18544 123 IGDLLLLIGILIA-MFLLNWrlaliSLLVLPLLLLATYL----FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1089 SQERFLAKsdflINKMNEAgYLVVVLQ--RWVGIFLDMV----AIAFALIITLLcvTRAFPISAASVGVLLTYVL----- 1157
Cdd:cd18544 198 REKREFEE----FDEINQE-YRKANLKsiKLFALFRPLVellsSLALALVLWYG--GGQVLSGAVTLGVLYAFIQyiqrf 270
|
250 260 270
....*....|....*....|....*....|
gi 398366407 1158 -----QLPGLLNTILRAMTqtendmnSAER 1182
Cdd:cd18544 271 frpirDLAEKFNILQSAMA-------SAER 293
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
604-786 |
2.91e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.28 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMR---KTDGKVEVNG-------------------DLLmcgYPwiqN 661
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGrrltalpaeqrrigilfqdDLL---FP---H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 662 ASVRDNIIFGSP--FNKEKYDEVVrvcslkadLDILPAGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLS 738
Cdd:COG4136 91 LSVGENLAFALPptIGRAQRRARV--------EQALEEAGLAGFADRDPaTLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398366407 739 AVDSRVGKHIMDECLTgMLanKTR----ILATHQLSLIERASRVIVLGTDGQ 786
Cdd:COG4136 163 KLDAALRAQFREFVFE-QI--RQRgipaLLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1217-1455 |
3.23e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1217 NVDFAYRPGL-------PIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNElTAGKILIDNVDISQLG---LFDL 1286
Cdd:PRK15134 282 QVAFPIRKGIlkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1287 RRKLAIIPQDPvlfrgtiRKNLDPfneRTDDElwdalvrggAIAKDDLpevKLQKPDENGTHGK------MHKFHLDQAV 1360
Cdd:PRK15134 361 RHRIQVVFQDP-------NSSLNP---RLNVL---------QIIEEGL---RVHQPTLSAAQREqqviavMEEVGLDPET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1361 EEE-GSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT--RIVEEFGDCTILCIAHRLKTIVNY-DRILV 1436
Cdd:PRK15134 419 RHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILAllKSLQQKHQLAYLFISHDLHVVRALcHQVIV 498
|
250 260
....*....|....*....|....*.
gi 398366407 1437 LEKGEVAE-------FDTPWTLFSQE 1455
Cdd:PRK15134 499 LRQGEVVEqgdcervFAAPQQEYTRQ 524
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1212-1459 |
3.61e-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: 73.91 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1212 EIIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDlrRKLA 1291
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1292 IIPQDPVLFRG-TIRKNLdPFNERtddelwdalVRGGAiakddlpevklQKPDENGTHGKMHKF----HLDQAVEEEGSN 1366
Cdd:cd03296 78 FVFQHYALFRHmTVFDNV-AFGLR---------VKPRS-----------ERPPEAEIRAKVHELlklvQLDWLADRYPAQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1367 FSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVA 1443
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRwlrRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
250
....*....|....*.
gi 398366407 1444 EFDTPWTLFSQEDSIF 1459
Cdd:cd03296 217 QVGTPDEVYDHPASPF 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1213-1445 |
5.10e-14 |
|
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: 72.61 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGlpIVLKNLNLNIKSGeKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfDLRRKLAI 1292
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPvlfrgTIRKNLdpfnerTDDELWDALVRGGAIAKDDLPEVKLQkpdengthgKMHKFHLDQAVEEEGSNFSLGER 1372
Cdd:cd03264 77 LPQEF-----GVYPNF------TVREFLDYIAWLKGIPSKEVKARVDE---------VLELVNLGDRAKKKIGSLSGGMR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1373 QLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHrlktIV-----NYDRILVLEKGEVAEF 1445
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH----IVedvesLCNQVAVLNKGKLVFE 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
605-882 |
5.46e-14 |
|
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: 76.48 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKT---DGKVEVNGDLLMCGYPWIQNASVRdnIIFGSPFN------ 675
Cdd:COG1123 23 DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIG--MVFQDPMTqlnpvt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 676 -KEKYDEVVRVCSLKAD------LDILPAGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKH 747
Cdd:COG1123 101 vGDQIAEALENLGLSRAeararvLELLEAVGLERRLDRYPhQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 748 IMDecLTGMLA---NKTRILATHQLSLI-ERASRVIVLGTDGQVDIGTVDELKARNQTL--INLLQFSSQNSEKEDEEQE 821
Cdd:COG1123 181 ILD--LLRELQrerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQALaaVPRLGAARGRAAPAAAAAE 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 822 AVVagelgqlkyesEVKELTelkkkatemsqtansgkiVADGHTSSKEERAVNSISLKIYR 882
Cdd:COG1123 259 PLL-----------EVRNLS------------------KRYPVRGKGGVRAVDDVSLTLRR 290
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
594-787 |
5.54e-14 |
|
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: 73.37 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT---SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD------------------LL 652
Cdd:cd03256 4 ENLSKTypnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqigMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 653 MCGYPWIQNASVRDNIIFG------------SPFNKEkydEVVRVCSLKADLDILpagDMTEIgeRGITLSGGQKARINL 720
Cdd:cd03256 84 FQQFNLIERLSVLENVLSGrlgrrstwrslfGLFPKE---EKQRALAALERVGLL---DKAYQ--RADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 721 ARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLT-GMLANKTRILATHQLSLIER-ASRVIVLgTDGQV 787
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREyADRIVGL-KDGRI 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1197-1446 |
7.28e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1197 RKPEMTPPESwPSMGEIIF--ENVDFAYrPGLPIvLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILI- 1273
Cdd:COG0488 299 KTVEIRFPPP-ERLGKKVLelEGLSKSY-GDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLg 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1274 DNVDIsqlGLFDlrrklaiipQDpvlfrgtiRKNLDPfnertDDELWDALVRGGaiakDDLPEVKLQ--------KPDEn 1345
Cdd:COG0488 376 ETVKI---GYFD---------QH--------QEELDP-----DKTVLDELRDGA----PGGTEQEVRgylgrflfSGDD- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1346 gthgkmhkfhLDQAVeeegSNFSLGERQLLALTRALVRQSKILILDEATSSVDyetdgkIQTR-IVEEF-----GdcTIL 1419
Cdd:COG0488 426 ----------AFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD------IETLeALEEAlddfpG--TVL 483
|
250 260 270
....*....|....*....|....*....|
gi 398366407 1420 CIAH-R--LKTIVnyDRILVLEKGEVAEFD 1446
Cdd:COG0488 484 LVSHdRyfLDRVA--TRILEFEDGGVREYP 511
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1215-1452 |
8.82e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1215 FENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNvdisqlglfDLRrkLAIIP 1294
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1295 QDPVLFRG-TIRKNLdpfnERTDDELWDALVRGGAIakddlpEVKLQKPDENGT-----HGKMHKFH---LDQAVEE--E 1363
Cdd:COG0488 68 QEPPLDDDlTVLDTV----LDGDAELRALEAELEEL------EAKLAEPDEDLErlaelQEEFEALGgweAEARAEEilS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1364 G------------SNFSLGERQLLALTRALVRQSKILILDEATSSVDYETdgkiqtrIV--EEF---GDCTILCIAH-R- 1424
Cdd:COG0488 138 GlgfpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES-------IEwlEEFlknYPGTVLVVSHdRy 210
|
250 260
....*....|....*....|....*....
gi 398366407 1425 -LKTIVNydRILVLEKGEVAEFDTPWTLF 1452
Cdd:COG0488 211 fLDRVAT--RILELDRGKLTLYPGNYSAY 237
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1216-1458 |
8.94e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYRPGLPI-VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIP 1294
Cdd:PRK13642 8 ENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1295 QDPvlfrgtirknldpfnertDDELWDALVRGG---AIAKDDLP-EVKLQKPDENGTHGKMHKFHldqavEEEGSNFSLG 1370
Cdd:PRK13642 88 QNP------------------DNQFVGATVEDDvafGMENQGIPrEEMIKRVDEALLAVNMLDFK-----TREPARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKIQtRIVEEFGD---CTILCIAHRLKTIVNYDRILVLEKGEVAEFDT 1447
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM-RVIHEIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
250
....*....|.
gi 398366407 1448 PWTLFSQEDSI 1458
Cdd:PRK13642 224 PSELFATSEDM 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
604-782 |
9.42e-14 |
|
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: 71.76 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-------DLLMCGYPWIQNA-------SVRDNII 669
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqrDSIARGLLYLGHApgikttlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 670 FGSPFnkekydevvrvCSLKADLDILPAGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVD----SRV 744
Cdd:cd03231 96 FWHAD-----------HSDEQVEEALARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARF 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 398366407 745 GKHIMDECLTGMLAnktrILATHQ-LSLIERASRVIVLG 782
Cdd:cd03231 165 AEAMAGHCARGGMV----VLTTHQdLGLSEAGARELDLG 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1230-1465 |
1.15e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIM---SALYRLNELTaGKILIDNVDISQLGLFDLRRK-LAIIPQDPVLFRG-TI 1304
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMkvlSGVYPHGTYE-GEIIFEGEELQASNIRDTERAgIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1305 RKNLDPFNErtddelwdaLVRGGAIakdDLPEVKLQkpdengTHGKMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQ 1384
Cdd:PRK13549 100 LENIFLGNE---------ITPGGIM---DYDAMYLR------AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1385 SKILILDEATSSVDyETDGKIQTRIVEEFGDCTILC--IAHRL---KTIVnyDRILVLEKGE-VAEfdTPWTLFSqEDSI 1458
Cdd:PRK13549 162 ARLLILDEPTASLT-ESETAVLLDIIRDLKAHGIACiyISHKLnevKAIS--DTICVIRDGRhIGT--RPAAGMT-EDDI 235
|
....*..
gi 398366407 1459 FRSMCSR 1465
Cdd:PRK13549 236 ITMMVGR 242
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
605-795 |
1.46e-13 |
|
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: 71.95 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLM----------CGYPwIQNA------SVRDNI 668
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdpvelrrkIGYV-IQQIglfphmTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 669 -----IFGSPfnKEKYDEvvRVCSLKADLDILPAgdmtEIGER-GITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDS 742
Cdd:cd03295 97 alvpkLLKWP--KEKIRE--RADELLALVGLDPA----EFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 743 RVGKHIMDECLT-GMLANKTRILATHQlslIERASRV---IVLGTDGQ-VDIGTVDEL 795
Cdd:cd03295 169 ITRDQLQEEFKRlQQELGKTIVFVTHD---IDEAFRLadrIAIMKNGEiVQVGTPDEI 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1229-1455 |
1.47e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 72.46 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVL-Frgtirkn 1307
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaF------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 ldPFNERtddelwdALVRGGAIAkddlpevklqkpdengtHGKMHKfHLDQAVEE----------EGSNF---SLGERQL 1374
Cdd:COG4559 89 --PFTVE-------EVVALGRAP-----------------HGSSAA-QDRQIVREalalvglahlAGRSYqtlSGGEQQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1375 LALTRALV-------RQSKILILDEATSSVDyetdgkI----QT-RIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEK 1439
Cdd:COG4559 142 VQLARVLAqlwepvdGGPRWLFLDEPTSALD------LahqhAVlRLARQLARrgGGVVAVLHDLNLAAQYaDRILLLHQ 215
|
250
....*....|....*.
gi 398366407 1440 GEVAEFDTPWTLFSQE 1455
Cdd:COG4559 216 GRLVAQGTPEEVLTDE 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1230-1448 |
1.54e-13 |
|
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: 71.63 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfDLRRKLAIIPQDPVLFRG-TIRKNL 1308
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 dpfnertddeLWDALVRG--GAIAKDDLPEVklqkpdengthgkMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQSK 1386
Cdd:cd03265 95 ----------YIHARLYGvpGAERRERIDEL-------------LDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1387 ILILDEATSSVDYETDGKIQTRI---VEEFGdCTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTP 1448
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIeklKEEFG-MTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTP 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
604-782 |
1.82e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG------------DLLMCGYpwiQNA-----SVRD 666
Cdd:PRK13538 17 FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGH---QPGiktelTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 667 NIIFGSPFNKEKYDEVV-----RVcSLKADLDiLPAGdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVD 741
Cdd:PRK13538 94 NLRFYQRLHGPGDDEALwealaQV-GLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398366407 742 srvgKHIMdECLTGMLANKTR-----ILATHQ-LSLIERASRVIVLG 782
Cdd:PRK13538 162 ----KQGV-ARLEALLAQHAEqggmvILTTHQdLPVASDKVRKLRLG 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1210-1456 |
1.98e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.47 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGeIIFENVDFAYRPGLPI---VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---- 1282
Cdd:PRK13649 1 MG-INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1283 LFDLRRKLAIIPQDP--VLFRGTIRKNL--DPFNERTDDELWDALVRggaiakddlpevklqkpdengthgkmHKFHLDQ 1358
Cdd:PRK13649 80 IKQIRKKVGLVFQFPesQLFEETVLKDVafGPQNFGVSQEEAEALAR--------------------------EKLALVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1359 AVEE--EGSNFSL--GERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTrIVEEF--GDCTILCIAHRLKTIVNY- 1431
Cdd:PRK13649 134 ISESlfEKNPFELsgGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLhqSGMTIVLVTHLMDDVANYa 212
|
250 260
....*....|....*....|....*
gi 398366407 1432 DRILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:PRK13649 213 DFVYVLEKGKLVLSGKPKDIFQDVD 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
604-787 |
2.16e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.86 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL-----------MCGYP---WIQNASVRDNII 669
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadyseaalrqaISVVSqrvHLFSATLRDNLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 670 FGSP-FNKEKYDEVVRvcslKADLDILPAGDM---TEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVG 745
Cdd:PRK11160 436 LAAPnASDEALIEVLQ----QVGLEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398366407 746 KHIMDECLTGMlANKTRILATHQLSLIERASRVIVLGtDGQV 787
Cdd:PRK11160 512 RQILELLAEHA-QNKTVLMITHRLTGLEQFDRICVMD-NGQI 551
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
594-795 |
2.37e-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: 73.21 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL------------------- 652
Cdd:COG3842 9 ENVSKRygDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekrnvgmvfqdyal 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 653 ---McgypwiqnaSVRDNIIFG---SPFNKEKYDEvvRVCSLkadLDILpagDMTEIGERGI-TLSGGQKARINLARSVY 725
Cdd:COG3842 89 fphL---------TVAENVAFGlrmRGVPKAEIRA--RVAEL---LELV---GLEGLADRYPhQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 726 KKKDIYLFDDVLSAVDSRVGKHIMDEcLTGMLA--NKTRILATH-Q---LSLierASRVIVLGtDGQV-DIGTVDEL 795
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREE-LRRLQRelGITFIYVTHdQeeaLAL---ADRIAVMN-DGRIeQVGTPEEI 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1229-1444 |
2.44e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.48 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNEL-----TAGKILIDNVDISQLGLFDLRRKLAIIPQDPvlfrgt 1303
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRRVQMVFQIP------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1304 irknldpfNERTDDELWDALVRGGAIAKddlpEVKLQKPDENGTHGKMHKFHLDQAVEEE----GSNFSLGERQLLALTR 1379
Cdd:PRK14247 92 --------NPIPNLSIFENVALGLKLNR----LVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1380 ALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNY-DRILVLEKGEVAE 1444
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVE 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
598-795 |
2.92e-13 |
|
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: 74.17 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 598 KTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG----DLLMCGYPWI--------QNA--- 662
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltKLSRRSLRELrrrvqmvfQDPyss 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 663 -----SVRDNIIFG----SPFNKEKYDEVVR----VCSLKAD-LDILPAgdmteigergiTLSGGQKARINLARSVYKKK 728
Cdd:COG1123 355 lnprmTVGDIIAEPlrlhGLLSRAERRERVAelleRVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEP 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 729 DIYLFDDVLSAVDSRVGKHIMDecltgMLA------NKTRILATHQLSLIER-ASRVIVLGtDGQ-VDIGTVDEL 795
Cdd:COG1123 424 KLLILDEPTSALDVSVQAQILN-----LLRdlqrelGLTYLFISHDLAVVRYiADRVAVMY-DGRiVEDGPTEEV 492
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
600-795 |
3.70e-13 |
|
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: 70.67 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 600 SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAG-----SMRKTDGKVEVNGDLL---------------MC-GYPW 658
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIydldvdvlelrrrvgMVfQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 659 IQNASVRDNIIFGSPF----NKEKYDEVVRVCSLKADLDilpagdmTEIGER--GITLSGGQKARINLARSVYKKKDIYL 732
Cdd:cd03260 92 PFPGSIYDNVAYGLRLhgikLKEELDERVEEALRKAALW-------DEVKDRlhALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 733 FDDVLSAVDSrVGKHIMDECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQ-VDIGTVDEL 795
Cdd:cd03260 165 LDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRlVEFGPTEQI 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
604-768 |
4.26e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD-------LLMCGYPWIQNA-----SVRDNIIFG 671
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpdvAEACHYLGHRNAmkpalTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 672 SPF-NKEKYDEVVRVCSLK-ADLDILPAGDmteigergitLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:PRK13539 98 AAFlGGEELDIAAALEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170
....*....|....*....
gi 398366407 750 DECLTGMLANKTRILATHQ 768
Cdd:PRK13539 168 ELIRAHLAQGGIVIAATHI 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
606-781 |
4.62e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYP--WIQNAS------------VRDNIIFG 671
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSycaqtptlfgdtVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 672 SPFNKEKYDEVvrvcSLKADLDI--LPagdmTEIGERGIT-LSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvGKHI 748
Cdd:PRK10247 105 WQIRNQQPDPA----IFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKHN 175
|
170 180 190
....*....|....*....|....*....|....*
gi 398366407 749 MDECLTGMLANK--TRILATHQLSLIERASRVIVL 781
Cdd:PRK10247 176 VNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1229-1446 |
4.64e-13 |
|
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: 69.98 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDlrRKLAIIPQDPVLF-RGTIRKN 1307
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYpHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 LdPFNERtddelwdalvrggaIAKDDLPEVKlqkpdeNGTHGKMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQSKI 1387
Cdd:cd03301 93 I-AFGLK--------------LRKVPKDEID------ERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1388 LILDEATSSVD----YETDGKIQtRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFD 1446
Cdd:cd03301 152 FLMDEPLSNLDaklrVQMRAELK-RLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1214-1458 |
4.71e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.26 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1214 IFENVDFAYR-PGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDN--VDISQLGLFDLRRKL 1290
Cdd:PRK13639 1 ILETRDLKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDP--VLFRGTIRKNL--DPFNERTDDELWDALVrggaiaKDDLPEVKLQKPDENGTHgkmhkfHLdqaveeegsn 1366
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVafGPLNLGLSKEEVEKRV------KEALKAVGMEGFENKPPH------HL---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1367 fSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGEVA 1443
Cdd:PRK13639 139 -SGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQI-MKLLYDLNKegITIIISTHDVDLVPVYaDKVYVMSDGKII 216
|
250
....*....|....*
gi 398366407 1444 EFDTPWTLFSQEDSI 1458
Cdd:PRK13639 217 KEGTPKEVFSDIETI 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1213-1456 |
5.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPIV---LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDIS----QLGLFD 1285
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 LRRKLAIIPQDP--VLFRGTIRKNL--DPFNERTDDElwdalvRGGAIAKDDLPEVKLQKpdengthgkmhkfhldQAVE 1361
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQNFGIPKE------KAEKIAAEKLEMVGLAD----------------EFWE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1362 EEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRI--VEEFGDcTILCIAHRLKTIVNY-DRILVLE 1438
Cdd:PRK13643 140 KSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFesIHQSGQ-TVVLVTHLMDDVADYaDYVYLLE 218
|
250
....*....|....*...
gi 398366407 1439 KGEVAEFDTPWTLFSQED 1456
Cdd:PRK13643 219 KGHIISCGTPSDVFQEVD 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1229-1453 |
6.52e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNV------DISQLGLFDLRRKLAIIPQDPvlfrg 1302
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQP----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1303 tirknlDPFNERT-DDELWDALVRGGAIAKDDLPEVKLQKPDENGTHGKMHkfhldQAVEEEGSNFSLGERQLLALTRAL 1381
Cdd:PRK14246 100 ------NPFPHLSiYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVY-----DRLNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1382 VRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTPWTLFS 1453
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFT 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1230-1447 |
9.15e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDN--VDIS------QLGLfdlrrklAIIPQDPVLFR 1301
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRsprdaiALGI-------GMVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1302 G-TIRKNLdpfnertddelwdAL----VRGGAIAKDDLpEVKLQKpdengthgKMHKFHL----DQAVEEegsnFSLGER 1372
Cdd:COG3845 94 NlTVAENI-------------VLglepTKGGRLDRKAA-RARIRE--------LSERYGLdvdpDAKVED----LSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1373 QLLALTRALVRQSKILILDEATsSV--DYETDGKIQT--RIVEEfgDCTILCIAHRLKTIVNY-DRILVLEKGE-VAEFD 1446
Cdd:COG3845 148 QRVEILKALYRGARILILDEPT-AVltPQEADELFEIlrRLAAE--GKSIIFITHKLREVMAIaDRVTVLRRGKvVGTVD 224
|
.
gi 398366407 1447 T 1447
Cdd:COG3845 225 T 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1213-1442 |
9.71e-13 |
|
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: 69.73 E-value: 9.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAY--RPglpiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKilidnvDISQLG-------L 1283
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN------DVRLFGerrggedV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1284 FDLRRKLAIIpqDPVLFRGTirknldpfneRTDDELWDAlVRGGAIAKDDLPEvKLQKPDENGTHGKMHKFHLDQAVEEE 1363
Cdd:COG1119 74 WELRKRIGLV--SPALQLRF----------PRDETVLDV-VLSGFFDSIGLYR-EPTDEQRERARELLELLGLAHLADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1364 GSNFSLGERQLLALTRALVRQSKILILDEATSSVDYEtdGKIQ-TRIVEEF---GDCTILCIAHRLKTIV-NYDRILVLE 1438
Cdd:COG1119 140 FGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLG--ARELlLALLDKLaaeGAPTLVLVTHHVEEIPpGITHVLLLK 217
|
....
gi 398366407 1439 KGEV 1442
Cdd:COG1119 218 DGRV 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
572-795 |
2.29e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.63 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 572 KPSASTNKAKR----LDNMLKDRDGPEDLEktsfrgfkDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEV 647
Cdd:PRK11607 7 RPQAKTRKALTplleIRNLTKSFDGQHAVD--------DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 648 NG-------------DLLMCGYPWIQNASVRDNIIFGSPFNKEKYDEVV-RVCslkadlDILPAGDMTEIGERGI-TLSG 712
Cdd:PRK11607 79 DGvdlshvppyqrpiNMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIAsRVN------EMLGLVHMQEFAKRKPhQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 713 GQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTGM-LANKTRILATH-QLSLIERASRVIVLGTDGQVDIG 790
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
....*
gi 398366407 791 TVDEL 795
Cdd:PRK11607 233 EPEEI 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
605-794 |
2.51e-12 |
|
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: 68.13 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DL------------LMCGYPWIQNASVRDNIIFG 671
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkDItnlppekrdisyVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 672 -------SPFNKEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRV 744
Cdd:cd03299 96 lkkrkvdKKEIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398366407 745 GKHIMDECLTGMLANKTRIL-ATHQLSLIER-ASRVIVLGTDGQVDIGTVDE 794
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1233-1443 |
2.54e-12 |
|
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: 67.52 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1233 LNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDlrRKLAIIPQDPVLFRG-TIRKNLDpf 1311
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVG-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1312 nertddelwdaLVRGgaiakddlPEVKLQKPDENGTHGKMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILD 1391
Cdd:cd03298 93 -----------LGLS--------PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1392 EATSSVDYETDGKIQTRIVE---EFGDcTILCIAHRLKTIVN-YDRILVLEKGEVA 1443
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDlhaETKM-TVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1213-1441 |
3.42e-12 |
|
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: 65.55 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKI-LIDNVDISqlglfdlrrkla 1291
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKIG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1292 iipqdpvlfrgtirknldpfnertddelwdalvrggaiakddlpevklqkpdengthgkmhkfHLDQaveeegsnFSLGE 1371
Cdd:cd03221 67 ---------------------------------------------------------------YFEQ--------LSGGE 75
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVDYETdgkiQTRIVEEFGD--CTILCIAH-R--LKTIVNydRILVLEKGE 1441
Cdd:cd03221 76 KMRLALAKLLLENPNLLLLDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQVAT--KIIELEDGK 144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
605-809 |
3.71e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DL-------------LMCGYPWIQNASVRDNIIF 670
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhDLrdytlaslrnqvaLVSQNVHLFNDTIANNIAY 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSpfnKEKY--DEVVRVCSLKADLDI---LPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvG 745
Cdd:PRK11176 440 AR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-S 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 746 KHIMDECLTGMLANKTRILATHQLSLIERASRVIVLgTDGQ-VDIGTVDELKARNQTLINL--LQFS 809
Cdd:PRK11176 516 ERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV-EDGEiVERGTHAELLAQNGVYAQLhkMQFG 581
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1229-1440 |
4.41e-12 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 66.86 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLgLFDLRRKLAIIpQDPVLfrgtirknl 1308
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGALI-EAPGF--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 dpFNERTDDElwdALVRGGAIakddlpevkLQKPDENgthgkmhkfhLDQAVEEEG---------SNFSLGERQLLALTR 1379
Cdd:cd03268 84 --YPNLTARE---NLRLLARL---------LGIRKKR----------IDEVLDVVGlkdsakkkvKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1380 ALVRQSKILILDEATSSVDyeTDGKIQTR--IVE--EFGdCTILCIAHRL---KTIVnyDRILVLEKG 1440
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLD--PDGIKELRelILSlrDQG-ITVLISSHLLseiQKVA--DRIGIINKG 202
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
605-791 |
4.45e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.59 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-------------DLLMCGYPWIQNASVRDNIIFG 671
Cdd:PRK09452 31 SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpaenrhvNTVFQSYALFPHMTVFENVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 672 SPFNKEKYDEVV-RVcslkadLDILPAGDMTEIGERGIT-LSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:PRK09452 111 LRMQKTPAAEITpRV------MEALRMVQLEEFAQRKPHqLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQ 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398366407 750 DEclTGMLANK---TRILATH-QLSLIERASRVIVLgTDGQVD-IGT 791
Cdd:PRK09452 185 NE--LKALQRKlgiTFVFVTHdQEEALTMSDRIVVM-RDGRIEqDGT 228
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
897-1182 |
4.67e-12 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 68.58 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 897 LPLYAILVVGTTFCSLFSSVWLSYWTENKFKNRPPSF-----YMGLYSFFVFAAFI------FMNGQFTILCAMGIMask 965
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGgvdfsGLLRILLLLLGLYLlsalfsYLQNRLMARVSQRTV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 966 wLNLR--AVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESL-RLMTSqFANIVGVCVMCIVYLPWFA----IAI 1038
Cdd:cd18547 78 -YDLRkdLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLtQLISS-ILTIVGTLIMMLYISPLLTlivlVTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1039 PFLLVIFVLIAdhyqssGREIKRLEAVQRSFvyNNLN----EVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVL 1114
Cdd:cd18547 156 PLSLLVTKFIA------KRSQKYFRKQQKAL--GELNgyieEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1115 QRWVGIFLDMV-AIAFALII---TLLCVTRAFpisaaSVGVL---LTYVLQLPGLLNTILRAMTQTENDMNSAER 1182
Cdd:cd18547 228 SGLLMPIMNFInNLGYVLVAvvgGLLVINGAL-----TVGVIqafLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
596-781 |
5.02e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.09 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 596 LEKTSFR------GFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGdLLMCGYPWIQNASVRDNII 669
Cdd:PRK13644 4 LENVSYSypdgtpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-IDTGDFSKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 670 FGSPFNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGI--------------TLSGGQKARINLARSVYKKKDIYLFDD 735
Cdd:PRK13644 83 FQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALaeiglekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398366407 736 VLSAVDSRVGKHIMDECLTGMLANKTRILATHQLSLIERASRVIVL 781
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
605-805 |
6.22e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.83 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPW---------IQN-------ASVRDNI 668
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWdirhkigmvFQNpdnqfvgATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 669 IFGSPFNKEKYDEVV-RVcslKADLDILpagDMTEIGERGIT-LSGGQKARINLARSVYKKKDIYLFDDVLSAVDS---- 742
Cdd:PRK13650 104 AFGLENKGIPHEEMKeRV---NEALELV---GMQDFKEREPArLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPegrl 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 743 ---RVGKHIMDEcltgmlANKTRILATHQLSLIERASRVIVLgTDGQVD-IGTVDELKARNQTLINL 805
Cdd:PRK13650 178 eliKTIKGIRDD------YQMTVISITHDLDEVALSDRVLVM-KNGQVEsTSTPRELFSRGNDLLQL 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1229-1443 |
8.37e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDIS--------QLGLFdlrrklaIIPQDPVLF 1300
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpakahQLGIY-------LVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1301 RG-TIRKNLdpfnertddelwdaLVRggaIAKDDLPEVKL-QKPDENGTHgkmhkfhLDQAVEeeGSNFSLGERQLLALT 1378
Cdd:PRK15439 99 PNlSVKENI--------------LFG---LPKRQASMQKMkQLLAALGCQ-------LDLDSS--AGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1379 RALVRQSKILILDEATSSVD-YETD---GKIQTRIVEEFGdctILCIAHRLKTIVNY-DRILVLEKGEVA 1443
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTpAETErlfSRIRELLAQGVG---IVFISHKLPEIRQLaDRISVMRDGTIA 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
605-799 |
8.70e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.75 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMC--------GYPWIQN------ASVRDNIIF 670
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvlrqGVAMVQQdpvvlaDTFLANVTL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 GSPFNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHImD 750
Cdd:PRK10790 438 GRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI-Q 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398366407 751 ECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKARN 799
Cdd:PRK10790 517 QALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
596-799 |
8.83e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 66.70 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 596 LEKTSFR--GFKdLNFD--IKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLmcGYPWIQ---------- 660
Cdd:COG3840 4 LDDLTYRygDFP-LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLT--ALPPAErpvsmlfqen 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 661 N----ASVRDNIIFG-------SPFNKEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKD 729
Cdd:COG3840 81 NlfphLTVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 730 IYLFDDVLSAVDS--RvgkhimDECLTgmLANK-------TRILATHQLSLIER-ASRVIVLGtDGQVD-IGTVDELKAR 798
Cdd:COG3840 150 ILLLDEPFSALDPalR------QEMLD--LVDElcrerglTVLMVTHDPEDAARiADRVLLVA-DGRIAaDGPTAALLDG 220
|
.
gi 398366407 799 N 799
Cdd:COG3840 221 E 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1229-1444 |
9.57e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.02 E-value: 9.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQL---GLFDLRRKLAIIPQDP---VLFRG 1302
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1303 TIRKNLD-PFNERTDDELWDALVRGGAIakddLPEVKLqkPDEngthgkmhkfHLDQAVEEegsnFSLGERQLLALTRAL 1381
Cdd:PRK10419 107 TVREIIRePLRHLLSLDKAERLARASEM----LRAVDL--DDS----------VLDKRPPQ----LSGGQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1382 VRQSKILILDEATSSVDYETDGKI---QTRIVEEFGdCTILCIAHRLKtIVNY--DRILVLEKGEVAE 1444
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVirlLKKLQQQFG-TACLFITHDLR-LVERfcQRVMVMDNGQIVE 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1230-1441 |
1.33e-11 |
|
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: 68.70 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIM---SALYRLNELTaGKILIDNVDISQLGLFDLRRK-LAIIPQDPVLFRG-TI 1304
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMkilSGVYPHGTWD-GEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1305 RKNLDPFNE------RTDDelwDALVRGgaiAKDDLPEVKLqkPDENGTHGKMhkfhldqaveeegsNFSLGERQLLALT 1378
Cdd:TIGR02633 96 AENIFLGNEitlpggRMAY---NAMYLR---AKNLLRELQL--DADNVTRPVG--------------DYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1379 RALVRQSKILILDEATSSVDyETDGKIQTRIVEEFGDCTILC--IAHRLKTIVNY-DRILVLEKGE 1441
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLT-EKETEILLDIIRDLKAHGVACvyISHKLNEVKAVcDTICVIRDGQ 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
594-800 |
1.59e-11 |
|
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: 65.68 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT------SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGYPWIQNAS--- 663
Cdd:cd03258 5 KNVSKVfgdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtDLTLLSGKELRKARrri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 664 --------------VRDNI-----IFGSP--FNKEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLAR 722
Cdd:cd03258 85 gmifqhfnllssrtVFENValpleIAGVPkaEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 723 SVYKKKDIYLFDDVLSAVDSRVGKHIMdECLTGMlaNK----TRILATHQLSLIER-ASRVIVLGtDGQ-VDIGTVDELK 796
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSIL-ALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVME-KGEvVEEGTVEEVF 229
|
....
gi 398366407 797 ARNQ 800
Cdd:cd03258 230 ANPQ 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
605-781 |
1.68e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.75 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVnGDLLM---------CG--------YPwiqNASVRDN 667
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMndvppaergVGmvfqsyalYP---HLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGSPFNK-------EKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAV 740
Cdd:PRK11000 96 MSFGLKLAGakkeeinQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398366407 741 DS--RVGKHIMDECLTGMLaNKTRILATH-QLSLIERASRVIVL 781
Cdd:PRK11000 165 DAalRVQMRIEISRLHKRL-GRTMIYVTHdQVEAMTLADKIVVL 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1215-1392 |
1.80e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1215 FENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD-LRRKLAII 1293
Cdd:PRK11614 8 FDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1294 PQDPVLF-RGTIRKNLdpfnertddelwdalVRGGAIAKDDLPEVKLQKpdengTHGKMHKFHlDQAVEEEGSnFSLGER 1372
Cdd:PRK11614 86 PEGRRVFsRMTVEENL---------------AMGGFFAERDQFQERIKW-----VYELFPRLH-ERRIQRAGT-MSGGEQ 143
|
170 180
....*....|....*....|
gi 398366407 1373 QLLALTRALVRQSKILILDE 1392
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDE 163
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
604-768 |
1.93e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 64.69 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD------------LLMCGY-PWIQNA-SVRDNII 669
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHlPGLKPElSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 670 FGSPFNKEkydevvrvcslkADLDILPAgdMTEIGERGIT------LSGGQKARINLARSVYKKKDIYLFDDVLSAVD-- 741
Cdd:TIGR01189 96 FWAAIHGG------------AQRTIEDA--LAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDka 161
|
170 180
....*....|....*....|....*....
gi 398366407 742 --SRVGKHIMDECLTGMLAnktrILATHQ 768
Cdd:TIGR01189 162 gvALLAGLLRAHLARGGIV----LLTTHQ 186
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
594-787 |
1.99e-11 |
|
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: 65.24 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKtSFRGF---KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGYPWIQ--------- 660
Cdd:cd03262 4 KNLHK-SFGDFhvlKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlKLTDDKKNINElrqkvgmvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 661 -------NASVRDNIIFGsPFN--KEKYDEVVRvcslKAdLDILPAGDMTE-IGERGITLSGGQKARINLARSVYKKKDI 730
Cdd:cd03262 83 qqfnlfpHLTVLENITLA-PIKvkGMSKAEAEE----RA-LELLEKVGLADkADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 731 YLFDDVLSAVDSRVgkhiMDECLTGM--LA--NKTRILATHQLSLI-ERASRVIVLgTDGQV 787
Cdd:cd03262 157 MLFDEPTSALDPEL----VGEVLDVMkdLAeeGMTMVVVTHEMGFArEVADRVIFM-DDGRI 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1213-1442 |
2.12e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.28 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD---LRRK 1289
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVLFRgtirknldpfnERT-DDELWDALVRGGAiAKDDLPEVKLQKPDENGTHGKMHKFHLdqaveeegsNFS 1368
Cdd:PRK10908 81 IGMIFQDHHLLM-----------DRTvYDNVAIPLIIAGA-SGDDIRRRVSAALDKVGLLDKAKNFPI---------QLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1369 LGERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFG--DCTILCIAHRLKTIV--NYdRILVLEKGEV 1442
Cdd:PRK10908 140 GGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI-LRLFEEFNrvGVTVLMATHDIGLISrrSY-RMLTLSDGHL 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
596-787 |
2.28e-11 |
|
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: 64.82 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 596 LEKTSFR-GFKDLNFD--IKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPWIQNAS--------- 663
Cdd:cd03298 3 LDKIRFSyGEQPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSmlfqennlf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 664 ----VRDNIIFG-SPFNKEKYDEVVRVCSLKADLDIlpAGDMTEIGErgiTLSGGQKARINLARSVYKKKDIYLFDDVLS 738
Cdd:cd03298 83 ahltVEQNVGLGlSPGLKLTAEDRQAIEVALARVGL--AGLEKRLPG---ELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398366407 739 AVDSRVgKHIMDECLTGMLANK--TRILATHQLSLIER-ASRVIVLgTDGQV 787
Cdd:cd03298 158 ALDPAL-RAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFL-DNGRI 207
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
968-1182 |
3.36e-11 |
|
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: 65.99 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 968 NLRA--VKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFA----IAIPFL 1041
Cdd:cd18563 77 DLRRdlYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLAllvlIPVPLV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1042 LVIFVLIadhyqssGREIKRLEAVQ---RSFVYNNLNEVLGGMDTIKAY----RSQERFLAKSDFLINKMNEAGYLvvvl 1114
Cdd:cd18563 157 VWGSYFF-------WKKIRRLFHRQwrrWSRLNSVLNDTLPGIRVVKAFgqekREIKRFDEANQELLDANIRAEKL---- 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1115 qrWVGIF--LDMVAIAFALIITLLCVTRAfpISAA-SVGVL---LTYVLQLPGLLNTILRAMTQTENDMNSAER 1182
Cdd:cd18563 226 --WATFFplLTFLTSLGTLIVWYFGGRQV--LSGTmTLGTLvafLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1229-1448 |
3.92e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIdNVDISqlGLFDLRrkLAIIPQ----DPVLFRGTI 1304
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NGRVS--ALLELG--AGFHPEltgrENIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1305 ----RKNLDpfnERTDD-----ELWDALvrggaiakdDLPeVKlqkpdengthgkmhkfhldqaveeegsNFSLGERQLL 1375
Cdd:COG1134 116 lglsRKEID---EKFDEivefaELGDFI---------DQP-VK---------------------------TYSSGMRARL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1376 ALTRALVRQSKILILDEATSSVDYETDGKIQTRIvEEF--GDCTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTP 1448
Cdd:COG1134 156 AFAVATAVDPDILLVDEVLAVGDAAFQKKCLARI-RELreSGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDP 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
604-787 |
4.13e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLmcgyPWIQNASVRDNIIFGSPFNKEKydEVV 683
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN----QFGREASLIDAIGRKGDFKDAV--ELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 684 RVCSLkadldilpaGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVD---SRVGKHIMDECLTGmlANK 760
Cdd:COG2401 120 NAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR--AGI 188
|
170 180
....*....|....*....|....*....
gi 398366407 761 TRILATHQLSLIE--RASRVIVLGTDGQV 787
Cdd:COG2401 189 TLVVATHHYDVIDdlQPDLLIFVGYGGVP 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
608-741 |
6.12e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.22 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 608 NFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPWIQNAS-------------VRDNIIFG--- 671
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSmlfqennlfshltVAQNIGLGlnp 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 672 ----SPFNKEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVD 741
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1213-1453 |
6.23e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.34 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDI--SQLGLFDLRRKL 1290
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1291 AIIPQDPVLF-RGTIRKNLdPFNERTddelwdalVRGG------AIAKDDLPEVKLQKpdengthgKMHKFhldqaveee 1363
Cdd:PRK09493 80 GMVFQQFYLFpHLTALENV-MFGPLR--------VRGAskeeaeKQARELLAKVGLAE--------RAHHY--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1364 GSNFSLGERQLLALTRALVRQSKILILDEATSSVDYE-------------TDGKIQTRIVEEFGdctilcIAHRLKTivn 1430
Cdd:PRK09493 134 PSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhevlkvmqdlaEEGMTMVIVTHEIG------FAEKVAS--- 204
|
250 260
....*....|....*....|...
gi 398366407 1431 ydRILVLEKGEVAEFDTPWTLFS 1453
Cdd:PRK09493 205 --RLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
897-1133 |
6.85e-11 |
|
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: 65.14 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 897 LPLYAILVVGTTFCSLFSSVWLSYWTENKFKNRPPSFyMGLYSFFVFAAFI------FMNGQFTILCAMGIMAskwlNLR 970
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEA-LLLVPLAIIGLFLlrglasYLQTYLMAYVGQRVVR----DLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 971 A--VKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVG-VCVMciVYLPW-----FAIAIPFLL 1042
Cdd:cd18552 76 NdlFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGlLGVL--FYLDWkltliALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1043 VIFVLIadhyqssGREIKRL-EAVQRSF--VYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVG 1119
Cdd:cd18552 154 LPIRRI-------GKRLRKIsRRSQESMgdLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSS 226
|
250
....*....|....*
gi 398366407 1120 IFLDMV-AIAFALII 1133
Cdd:cd18552 227 PLMELLgAIAIALVL 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
605-795 |
7.20e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.63 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMC-GYPWIQN---------------ASVRDNI 668
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKeNLKEIRKkigiifqnpdnqfigATVEDDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 669 IFG---SPFNKEKYDEVVRVCSLKADldilpagdMTEIGER-GITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRv 744
Cdd:PRK13632 106 AFGlenKKVPPKKMKDIIDDLAKKVG--------MEDYLDKePQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 745 GKH----IMDECLTGMlaNKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDEL 795
Cdd:PRK13632 177 GKReikkIMVDLRKTR--KKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1232-1454 |
8.92e-11 |
|
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: 66.36 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1232 NLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILI----DNVDISQLGlFDLR----RKLAIIPQDPVLFrgT 1303
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG-PDGRgrakRYIGILHQEYDLY--P 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1304 IRKNLDPFNERTDDELWDALVRGGAIakddlpeVKLqkpdengthgKMHKFHLDQAVE---EEGSNFSLGERQLLALTRA 1380
Cdd:TIGR03269 379 HRTVLDNLTEAIGLELPDELARMKAV-------ITL----------KMVGFDEEKAEEildKYPDELSEGERHRVALAQV 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1381 LVRQSKILILDEATSSVDYETDGKIQTRIV---EEFGDcTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTPWTLFSQ 1454
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHSILkarEEMEQ-TFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1232-1455 |
1.02e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.24 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1232 NLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFdlRRKLAIIPQDPVLF-RGTIRKNLdP 1310
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFpHMTVEQNI-A 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1311 FNERTDdelwdalvrggaiakddlpevKLQKPDENGTHGKMHKF-HLDQAVEEEGSNFSLGERQLLALTRALVRQSKILI 1389
Cdd:PRK11607 114 FGLKQD---------------------KLPKAEIASRVNEMLGLvHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1390 LDEATSSVDYETDGKIQTRIV---EEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAE-------FDTPWTLFSQE 1455
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVdilERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQigepeeiYEHPTTRYSAE 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1213-1305 |
1.06e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.56 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAI 1292
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90
....*....|....
gi 398366407 1293 IPQDPVL-FRGTIR 1305
Cdd:COG4604 80 LRQENHInSRLTVR 93
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1220-1444 |
1.10e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1220 FAYRPGL-----PIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISqLGLFDLR-RKLAII 1293
Cdd:PRK15112 14 FRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRsQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1294 PQDPVLF---RGTIRKNLDpFNERTDDELwDALVRGGAIaKDDLPEVKLqKPDENGTHGKMhkfhldqaveeegsnFSLG 1370
Cdd:PRK15112 93 FQDPSTSlnpRQRISQILD-FPLRLNTDL-EPEQREKQI-IETLRQVGL-LPDHASYYPHM---------------LAPG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKI---QTRIVEEFGDCTILCIAH--RLKTIVnyDRILVLEKGEVAE 1444
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLinlMLELQEKQGISYIYVTQHlgMMKHIS--DQVLVMHQGEVVE 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1229-1470 |
1.14e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.87 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDN--VDISQLGLFDLRRKLAIIPQDPvlfrgtirk 1306
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDP--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1307 NLDPFNERTDDELWDALvRGGAIAKDDLPevklQKPDENGTHGKMHKFHlDQAVEeegsNFSLGERQLLALTRALVRQSK 1386
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSL-RNLGVPEAEIT----RRVDEALTLVDAQHFR-HQPIQ----CLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1387 ILILDEATSSVDyeTDGKIQT-----RIVEEfGDCTILCiAHRLKTIVNY-DRILVLEKGEVAEFDTPWTLFSQEDSIFR 1460
Cdd:PRK13638 157 YLLLDEPTAGLD--PAGRTQMiaiirRIVAQ-GNHVIIS-SHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232
|
250
....*....|
gi 398366407 1461 SMCSRSGIVE 1470
Cdd:PRK13638 233 AGLTQPWLVK 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1229-1446 |
1.32e-10 |
|
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: 62.94 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGL---FDlrrklaiiPQ----DPVLFR 1301
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgggFN--------PEltgrENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1302 GTIrKNLDP--FNERTDD-----ELWDALvrggaiakdDLPeVKlqkpdengthgkmhkfhldqaveeegsNFSLGERQL 1374
Cdd:cd03220 109 GRL-LGLSRkeIDEKIDEiiefsELGDFI---------DLP-VK---------------------------TYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1375 LALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIA-HRLKTIVNY-DRILVLEKGEVAEFD 1446
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
605-786 |
1.52e-10 |
|
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: 61.40 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKV---EVNGDLLMCGYPWIQNASVRDNIIFgspfnkekyde 681
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmpEGEDLLFLPQRPYLPLGTLREQLIY----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 682 vvrvcslkadldilPAGDmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMdECLTGMLAnkT 761
Cdd:cd03223 87 --------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY-QLLKELGI--T 140
|
170 180
....*....|....*....|....*
gi 398366407 762 RILATHQLSLIERASRVIVLGTDGQ 786
Cdd:cd03223 141 VISVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
657-795 |
1.60e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 657 PWIQNASVRDNIIFGSpfNKEKYDEVVRVCSLKAD---LDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLF 733
Cdd:PTZ00265 1305 PMLFNMSIYENIKFGK--EDATREDVKRACKFAAIdefIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLL 1382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 734 DDVLSAVDSR----VGKHIMDeclTGMLANKTRILATHQLSLIERASRVIVL------GTDGQVDiGTVDEL 795
Cdd:PTZ00265 1383 DEATSSLDSNseklIEKTIVD---IKDKADKTIITIAHRIASIKRSDKIVVFnnpdrtGSFVQAH-GTHEEL 1450
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1229-1448 |
1.82e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.58 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGlfDLRRKLAIIPQDPVLF-RGTIRKN 1307
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP--AENRHVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 L-----------DPFNERTDDELwdALVRggaiakddLPEVKLQKPdengthgkmhkfhldqaveeegSNFSLGERQLLA 1376
Cdd:PRK09452 107 VafglrmqktpaAEITPRVMEAL--RMVQ--------LEEFAQRKP----------------------HQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1377 LTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGdCTILCIAH-RLKTIVNYDRILVLEKGEVAEFDTP 1448
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNelkALQRKLG-ITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1217-1454 |
1.84e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1217 NVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRL---NELTAGKILIDNVDISQLGLFDLRR----K 1289
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKELNKlraeQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVlfrgtirKNLDPFnERTDDELWDALVRGGAIAKDD--------LPEVKLqkPDengTHGKMHKF-Hldqav 1360
Cdd:PRK09473 99 ISMIFQDPM-------TSLNPY-MRVGEQLMEVLMLHKGMSKAEafeesvrmLDAVKM--PE---ARKRMKMYpH----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1361 eeegsNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE---EFgDCTILCIAHRLKTIVNY-DRILV 1436
Cdd:PRK09473 161 -----EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEF-NTAIIMITHDLGVVAGIcDKVLV 234
|
250
....*....|....*...
gi 398366407 1437 LEKGEVAEFDTPWTLFSQ 1454
Cdd:PRK09473 235 MYAGRTMEYGNARDVFYQ 252
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1210-1457 |
1.84e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.06 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEIIFENVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDIS-------QLG 1282
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1283 LFD------LRRKLAIIPQDPVLFRG-TIRKNldpfnertddeLWDALVRGGAIAKDDLPEVKLQKPDENGTHgkmhkfh 1355
Cdd:PRK10619 81 VADknqlrlLRTRLTMVFQHFNLWSHmTVLEN-----------VMEAPIQVLGLSKQEARERAVKYLAKVGID------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1356 lDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFGD--CTILCIAHRLKTIVNY-D 1432
Cdd:PRK10619 143 -ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEV-LRIMQQLAEegKTMVVVTHEMGFARHVsS 220
|
250 260
....*....|....*....|....*
gi 398366407 1433 RILVLEKGEVAEFDTPWTLFSQEDS 1457
Cdd:PRK10619 221 HVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
606-795 |
1.97e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.33 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD-------------LLMCGYPWIQNASVRDNIIFGS 672
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkvgFVFQHYALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 673 ---PFNKEKYDEVVR--VCSLkadLDILpagDMTEIGERGIT-LSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGK 746
Cdd:PRK10851 100 tvlPRRERPNAAAIKakVTQL---LEMV---QLAHLADRYPAqLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 747 HI------MDECLtgmlaNKTRILATH-QLSLIERASRVIVLGTDGQVDIGTVDEL 795
Cdd:PRK10851 174 ELrrwlrqLHEEL-----KFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1230-1440 |
1.99e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGlFDLRRKLAIipqdpvlfrGTIRKNLD 1309
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLGI---------GIIYQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1310 PFNERTDDE------LWDALVRGGAIAkdDLPEVKLQkpdengTHGKMHKFHLDQAVEEEGSNFSLGERQLLALTRALVR 1383
Cdd:PRK09700 91 VIDELTVLEnlyigrHLTKKVCGVNII--DWREMRVR------AAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 1384 QSKILILDEATSSV-DYETDG--KIQTRIVEEfgDCTILCIAHRLKTIVNY-DRILVLEKG 1440
Cdd:PRK09700 163 DAKVIIMDEPTSSLtNKEVDYlfLIMNQLRKE--GTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
605-781 |
2.00e-10 |
|
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: 61.91 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL------MCGY-P----WIQNASVRDNII-FGS 672
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdiaarnRIGYlPeergLYPKMKVIDQLVyLAQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 673 PFNKEKYDEVVRVCSLKADLDIlpagdmTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDE 751
Cdd:cd03269 97 LKGLKKEEARRRIDEWLERLEL------SEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV 170
|
170 180 190
....*....|....*....|....*....|.
gi 398366407 752 CLTGMLANKTRILATHQLSLIER-ASRVIVL 781
Cdd:cd03269 171 IRELARAGKTVILSTHQMELVEElCDRVLLL 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
605-795 |
2.02e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 62.48 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD----------LLMCGY---PWIqnaSVRDNIIFG 671
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrmVVFQNYsllPWL---TVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 672 -----SPFNKEKYDEVVRvcslkADLDILpagDMTEIGERGIT-LSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVG 745
Cdd:TIGR01184 79 vdrvlPDLSKSERRAIVE-----EHIALV---GLTEAADKRPGqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398366407 746 KHIMDECLTGMLANK-TRILATHQL-SLIERASRVIVLGTDGQVDIGTVDEL 795
Cdd:TIGR01184 151 GNLQEELMQIWEEHRvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1213-1431 |
2.18e-10 |
|
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: 65.16 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAyRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNvdisqlglfdlRRKLAI 1292
Cdd:TIGR00954 452 IKFENIPLV-TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFY 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDPVLFRGTIRKNLdPFNERTDDelwdalvrggaIAKDDLPEVKLQKPDENgthgkmhkFHLDQAVEEEGS------- 1365
Cdd:TIGR00954 520 VPQRPYMTLGTLRDQI-IYPDSSED-----------MKRRGLSDKDLEQILDN--------VQLTHILEREGGwsavqdw 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1366 --NFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFGdCTILCIAHRlKTIVNY 1431
Cdd:TIGR00954 580 mdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM-YRLCREFG-ITLFSVSHR-KSLWKY 644
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1223-1459 |
2.21e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1223 RPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfdLRRKLAIIPQDPVLF-R 1301
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI--QQRDICMVFQSYALFpH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1302 GTIRKNL-----------DPFNERTDDELwdALVrggaiakdDLpevklqkpdengthGKMHKFHLDQaveeegsnFSLG 1370
Cdd:PRK11432 93 MSLGENVgyglkmlgvpkEERKQRVKEAL--ELV--------DL--------------AGFEDRYVDQ--------ISGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE---EFGdCTILCIAH-RLKTIVNYDRILVLEKGEVAEFD 1446
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqQFN-ITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIG 219
|
250
....*....|...
gi 398366407 1447 TPWTLFSQEDSIF 1459
Cdd:PRK11432 220 SPQELYRQPASRF 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1229-1444 |
2.47e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.77 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSAL-----YrlnELTAGKILIDNVDISQLGLfDLRRKLAII--PQDPVLFR 1301
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkY---EVTEGEILFKGEDITDLPP-EERARLGIFlaFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1302 GTirKNLDpfnertddelwdaLVRGgaiakddlpevklqkpdengthgkmhkfhldqaVEEegsNFSLGERQLLALTRAL 1381
Cdd:cd03217 91 GV--KNAD-------------FLRY---------------------------------VNE---GFSGGEKKRNEILQLL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1382 VRQSKILILDEATSSVDYETdGKIQTRIVEEF--GDCTILCIAHRLKtIVNY---DRILVLEKGEVAE 1444
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDA-LRLVAEVINKLreEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVK 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1230-1452 |
3.01e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNEL-----TAGKILIDNVDI--SQLGLFDLRRKLAIIPQDPVLFRG 1302
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1303 TIRKNLD---PFNERTDDELWDALVRGGAIAKDDLPEVKlqkpdengthGKMHkfhlDQAVEEEGsnfslGERQLLALTR 1379
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQVLDEAVEKSLKGASIWDEVK----------DRLH----DSALGLSG-----GQQQRVCIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1380 ALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTPWTLF 1452
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQMF 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1198-1444 |
3.23e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1198 KPEMTPPESWPSMGEIIFENVDFAYrPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVD 1277
Cdd:PRK10522 308 KAEFPRPQAFPDWQTLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1278 ISQLGLFDLRRKLAIIPQDPVLFrgtiRKNLDPFNERTDDELWDALvrggaiakddLPEVKLQkpdengthgkmHKFHLD 1357
Cdd:PRK10522 387 VTAEQPEDYRKLFSAVFTDFHLF----DQLLGPEGKPANPALVEKW----------LERLKMA-----------HKLELE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1358 qavEEEGSN--FSLGERQLLALTRALVRQSKILILDEatssvdYETDGKIQTR---------IVEEFGDcTILCIAHRLK 1426
Cdd:PRK10522 442 ---DGRISNlkLSKGQKKRLALLLALAEERDILLLDE------WAADQDPHFRrefyqvllpLLQEMGK-TIFAISHDDH 511
|
250
....*....|....*...
gi 398366407 1427 TIVNYDRILVLEKGEVAE 1444
Cdd:PRK10522 512 YFIHADRLLEMRNGQLSE 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
593-787 |
3.52e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 61.03 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 593 PEDLEKTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGsmRKTDGKVEvnGDLLMCGYP----WIQNAS---VR 665
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGLGVS--GEVLINGRPldkrSFRKIIgyvPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 DNIIFGspfnkekYDEVVRVCSLKADLdilpagdmteigeRGItlSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVG 745
Cdd:cd03213 90 DDILHP-------TLTVRETLMFAAKL-------------RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398366407 746 KHIMdECLTGM-LANKTRILATHQLS--LIERASRVIVLgTDGQV 787
Cdd:cd03213 148 LQVM-SLLRRLaDTGRTIICSIHQPSseIFELFDKLLLL-SQGRV 190
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1211-1456 |
3.76e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.72 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1211 GEIIFENVDFAYRPGLPI---VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQ-----LG 1282
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1283 LFDLRRKLAIIPQDP--VLFRGTIRKNL--DPFNERTDDELwdalvrggaiAKDDLPEV--KLQKPDEngtHGKMHKFHL 1356
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQE----------AYKKVPELlkLVQLPED---YVKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1357 dqaveeegsnfSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQT---RIVEEFGDcTILCIAHRLKTIVNY-D 1432
Cdd:PRK13645 152 -----------SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINlfeRLNKEYKK-RIIMVTHNMDQVLRIaD 219
|
250 260
....*....|....*....|....
gi 398366407 1433 RILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:PRK13645 220 EVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1213-1453 |
3.97e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTA-----GKILIDNVDI--SQLGLFD 1285
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 LRRKLAIIPQDPVLFRGTIRKN----LDPFNERTDDELwDALVRGGAIAKDDLPEVKlqkpdengthGKMHKFHLDqave 1361
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNvaygVKIVGWRPKLEI-DDIVESALKDADLWDEIK----------HKIHKSALD---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1362 eegsnFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEF--GDCTILCIAHRLKTIV---------- 1429
Cdd:PRK14258 151 -----LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrlsdftaffk 225
|
250 260
....*....|....*....|....*
gi 398366407 1430 -NYDRIlvlekGEVAEFDTPWTLFS 1453
Cdd:PRK14258 226 gNENRI-----GQLVEFGLTKKIFN 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1213-1458 |
4.04e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGLPI---VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG----LFD 1285
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 LRRKLAIIPQDP--VLFRGTIRKNLD--PFNertddelwdalvrggaiAKDDLPEVKlqkpdengthGKMHKFHLDQAVE 1361
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVEREIIfgPKN-----------------FKMNLDEVK----------NYAHRLLMDLGFS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1362 E---EGSNF--SLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRI--VEEFGDCTILCIAHRLKTIVNY-DR 1433
Cdd:PRK13646 136 RdvmSQSPFqmSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYaDE 215
|
250 260
....*....|....*....|....*
gi 398366407 1434 ILVLEKGEVAEFDTPWTLFSQEDSI 1458
Cdd:PRK13646 216 VIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
604-785 |
4.48e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.06 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD---LLMCGYPWIQNASVRDNIIFGSP---FNKE 677
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGarvLFLPQRPYLPLGTLREALLYPATaeaFSDA 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 678 KYDEVVRVCSLkADLdilpAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDEcLTGML 757
Cdd:COG4178 459 ELREALEAVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREEL 532
|
170 180
....*....|....*....|....*...
gi 398366407 758 ANKTRILATHQLSLIERASRVIVLGTDG 785
Cdd:COG4178 533 PGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
597-783 |
4.88e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 61.58 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 597 EKTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLlmcgyPWIQNASVRDNI--IFGSP- 673
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRKKFLRRIgvVFGQKt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 674 -------------FNKEKYDevVRVCSLKADLDILpaGDMTEIGE------RgiTLSGGQKARINLARSVYKKKDIYLFD 734
Cdd:cd03267 105 qlwwdlpvidsfyLLAAIYD--LPPARFKKRLDEL--SELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 735 ------DVLSavDSRVGKHIMDECltgMLANKTRILATHQLSLIER-ASRVIVLGT 783
Cdd:cd03267 179 eptiglDVVA--QENIRNFLKEYN---RERGTTVLLTSHYMKDIEAlARRVLVIDK 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
605-807 |
4.98e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.65 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLL---NAM---------AGSMRKTDGKVEVNGDLLMCGYPWIQ-----NASVRDN 667
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLeeitsgdliVDGLKVNDPKVDERLIRQEAGMVFQQfylfpHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 IIFGsPFNkekydevVRVCSlKADLDILPAGDMTEIG--ERG----ITLSGGQKARINLARSVYKKKDIYLFDDVLSAVD 741
Cdd:PRK09493 98 VMFG-PLR-------VRGAS-KEEAEKQARELLAKVGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 742 SRVgKHimdECLTGM--LANK--TRILATHQLSLIER-ASRVIVLGTDGQVDIGTVDELKAR--NQTLINLLQ 807
Cdd:PRK09493 169 PEL-RH---EVLKVMqdLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNppSQRLQEFLQ 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
619-787 |
5.19e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 619 ITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL------MC--------GYPWiQNA------SVRDNIIFG-SPFNKE 677
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgIClppekrriGYVF-QDArlfphyKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 678 KYDEVVRVCSLKADLDILPagdmteigergITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMD--ECLTG 755
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPylERLAR 176
|
170 180 190
....*....|....*....|....*....|....
gi 398366407 756 MLanKTRIL-ATHQLSLIER-ASRVIVLgTDGQV 787
Cdd:PRK11144 177 EI--NIPILyVSHSLDEILRlADRVVVL-EQGKV 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
605-798 |
5.64e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-----------DLLMCgypwIQN------ASVRDN 667
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelepadrDIAMV----FQNyalyphMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 668 I-----IFGSPfnkekydevvrvcslKADLD--ILPAGDMTEIGE----RGITLSGGQKARINLARSVYKKKDIYLFDDV 736
Cdd:PRK11650 97 MayglkIRGMP---------------KAEIEerVAEAARILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 737 LSAVDS--RVGKHIMDECLTGMLaNKTRILATH-QLSLIERASRVIVLgTDGQVD-IGTVDELKAR 798
Cdd:PRK11650 162 LSNLDAklRVQMRLEIQRLHRRL-KTTSLYVTHdQVEAMTLADRVVVM-NGGVAEqIGTPVEVYEK 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
600-778 |
8.40e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 8.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 600 SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLL------NAMAGSMRkTDGKVEVNGDLLMCgyPWIQNASVRDNI--IFG 671
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFR-VEGKVTFHGKNLYA--PDVDPVEVRRRIgmVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 672 --SPFNKEKYDEV---VRVCSLKADLDILPAGDMTE----------IGERGITLSGGQKARINLARSVYKKKDIYLFDDV 736
Cdd:PRK14243 99 kpNPFPKSIYDNIaygARINGYKGDMDELVERSLRQaalwdevkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 398366407 737 LSAVDSrVGKHIMDECLTGMLANKTRILATHQLsliERASRV 778
Cdd:PRK14243 179 CSALDP-ISTLRIEELMHELKEQYTIIIVTHNM---QQAARV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
572-794 |
1.25e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.39 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 572 KPSASTNKAKRLDNMLKD----RDGP------------------EDLEKtSFRG---FKDLNFDIKKGEFIMITGPIGTG 626
Cdd:COG0488 275 KAKQAQSRIKALEKLEREepprRDKTveirfppperlgkkvlelEGLSK-SYGDktlLDDLSLRIDRGDRIGLIGPNGAG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 627 KSSLLNAMAGSMRKTDGKVEVnGDLLMCGY---------PwiqNASVRDNIIFGSPFNKEKYdevVRvcSLKADLdiLPA 697
Cdd:COG0488 354 KSTLLKLLAGELEPDSGTVKL-GETVKIGYfdqhqeeldP---DKTVLDELRDGAPGGTEQE---VR--GYLGRF--LFS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 698 GDM--TEIGergiTLSGGQKARINLARSVYKKKDIYLFD------DvlsaVDSRvgkhimdECLTGMLAN--KTRILATH 767
Cdd:COG0488 423 GDDafKPVG----VLSGGEKARLALAKLLLSPPNVLLLDeptnhlD----IETL-------EALEEALDDfpGTVLLVSH 487
|
250 260 270
....*....|....*....|....*....|
gi 398366407 768 QLSLIER-ASRVIVLgTDGQVD--IGTVDE 794
Cdd:COG0488 488 DRYFLDRvATRILEF-EDGGVReyPGGYDD 516
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1229-1448 |
1.41e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNEL--TAGKIL---------------------------------I 1273
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1274 DNVDISQLGLFDLRRKLAIIPQDPVLFRGtirknldpfNERTDDELWDALVRGGAIAKDDLPE-VKLqkpdengthgkMH 1352
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYG---------DDTVLDNVLEALEEIGYEGKEAVGRaVDL-----------IE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1353 KFHLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE--EFGDCTILCIAHRLKTIVN 1430
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIED 234
|
250
....*....|....*....
gi 398366407 1431 Y-DRILVLEKGEVAEFDTP 1448
Cdd:TIGR03269 235 LsDKAIWLENGEIKEEGTP 253
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
605-722 |
1.66e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.17 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLmCGYPWIQNASVR------DNIIFgsPFNKEk 678
Cdd:PRK13548 19 DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-ADWSPAELARRRavlpqhSSLSF--PFTVE- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 679 ydEVVRV-----CSLKADLDILPAGDMTEIG-----ERGI-TLSGGQKARINLAR 722
Cdd:PRK13548 95 --EVVAMgraphGLSRAEDDALVAAALAQVDlahlaGRDYpQLSGGEQQRVQLAR 147
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
605-788 |
1.74e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 59.75 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL--------------MCGY-----PWIQNASVR 665
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedararlrarHVGFvfqsfQLLPTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 DNI-----IFGSPFNKEK-YDEVVRVcSLKADLDILPAGdmteigergitLSGGQKARINLARSVYKKKDIYLFDDVLSA 739
Cdd:COG4181 109 ENVmlpleLAGRRDARARaRALLERV-GLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 740 VDSRVGKHIMDecltgML--ANKTR----ILATHQLSLIERASRVIVLGtDGQVD 788
Cdd:COG4181 177 LDAATGEQIID-----LLfeLNRERgttlVLVTHDPALAARCDRVLRLR-AGRLV 225
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
967-1172 |
1.80e-09 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 60.52 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 967 LNLR--AVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMcIVYLPWF-----AIAIP 1039
Cdd:cd18551 69 LDLRrrLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVL-MFLLDWVltlvtLAVVP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1040 FLLVIFVLIAdhyqssgreiKRLEAVQRSF------VYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVV 1113
Cdd:cd18551 148 LAFLIILPLG----------RRIRKASKRAqdalgeLSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAK 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1114 LQRWVGIFLdMVAIAFALIITLLcvtrafpISAA-------SVGVL---LTYVLQLPGLLNTILRAMTQ 1172
Cdd:cd18551 218 IEALIGPLM-GLAVQLALLVVLG-------VGGArvasgalTVGTLvafLLYLFQLITPLSQLSSFFTQ 278
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1229-1442 |
1.90e-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: 59.65 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALyrlneltAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFrgtirknl 1308
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL-------SGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 dpfNERTddEL-WDALVRGG-AIAKD--DLPEVKLQKP-DENGTHGKMHKFhLDQAVEeegsNFSLGERQLLALTRALVR 1383
Cdd:cd03267 101 ---GQKT--QLwWDLPVIDSfYLLAAiyDLPPARFKKRlDELSELLDLEEL-LDTPVR----QLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1384 QSKILILDEATSSVDYETDGKIQTRIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKGRL 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
606-742 |
2.18e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-----------DLLMC--GYPWIQNASVRDNIIFGS 672
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthrsiqqrDICMVfqSYALFPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 673 PFNKEKYDEVV-RVcslKADLDILpagDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDS 742
Cdd:PRK11432 104 KMLGVPKEERKqRV---KEALELV---DLAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
594-795 |
2.33e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.10 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGYPW---------IQN-- 661
Cdd:PRK13633 16 SNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWdirnkagmvFQNpd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 662 -----ASVRDNIIFGsPFNKEKYDEVVRvcsLKADlDILPAGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDD 735
Cdd:PRK13633 96 nqivaTIVEEDVAFG-PENLGIPPEEIR---ERVD-ESLKKVGMYEYRRHAPhLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 736 VLSAVDSRVGKHIMDeclTGMLANK----TRILATHQLSLIERASRVIVLGTDGQVDIGTVDEL 795
Cdd:PRK13633 171 PTAMLDPSGRREVVN---TIKELNKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1229-1456 |
2.44e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDP--VLFRGTIRK 1306
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1307 NL--DPFNERTDDElwdalvrggAIAkddlpevklQKPDEngthgKMHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQ 1384
Cdd:PRK13652 99 DIafGPINLGLDEE---------TVA---------HRVSS-----ALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1385 SKILILDEATSSVDYETDGKI---QTRIVEEFGdCTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELidfLNDLPETYG-MTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1228-1443 |
2.93e-09 |
|
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: 58.82 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1228 IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNE---LTAGKILIDNVDISQlGLFdlRRKLAIIPQDPVLFRG-T 1303
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKP-DQF--QKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1304 IRKNLdpfnertddeLWDALVRGGAIAKDDLPevklQKPDENgthGKMHKFHLDQAVEEEGSNFSLGERQLLALTRALVR 1383
Cdd:cd03234 98 VRETL----------TYTAILRLPRKSSDAIR----KKRVED---VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1384 QSKILILDEATSSVDYETDGKIqTRIVEEF--GDCTILCIAH-------RLktivnYDRILVLEKGEVA 1443
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNL-VSTLSQLarRNRIVILTIHqprsdlfRL-----FDRILLLSSGEIV 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
606-797 |
3.07e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.01 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD-----------LLMCGYPwiQNAS------VRDNI 668
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasRRVASVP--QDTSlsfefdVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 669 IFGSPFNKEKY---DEVVRVCSLKAdldiLPAGDMTEIGERGIT-LSGGQKARINLARSVYKKKDIYLFDDVLSAVDsrV 744
Cdd:PRK09536 99 EMGRTPHRSRFdtwTETDRAAVERA----MERTGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD--I 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 745 GKHIMDECLTGMLAN--KTRILATHQLSLIERASRVIVLGTDGQV-DIG------TVDELKA 797
Cdd:PRK09536 173 NHQVRTLELVRRLVDdgKTAVAAIHDLDLAARYCDELVLLADGRVrAAGppadvlTADTLRA 234
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
604-806 |
3.14e-09 |
|
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: 59.54 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGdLLMCGYPwIQNASVRDNIIFGSP--------FN 675
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG-IDISKLP-LHTLRSRLSIILQDPilfsgsirFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 676 --------KEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVgKH 747
Cdd:cd03288 115 ldpeckctDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-EN 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 748 IMDECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKARNQTLINLL 806
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASL 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
582-893 |
3.19e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.36 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 582 RLDNMLKDRDGpedlektsFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAG--SMRKTDGKV-------------- 645
Cdd:TIGR03269 2 EVKNLTKKFDG--------KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyve 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 646 -----------------EVNGDLLMCGYPWIQNASVRDNIIFGSPF----NKEKYDEVVRVC---------SLKADLDIL 695
Cdd:TIGR03269 74 rpskvgepcpvcggtlePEEVDFWNLSDKLRRRIRKRIAIMLQRTFalygDDTVLDNVLEALeeigyegkeAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 696 pagDMTEIGERgIT-----LSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTGMLANK-TRILATHQL 769
Cdd:TIGR03269 154 ---EMVQLSHR-IThiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGiSMVLTSHWP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 770 SLIERASRVIVLGTDGQV-DIGTVDELKARnqtlinllqFSSQNSEKEDEEQEAVvagelgqlkyESEVKELTELKKKAT 848
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIkEEGTPDEVVAV---------FMEGVSEVEKECEVEV----------GEPIIKVRNVSKRYI 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 398366407 849 EMSQtansGKIvadghtsskeeRAVNSISLKIYREYIKAAVGKWG 893
Cdd:TIGR03269 291 SVDR----GVV-----------KAVDNVSLEVKEGEIFGIVGTSG 320
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1213-1398 |
3.34e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRpGLPIvlkNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVD-----ISQlglfdlr 1287
Cdd:PRK10771 2 LKLTDITWLYH-HLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttpPSR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1288 RKLAIIPQDPVLFRG-TIRKN----LDPfNERTDDELWDALVrggAIAKddlpevklqkpdengthgkmhKFHLDQAVEE 1362
Cdd:PRK10771 71 RPVSMLFQENNLFSHlTVAQNiglgLNP-GLKLNAAQREKLH---AIAR---------------------QMGIEDLLAR 125
|
170 180 190
....*....|....*....|....*....|....*.
gi 398366407 1363 EGSNFSLGERQLLALTRALVRQSKILILDEATSSVD 1398
Cdd:PRK10771 126 LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
594-649 |
3.56e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 59.33 E-value: 3.56e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 594 EDLEKTSFRG-------FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG 649
Cdd:COG1101 5 KNLSKTFNPGtvnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG 67
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
605-787 |
3.99e-09 |
|
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: 58.19 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGY-------------PWIQNASVRDNIif 670
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGiDISTIPLedlrssltiipqdPTLFSGTIRSNL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 gSPFNkeKYDEVVRVCSLKadldilpagdmteIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVgKHIMD 750
Cdd:cd03369 103 -DPFD--EYSDEEIYGALR-------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DALIQ 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 398366407 751 ECLTGMLANKTRILATHQLSLIERASRVIVLgTDGQV 787
Cdd:cd03369 166 KTIREEFTNSTILTIAHRLRTIIDYDKILVM-DAGEV 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
602-735 |
4.26e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.80 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPW-------------------IQNA 662
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagiayvpedrkgeglVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 663 SVRDNIIFGS--------PFNKEKYDEVVRvcSLKADLDILPAGDMTEIGergiTLSGG--QKarINLARSVYKKKDIYL 732
Cdd:COG1129 346 SIRENITLASldrlsrggLLDRRRERALAE--EYIKRLRIKTPSPEQPVG----NLSGGnqQK--VVLAKWLATDPKVLI 417
|
...
gi 398366407 733 FDD 735
Cdd:COG1129 418 LDE 420
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1229-1442 |
4.55e-09 |
|
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: 58.06 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISqlglFDLRRKLAIIPQDPVLFRG-TIRKN 1307
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLPEERGLYPKmKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 LDPFNERTDDELWDALVRggaiAKDDLPEVKLQKpdengthgkmhkfHLDQAVEEegsnFSLGERQLLALTRALVRQSKI 1387
Cdd:cd03269 91 LVYLAQLKGLKKEEARRR----IDEWLERLELSE-------------YANKRVEE----LSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1388 LILDEATSSVDyETDGKIQTRIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:cd03269 150 LILDEPFSGLD-PVNVELLKDVIRELARagKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1230-1444 |
5.13e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKIL-----IDNVDISQLGlfDLRRKLAIIPQDPVlfrgti 1304
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGKLQ--ALRRDIQFIFQDPY------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1305 rKNLDPfNERTDDELWD-----ALVRGGAIAKDD---------LPEVKLQKPDEngthgkmhkfhldqaveeegsnFSLG 1370
Cdd:PRK10261 412 -ASLDP-RQTVGDSIMEplrvhGLLPGKAAAARVawllervglLPEHAWRYPHE----------------------FSGG 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1371 ERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE---EFGdCTILCIAHRLKTIVNYD-RILVLEKGEVAE 1444
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDlqrDFG-IAYLFISHDMAVVERIShRVAVMYLGQIVE 544
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1200-1451 |
6.54e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.18 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1200 EMTPPESWPSMGEIIFENVDFAYRPGlpIVLKNL---------------NLNIKSGEKIGICGRTGAGKSTIMSALYRLN 1264
Cdd:TIGR01257 903 EMEDPEHPEGINDSFFERELPGLVPG--VCVKNLvkifepsgrpavdrlNITFYENQITAFLGHNGAGKTTTLSILTGLL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1265 ELTAGKILIDNVDIsQLGLFDLRRKLAIIPQDPVLFRG-TIRKNLdpfnertddeLWDALVRGGAIAKDDLP-EVKLQkp 1342
Cdd:TIGR01257 981 PPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHI----------LFYAQLKGRSWEEAQLEmEAMLE-- 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1343 dENGTHGKMHkfhldqaveEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIA 1422
Cdd:TIGR01257 1048 -DTGLHHKRN---------EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMST 1117
|
250 260 270
....*....|....*....|....*....|
gi 398366407 1423 HRL-KTIVNYDRILVLEKGEVAEFDTPWTL 1451
Cdd:TIGR01257 1118 HHMdEADLLGDRIAIISQGRLYCSGTPLFL 1147
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1216-1426 |
6.64e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.64 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNEL-----TAGKILIDNVDI--SQLGLFDLRR 1288
Cdd:PRK14243 14 ENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1289 KLAIIPQDPVLFRGTIRKNLdPFNERTD------DELWDALVRGGAIakddLPEVKlqkpdengthgkmhkfhldQAVEE 1362
Cdd:PRK14243 92 RIGMVFQKPNPFPKSIYDNI-AYGARINgykgdmDELVERSLRQAAL----WDEVK-------------------DKLKQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1363 EGSNFSLGERQLLALTRALVRQSKILILDEATSSVDyetdgKIQTRIVEEF-----GDCTILCIAHRLK 1426
Cdd:PRK14243 148 SGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD-----PISTLRIEELmhelkEQYTIIIVTHNMQ 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1229-1423 |
6.94e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.31 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTA-----GKILIDNVDI--SQLGLFDLRRKLAIIPQDPvlfr 1301
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQYP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1302 gtirknlDPFNERT--DDELWDALVRGGAIAKDDLPEV---KLQKP---DEngthgkmhkfhLDQAVEEEGSNFSLGERQ 1373
Cdd:PRK14267 95 -------NPFPHLTiyDNVAIGVKLNGLVKSKKELDERvewALKKAalwDE-----------VKDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398366407 1374 LLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAH 1423
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
606-742 |
7.98e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.17 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG----------------DLLMcgyPWiqnASVRDNII 669
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvegpgaergvvfqnEGLL---PW---RNVQDNVA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 670 FG---SPFNKEKYDEVVRVCSLKADLDilpagdmtEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDS 742
Cdd:PRK11248 93 FGlqlAGVEKMQRLEIAHQMLKKVGLE--------GAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
613-793 |
8.44e-09 |
|
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: 55.84 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 613 KGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKV-EVNGDLLMCGYPWIQNasvrdniifgspfnkekydevvrvcslkad 691
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 692 ldilpagdMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTGMLA-----NKTRILAT 766
Cdd:smart00382 51 --------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLllkseKNLTVILT 122
|
170 180
....*....|....*....|....*..
gi 398366407 767 HQLSLIERaSRVIVLGTDGQVDIGTVD 793
Cdd:smart00382 123 TNDEKDLG-PALLRRRFDRRIVLLLIL 148
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1201-1444 |
9.38e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1201 MTPPESWPSMGEIIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDI-S 1279
Cdd:PRK13536 30 KASIPGSMSTVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1280 QLGLfdLRRKLAIIPQ-DPVLFRGTIRKNLDPF------NERTDDELWDALVRggaIAKddlpevklqkpdengthgkmh 1352
Cdd:PRK13536 108 RARL--ARARIGVVPQfDNLDLEFTVRENLLVFgryfgmSTREIEAVIPSLLE---FAR--------------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1353 kfhLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVD-------YE------TDGK---IQTRIVEEfgdc 1416
Cdd:PRK13536 162 ---LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDpharhliWErlrsllARGKtilLTTHFMEE---- 234
|
250 260
....*....|....*....|....*....
gi 398366407 1417 tilciAHRLktivnYDRILVLEKG-EVAE 1444
Cdd:PRK13536 235 -----AERL-----CDRLCVLEAGrKIAE 253
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
596-795 |
9.75e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.28 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 596 LEKTSFR-GFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-------------------DLLMCG 655
Cdd:PRK10070 35 LEKTGLSlGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkkiAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 656 YPWIQNASVRDNIIFGSPF-------NKEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKK 728
Cdd:PRK10070 115 FALMPHMTVLDNTAFGMELaginaeeRREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 729 DIYLFDDVLSAVDSRVGKHIMDEcLTGMLA--NKTRILATHQLSLIERASRVIVLGTDGQ-VDIGTVDEL 795
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDE-LVKLQAkhQRTIVFISHDLDEAMRIGDRIAIMQNGEvVQVGTPDEI 252
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1210-1452 |
1.29e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEIIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDlrRK 1289
Cdd:PRK11000 1 MASVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVLFrgtirKNLDpfnertddeLWDALVRGGAIAKDDLPEVK---------LQkpdengthgkmhkfhLDQAV 1360
Cdd:PRK11000 77 VGMVFQSYALY-----PHLS---------VAENMSFGLKLAGAKKEEINqrvnqvaevLQ---------------LAHLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1361 EEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETdgKIQTRI----VEEFGDCTILCIAH-RLKTIVNYDRIL 1435
Cdd:PRK11000 128 DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL--RVQMRIeisrLHKRLGRTMIYVTHdQVEAMTLADKIV 205
|
250
....*....|....*..
gi 398366407 1436 VLEKGEVAEFDTPWTLF 1452
Cdd:PRK11000 206 VLDAGRVAQVGKPLELY 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1212-1441 |
1.43e-08 |
|
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: 59.18 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1212 EIIFE--NVDFAYRPGLPIvLKNLNLNIKSGEKIGICGRTGAGKSTIMsalyrlnELTAGkilIDNvDISQLGLFDLRRK 1289
Cdd:TIGR03719 2 QYIYTmnRVSKVVPPKKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLL-------RIMAG---VDK-DFNGEARPQPGIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVL-----FRGT-------IRKNLDPFNE-----RTDDELWDALVRGGAiakddlpevKLQ-KPDENGTHGKM 1351
Cdd:TIGR03719 70 VGYLPQEPQLdptktVRENveegvaeIKDALDRFNEisakyAEPDADFDKLAAEQA---------ELQeIIDAADAWDLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1352 HKfhLDQAVE--------EEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQtRIVEEF-GdcTILCIA 1422
Cdd:TIGR03719 141 SQ--LEIAMDalrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE-RHLQEYpG--TVVAVT 215
|
250 260
....*....|....*....|....*...
gi 398366407 1423 HrlktivnyDR---------ILVLEKGE 1441
Cdd:TIGR03719 216 H--------DRyfldnvagwILELDRGR 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
602-787 |
1.50e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.82 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGYPWIQN---------------ASVR 665
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrEVNAENEKWVRSkvglvfqdpddqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 DNIIFGsPFN----KEKYDEVVRvcslkadlDILPAGDMTEIGERG-ITLSGGQKARINLARSVYKKKDIYLFDDVLSAV 740
Cdd:PRK13647 99 DDVAFG-PVNmgldKDEVERRVE--------EALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398366407 741 DSRvGKHIMDECLTGMLAN-KTRILATHQLSL-IERASRVIVLgTDGQV 787
Cdd:PRK13647 170 DPR-GQETLMEILDRLHNQgKTVIVATHDVDLaAEWADQVIVL-KEGRV 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1229-1448 |
1.59e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.17 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDlrRKLAIIPQDPVLFRG-TIRKN 1307
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 LdpfnertddelwdalvrggAIAKDDLPevKLQKPDENGTHGKMHKF----HLDQAVEEEGSNFSLGERQLLALTRALVR 1383
Cdd:PRK10851 95 I-------------------AFGLTVLP--RRERPNAAAIKAKVTQLlemvQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1384 QSKILILDEATSSVDYETDGKIQT---RIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGEVAEFDTP 1448
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRwlrQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
606-772 |
1.66e-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: 59.38 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAG---SMRKTDGKVEVNGDLLMCGYPWIQNASVRDNIIFgsPFNKEKY-DE 681
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGElwpVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIY--PDSSEDMkRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 682 VVRVCSLKADLDILpagDMTEIGERGI----------TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDE 751
Cdd:TIGR00954 548 GLSDKDLEQILDNV---QLTHILEREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
170 180
....*....|....*....|.
gi 398366407 752 CLTgmlANKTRILATHQLSLI 772
Cdd:TIGR00954 625 CRE---FGITLFSVSHRKSLW 642
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
610-786 |
1.82e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.03 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 610 DIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPWI---QNASVRDniifgspFNKEKYDEVVRVC 686
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIkadYEGTVRD-------LLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 687 SLKADLdILPAGdMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVDS-------RVGKHIMDEcltgmlA 758
Cdd:cd03237 94 YFKTEI-AKPLQ-IEQILDREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlmasKVIRRFAEN------N 165
|
170 180
....*....|....*....|....*....
gi 398366407 759 NKTRILATHQLSLIER-ASRVIVLgtDGQ 786
Cdd:cd03237 166 EKTAFVVEHDIIMIDYlADRLIVF--EGE 192
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
602-768 |
2.17e-08 |
|
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: 56.51 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRK---TDGKVEVNGDLL-------MCGY-----PWIQNASVRD 666
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRkpdqfqkCVAYvrqddILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 667 NIIFGSPF-----NKEKYDEVVRVCSLKADLDILPAGDMTEIGergitLSGGQKARINLARSVYKKKDIYLFDDVLSAVD 741
Cdd:cd03234 101 TLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190
....*....|....*....|....*....|..
gi 398366407 742 SRVGKHIMDecltgMLA-----NKTRILATHQ 768
Cdd:cd03234 176 SFTALNLVS-----TLSqlarrNRIVILTIHQ 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1216-1398 |
2.18e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQ 1295
Cdd:PRK10253 11 EQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1296 dpvlfrgtirkNLDPFNERTDDELwdalvrggaIAKDDLPEVKL----QKPDENGTHGKMHKFHLDQAVEEEGSNFSLGE 1371
Cdd:PRK10253 89 -----------NATTPGDITVQEL---------VARGRYPHQPLftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQ 148
|
170 180
....*....|....*....|....*..
gi 398366407 1372 RQLLALTRALVRQSKILILDEATSSVD 1398
Cdd:PRK10253 149 RQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
594-787 |
2.42e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.94 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSM---RKTDGKVEVNGDLLMC-------------- 654
Cdd:PRK09984 8 EKLAKTfnQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlardirksran 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 655 -GYPWIQ-----NASVRDNIIFG----SPFNKEKYDEVVRVCSLKADLDILPAGDMTEIGERGITLSGGQKARINLARSV 724
Cdd:PRK09984 88 tGYIFQQfnlvnRLSVLENVLIGalgsTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 725 YKKKDIYLFDDVLSAVDSRVGKHIMDeCLTGMLANK--TRILATHQLSLIERASRVIVLGTDGQV 787
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMD-TLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1229-1442 |
2.59e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.61 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQlglfdLRRKLAIIPQDPVLFrgtirknl 1308
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMFQDARLL-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 dPFNERTDDElwdAL-VRGG--AIAKDDLPEVKLQkpdengthgkmhkfhlDQAVEEEGSnFSLGERQLLALTRALVRQS 1385
Cdd:PRK11247 94 -PWKKVIDNV---GLgLKGQwrDAALQALAAVGLA----------------DRANEWPAA-LSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 1386 KILILDEATSSVDYETDGKIQTRIV---EEFGdCTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIEslwQQHG-FTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1229-1453 |
3.27e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.64 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLF------DLRRKLAIIPQDPVLFRG 1302
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnyrdvlEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1303 TIRKNldpfnertddelwdalVRGGAIAKDDLPevklQKPDENGTHGKMHKFHLDQAVEEEGSN----FSLGERQLLALT 1378
Cdd:PRK14271 116 SIMDN----------------VLAGVRAHKLVP----RKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1379 RALVRQSKILILDEATSSVDYETDGKIQTRIVEEFGDCTILCIAHRLKTIVNY-DRILVLEKGEVAEFDTPWTLFS 1453
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1229-1453 |
3.45e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 56.30 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDI-------SQLGLF-DLRRKLAIIPQdpvlf 1300
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsQQKGLIrQLRQHVGFVFQ----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1301 rgtirkNLDPFNERTddeLWDALVRGGAIAKDDLPEVKLQKPDE----NGTHGKMHKFhldqaveeeGSNFSLGERQLLA 1376
Cdd:PRK11264 93 ------NFNLFPHRT---VLENIIEGPVIVKGEPKEEATARAREllakVGLAGKETSY---------PRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1377 LTRALVRQSKILILDEATSSVDYETDGKIQTriveefgdcTILCIAHRLKT--IVNY---------DRILVLEKGEVAEF 1445
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLN---------TIRQLAQEKRTmvIVTHemsfardvaDRAIFMDQGRIVEQ 225
|
....*...
gi 398366407 1446 DTPWTLFS 1453
Cdd:PRK11264 226 GPAKALFA 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
604-734 |
4.03e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.77 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMcGY-----PWIQNASVRDNIIFGspfNKEK 678
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRI-GYlpqepPLDDDLTVLDTVLDG---DAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 679 YDEVVRVCSLKADLDILPAgDMTEIGER-----------------------GI----------TLSGGQKARINLARSVY 725
Cdd:COG0488 90 RALEAELEELEAKLAEPDE-DLERLAELqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALL 168
|
....*....
gi 398366407 726 KKKDIYLFD 734
Cdd:COG0488 169 SEPDLLLLD 177
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1230-1465 |
4.22e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKI--LIDNVDIS------QLGLFDLRRKLAIIPQDpvlfr 1301
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlyLGKEVTFNgpkssqEAGIGIIHQELNLIPQL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1302 gTIRKNLDPFNERTDdelwdalvRGGAIakddlpevklqkpdengTHGKMH------------KFHLDQAVEEegsnFSL 1369
Cdd:PRK10762 95 -TIAENIFLGREFVN--------RFGRI-----------------DWKKMYaeadkllarlnlRFSSDKLVGE----LSI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSV-DYETDGKIqtRIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKG----- 1440
Cdd:PRK10762 145 GEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF--RVIRELKSqgRGIVYISHRLKEIFEIcDDVTVFRDGqfiae 222
|
250 260
....*....|....*....|....*.
gi 398366407 1441 -EVAEFDtpwtlfsqEDSIFRSMCSR 1465
Cdd:PRK10762 223 rEVADLT--------EDSLIEMMVGR 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1230-1476 |
4.64e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSAL--------YrlneltAGKILIDNV-----DIS---QLGLFDLRRKLAII 1293
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphgsY------EGEILFDGEvcrfkDIRdseALGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1294 PQdpvLfrgTIRKNLDPFNERTddelwdalvRGGAIakddlpevklqkpDENGTHGK----MHKFHLDQAVEEEGSNFSL 1369
Cdd:NF040905 91 PY---L---SIAENIFLGNERA---------KRGVI-------------DWNETNRRarelLAKVGLDESPDTLVTDIGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1370 GERQLLALTRALVRQSKILILDEATSSVDyETDGKIQTRIVEEFGDCTILC--IAHRLKTIVNY-DRILVLEKGEVAE-F 1445
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALN-EEDSAALLDLLLELKAQGITSiiISHKLNEIRRVaDSITVLRDGRTIEtL 221
|
250 260 270
....*....|....*....|....*....|.
gi 398366407 1446 DTPWTLFSqEDSIFRSMCSRsgivenDFENR 1476
Cdd:NF040905 222 DCRADEVT-EDRIIRGMVGR------DLEDR 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
595-781 |
5.31e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 55.07 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 595 DLEKTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLL----------------MCGYP 657
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVkepaearrrlgfvsdsTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 658 WIqnaSVRDNIIFGSPFNKEKYDEvvrvcsLKADLDILpaGDMTEIGE----RGITLSGGQKARINLARSVYKKKDIYLF 733
Cdd:cd03266 92 RL---TARENLEYFAGLYGLKGDE------LTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 734 D------DVLSAVDSR-VGKHIMDEcltgmlaNKTRILATHQLSLIER-ASRVIVL 781
Cdd:cd03266 161 DepttglDVMATRALReFIRQLRAL-------GKCILFSTHIMQEVERlCDRVVVL 209
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
967-1133 |
5.43e-08 |
|
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: 56.30 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 967 LNLRAVKRILHTPMSYIDTTPLGRILNRFTkDTDSLDNELTE-SLRLMTSQFANIVGVCVMCIVYLPWFAIA---IPFLL 1042
Cdd:cd18570 77 LILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISStTISLFLDLLMVIISGIILFFYNWKLFLITlliIPLYI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1043 VIFVLIADHYQSSGREIKRLEAVQRSfvynNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFL 1122
Cdd:cd18570 156 LIILLFNKPFKKKNREVMESNAELNS----YLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIK 231
|
170
....*....|.
gi 398366407 1123 DMVAIAFALII 1133
Cdd:cd18570 232 GLISLIGSLLI 242
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
594-796 |
5.92e-08 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 55.07 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKT--SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMC---------GYPWiQNA 662
Cdd:cd03265 4 ENLVKKygDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVReprevrrriGIVF-QDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 663 SV------RDNI-IFGSPFN------KEKYDEVVRVcslkadLDILPAGDmteigERGITLSGGQKARINLARSVYKKKD 729
Cdd:cd03265 83 SVddeltgWENLyIHARLYGvpgaerRERIDELLDF------VGLLEAAD-----RLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 730 IYLFDDVLSAVDSRVGKHIMdECLTGMLA--NKTRILATHQLSLIER-ASRVIVLGTDGQVDIGTVDELK 796
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVW-EYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEELK 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1210-1442 |
6.55e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.51 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEII-FENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRR 1288
Cdd:PRK13647 1 MDNIIeVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1289 KLAIIPQDP--VLFRGTIRKNL--DPFNERTDDELWDALVRggaiakDDLPEVKLQKPDENGTHgkmhkfHLdqaveeeg 1364
Cdd:PRK13647 80 KVGLVFQDPddQVFSSTVWDDVafGPVNMGLDKDEVERRVE------EALKAVRMWDFRDKPPY------HL-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1365 snfSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTrIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:PRK13647 140 ---SYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME-ILDRLHNqgKTVIVATHDVDLAAEWaDQVIVLKEGR 215
|
.
gi 398366407 1442 V 1442
Cdd:PRK13647 216 V 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
602-778 |
6.65e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.55 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMaGSMRKTDGKVEVNGDLLMCGY----PWIQNASVR------------ 665
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYNGHniysPRTDTVDLRkeigmvfqqpnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 ------DNIIFGSPFN----KEKYDEVVRVcSLKAdldilpAGDMTEIGER----GITLSGGQKARINLARSVYKKKDIY 731
Cdd:PRK14239 98 fpmsiyENVVYGLRLKgikdKQVLDEAVEK-SLKG------ASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 398366407 732 LFDDVLSAVDSRVGKHImDECLTGMLANKTRILATHQLsliERASRV 778
Cdd:PRK14239 171 LLDEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSM---QQASRI 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
605-802 |
7.46e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.47 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG--------DLLMC----GYPWiQNA-------SVR 665
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVrktvGIVF-QNPddqlfapTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 DNIIFGsPFN----KEKYDEVVRvcslkadlDILPAGDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAV 740
Cdd:PRK13639 98 EDVAFG-PLNlglsKEEVEKRVK--------EALKAVGMEGFENKPPhHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 741 DSRVGKHIM----DECLTGMlankTRILATHQLSLIER-ASRVIVLGTDGQVDIGTVDELKARNQTL 802
Cdd:PRK13639 169 DPMGASQIMkllyDLNKEGI----TIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
939-1174 |
7.49e-08 |
|
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: 55.64 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 939 SFFVFAAFIFMNGQFT-----ILCAMGIMASKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLM 1013
Cdd:cd18557 38 LALILLAIYLLQSVFTfvryyLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1014 TSQFANIVGVCVMcIVYLPW-----FAIAIPFLLVIFVLiadhyqsSGREIKRLEA-VQRSFVYNN--LNEVLGGMDTIK 1085
Cdd:cd18557 118 LRNILQVIGGLII-LFILSWkltlvLLLVIPLLLIASKI-------YGRYIRKLSKeVQDALAKAGqvAEESLSNIRTVR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1086 AYRSQERFLAKSDfliNKMNEAGYLVVVLQRWVGIF--LDMVAIAFALIITLLCVTRAFPISAASVGVLLTYVL------ 1157
Cdd:cd18557 190 SFSAEEKEIRRYS---EALDRSYRLARKKALANALFqgITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILytimva 266
|
250 260
....*....|....*....|.
gi 398366407 1158 ----QLPGLLNTILRAMTQTE 1174
Cdd:cd18557 267 ssvgGLSSLLADIMKALGASE 287
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
896-1182 |
7.89e-08 |
|
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: 55.55 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 896 ALPLYAILVVGTTFCSLFSSVWLSYWTENKFKNRPPS---FYMGLYSFFVFAAFIFMNGQFTIlcaMGIMASKWL-NLRA 971
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSgllIIALLFLALNLVNWVASRLRIYL---MAKVGQRILyDLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 972 --VKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAIA----IPFLLVIF 1045
Cdd:cd18545 78 dlFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVtlavLPLLVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1046 VLIADHYQSSGREIKRleavQRSFVYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQRWVGIFLDMV 1125
Cdd:cd18545 158 FLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1126 -AIAFALIItLLCVTRAFPIsAASVGVL---LTYV-------LQLPGLLNTILRAMTqtendmnSAER 1182
Cdd:cd18545 234 sALGTALVY-WYGGKLVLGG-AITVGVLvafIGYVgrfwqpiRNLSNFYNQLQSAMA-------SAER 292
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1229-1441 |
9.64e-08 |
|
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: 55.25 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNvdisqlglfdlrrKLAIIPQDPVLFRGTIRKNL 1308
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 dPFNERTDDELWDALVRGGAIAKDdlpevKLQKPDENGThgkmhkfhldqAVEEEGSNFSLGERQLLALTRALVRQSKIL 1388
Cdd:cd03291 119 -IFGVSYDEYRYKSVVKACQLEED-----ITKFPEKDNT-----------VLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1389 ILDEATSSVDYETDGKI-QTRIVEEFGDCTILCIAHRLKTIVNYDRILVLEKGE 1441
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
594-791 |
1.14e-07 |
|
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: 52.82 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKtSFRGF---KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLlmcgypwIQNASVRDNIif 670
Cdd:cd03216 4 RGITK-RFGGVkalDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-------VSFASPRDAR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 gspfnkekydevvrvcslkadldilpagdmteigERGIT----LSGGQKARINLARSVYKKKDIYLFDD---VLSAVDS- 742
Cdd:cd03216 74 ----------------------------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEptaALTPAEVe 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 398366407 743 RVGKHImdecltGMLAN--KTRILATHQLSLIER-ASRVIVLgTDGQVdIGT 791
Cdd:cd03216 120 RLFKVI------RRLRAqgVAVIFISHRLDEVFEiADRVTVL-RDGRV-VGT 163
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
606-774 |
1.30e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.20 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGsMRKTDGkvevnGDLLMCGYPWIQNA--------------------SVR 665
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLG-LTHPDA-----GSISLCGEPVPSRArharqrvgvvpqfdnldpdfTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 DNI-IFGSPFNKEKYDEVVRVCSL--------KADldilpagdmTEIGErgitLSGGQKARINLARSVYKKKDIYLFDDV 736
Cdd:PRK13537 99 ENLlVFGRYFGLSAAAARALVPPLlefaklenKAD---------AKVGE----LSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 398366407 737 LSAVDSRvGKHIMDECLTGMLAN-KTRILATHQLSLIER 774
Cdd:PRK13537 166 TTGLDPQ-ARHLMWERLRSLLARgKTILLTTHFMEEAER 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1231-1443 |
1.39e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1231 KNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD-LRRKLAIIPQDpvlfRGTIRKNLD 1309
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPED----RQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1310 -PFNertddelWDALvrggAIAKDDLPeVKLQKPDENGTHGKMH-----KF-HLDQAVEeegsNFSLGERQLLALTRALV 1382
Cdd:PRK15439 356 aPLA-------WNVC----ALTHNRRG-FWIKPARENAVLERYRralniKFnHAEQAAR----TLSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1383 RQSKILILDEATSSVDYETDGKIQT---RIVEEfgDCTILCIAHRLKTIVNY-DRILVLEKGEVA 1443
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQlirSIAAQ--NVAVLFISSDLEEIEQMaDRVLVMHQGEIS 482
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1229-1398 |
1.46e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQL---GLFDLR-RKLAIIPQDPVLfrgti 1304
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRnQKLGFIYQFHHL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1305 rknLDPFNERTDDELwdALVRGGAiakddlpevklqKPDE--NGTHGKMHKFHLDQAVEEEGSNFSLGERQLLALTRALV 1382
Cdd:PRK11629 99 ---LPDFTALENVAM--PLLIGKK------------KPAEinSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170
....*....|....*.
gi 398366407 1383 RQSKILILDEATSSVD 1398
Cdd:PRK11629 162 NNPRLVLADEPTGNLD 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
604-769 |
1.52e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVngdllmCGYPwiQNASVRDNIIFGSPFNKE------ 677
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI------LGQP--TRQALQKNLVAYVPQSEEvdwsfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 678 ----------KYDEVVRVCSLKA-DLDILPAG----DMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFDDVLSAVD 741
Cdd:PRK15056 95 vlvedvvmmgRYGHMGWLRRAKKrDRQIVTAAlarvDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190
....*....|....*....|....*....|
gi 398366407 742 SRVGKHIMDecLTGMLAN--KTRILATHQL 769
Cdd:PRK15056 175 VKTEARIIS--LLRELRDegKTMLVSTHNL 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
605-741 |
1.55e-07 |
|
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: 54.09 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DL----------LMCGY-PwiQNAS------VRD 666
Cdd:cd03218 17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqDItklpmhkrarLGIGYlP--QEASifrkltVEE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 667 NIIFGSPFNKEKYDEVV-RVCSLKADLDILPAGDmteigERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVD 741
Cdd:cd03218 95 NILAVLEIRGLSKKEREeKLEELLEEFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
594-800 |
1.74e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKtSFRG---FKDLNFDIKKGEFIMITGPIGTGKSSLLNAM-------AGSMRKtdGKVEVNGDLLM---------- 653
Cdd:PRK11264 7 KNLVK-KFHGqtvLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRV--GDITIDTARSLsqqkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 654 ---CGYPWiQN------ASVRDNIIFGsPF--NKEKYDEVV-RVCSLKADLDIlpAGDMTEIGERgitLSGGQKARINLA 721
Cdd:PRK11264 84 rqhVGFVF-QNfnlfphRTVLENIIEG-PVivKGEPKEEATaRARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 722 RSVYKKKDIYLFDDVLSAVDSR-VGkhimdECLTGM--LA--NKTRILATHQLSLI-ERASRVIVLGTDGQVDIGTVDEL 795
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPElVG-----EVLNTIrqLAqeKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
|
....*
gi 398366407 796 KARNQ 800
Cdd:PRK11264 232 FADPQ 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
602-794 |
2.31e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD------------------LLMCGYPWIQNAS 663
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlknrevpflrrqigMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 664 VRDNIIFGSPFNKEKYDEVVRVCSlkADLDilPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSR 743
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVS--AALD--KVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 398366407 744 VGKHIMDECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQVDIGTVDE 794
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
602-781 |
2.48e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.06 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-------------DL-----LMCGYPWIQ--N 661
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkKLrkkvsLVFQFPEAQlfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 662 ASVRDNIIFGsPFN--------KEKYDEVVRVCSLKADLdilpagdmteIGERGITLSGGQKARINLARSVYKKKDIYLF 733
Cdd:PRK13641 101 NTVLKDVEFG-PKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398366407 734 DDVLSAVDSRVGKHIMDECLTGMLANKTRILATHQLSLI-ERASRVIVL 781
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVL 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1212-1442 |
2.55e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.32 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1212 EIIFENVDFAYRPGLPIVLK---NLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKI---LIDNVDISQLGLF- 1284
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1285 --------------------DLRRKLAIIPQ--DPVLFRGTIRKNL--DPFNERTDDElwDALVRGGAIAK-DDLPEVKL 1339
Cdd:PRK13651 82 kvleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRAAKYIElVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1340 QKpdengthgkmhkfhldqaveeegSNFSL--GERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFGDC- 1416
Cdd:PRK13651 160 QR-----------------------SPFELsgGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQg 215
|
250 260
....*....|....*....|....*...
gi 398366407 1417 -TILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:PRK13651 216 kTIILVTHDLDNVLEWtKRTIFFKDGKI 243
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
602-794 |
2.67e-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: 52.33 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAmagsmrktdgkvevngdllmCGYpwiqnASVRDNIIFGSPfnKEKYDE 681
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--------------------GLY-----ASGKARLISFLP--KFSRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 682 VVRVCSLKADLDiLPAGDMTeIGERGITLSGGQKARINLARSVYK--KKDIYLFDDVLSAVDSRVGKHIMdECLTGMLAN 759
Cdd:cd03238 62 LIFIDQLQFLID-VGLGYLT-LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQLL-EVIKGLIDL 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 398366407 760 K-TRILATHQLSLIERASRVIVLGTDGQVDIGTVDE 794
Cdd:cd03238 139 GnTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVF 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
610-781 |
2.76e-07 |
|
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: 52.19 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 610 DIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDllmcgypwiqnasvrdniifgSPFNKEKYdevvrvcslk 689
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI---------------------TPVYKPQY---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 690 adldilpagdmteigergITLSGGQKARINLARSVYKKKDIYLFDDVLSAVD-------SRVGKHIMDEcltgmlANKTR 762
Cdd:cd03222 70 ------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKTA 125
|
170 180
....*....|....*....|
gi 398366407 763 ILATHQLSLIERAS-RVIVL 781
Cdd:cd03222 126 LVVEHDLAVLDYLSdRIHVF 145
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1228-1471 |
2.78e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1228 IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDnvdisqlglfdlrRKLAIIPQDPVLFRGTIRKN 1307
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1308 LDPFNERTDDELWDAlVRGGAIAKD--DLPevklqkpdeNGthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVRQS 1385
Cdd:PTZ00243 741 ILFFDEEDAARLADA-VRVSQLEADlaQLG---------GG---------LETEIGEKGVNLSGGQKARVSLARAVYANR 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1386 KILILDEATSSVdyetDGKIQTRIVEEF------GDCTILCiAHRLKTIVNYDRILVLEKGEVaEFDTPWTLFSQEdSIF 1459
Cdd:PTZ00243 802 DVYLLDDPLSAL----DAHVGERVVEECflgalaGKTRVLA-THQVHVVPRADYVVALGDGRV-EFSGSSADFMRT-SLY 874
|
250
....*....|..
gi 398366407 1460 RSMcsRSGIVEN 1471
Cdd:PTZ00243 875 ATL--AAELKEN 884
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
210-486 |
2.83e-07 |
|
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: 54.09 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 210 SIVFAILANCTSGFNPMITKRLIEFVEEKAIFHSMHVnkgigYAIGACLMMFVNGLTFnhFFHTSQLTGVQAKSI--LTK 287
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLW-----IALLLLLLALLRALLS--YLRRYLAARLGQRVVfdLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 288 AAMKKM--FNASNYARHcfPNGKVTSFVTTDLARIE---FALSFQPFLAGFpAILAICIVLLIVNLgPIALVgigiffgg 362
Cdd:cd07346 77 DLFRHLqrLSLSFFDRN--RTGDLMSRLTSDVDAVQnlvSSGLLQLLSDVL-TLIGALVILFYLNW-KLTLV-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 363 ffiSLFAFKLILGF-----RIAANIFTDARVTM------MREVLNNIKMIKYYTWEDAYEKNIQDIRTKEISKVRKMQLS 431
Cdd:cd07346 145 ---ALLLLPLYVLIlryfrRRIRKASREVRESLaelsafLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARL 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 432 RNFLIAMAMSLPSIAS-LVTFLAMYKVNKGGRQPGNIFASLSLfqvlsLQMFFLPI 486
Cdd:cd07346 222 SALFSPLIGLLTALGTaLVLLYGGYLVLQGSLTIGELVAFLAY-----LGMLFGPI 272
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
597-794 |
4.21e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.51 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 597 EKTSF--RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-----------DL-----LMCGYPW 658
Cdd:PRK13637 14 EGTPFekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsDIrkkvgLVFQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 659 IQ--NASVRDNIIFGsPFNKEKYDEVV--RVcslKADLDILPAgDMTEIGERG-ITLSGGQKARINLARSVYKKKDIYLF 733
Cdd:PRK13637 94 YQlfEETIEKDIAFG-PINLGLSEEEIenRV---KRAMNIVGL-DYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 734 DDVLSAVDSRvGKhimDECLTGMLA-----NKTRILATHQLSLIER-ASRVIVLGTDGQVDIGTVDE 794
Cdd:PRK13637 169 DEPTAGLDPK-GR---DEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
578-810 |
4.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 578 NKAKRLDNMLKDRDGPEDLEKtsfrgFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYP 657
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNQ-----LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 658 W---------IQN-------ASVRDNIIFGSPFNKEKYDEVVRvcslKADLDILPAGDMTEIGERGITLSGGQKARINLA 721
Cdd:PRK13642 77 WnlrrkigmvFQNpdnqfvgATVEDDVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 722 RSVYKKKDIYLFDDVLSAVDSRVGKHIMDecLTGMLANK---TRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKAR 798
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
250
....*....|....*
gi 398366407 799 NQTLINL---LQFSS 810
Cdd:PRK13642 231 SEDMVEIgldVPFSS 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
604-787 |
4.71e-07 |
|
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: 52.78 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGK-VEVNG---------DL----------LMCGYPwiQNAS 663
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwELrkriglvspaLQLRFP--RDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 664 VRDNII---FGSPFNKEKYDEVVRvcsLKAD--LDILpagDMTEIGERGI-TLSGGQKARINLARSVYKKKDIYLFD--- 734
Cdd:COG1119 97 VLDVVLsgfFDSIGLYREPTDEQR---ERARelLELL---GLAHLADRPFgTLSQGEQRRVLIARALVKDPELLILDept 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 735 ---------DVLSAVDsrvgkHIMDEcltgmlANKTRILATHQLS-LIERASRVIVLgTDGQV 787
Cdd:COG1119 171 agldlgareLLLALLD-----KLAAE------GAPTLVLVTHHVEeIPPGITHVLLL-KDGRV 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1200-1446 |
5.39e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.87 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1200 EMTPPESwPSMGEIIFENVDFAyRPGlpiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDN--VD 1277
Cdd:COG1129 243 DLFPKRA-AAPGEVVLEVEGLS-VGG---VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1278 IS------QLGLF----DlRRKLAIIPQDPV--------LFRGTIRKNLDPFNERTD-DELWDALvrggaiakddlpEVK 1338
Cdd:COG1129 318 IRsprdaiRAGIAyvpeD-RKGEGLVLDLSIrenitlasLDRLSRGGLLDRRRERALaEEYIKRL------------RIK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1339 LQkpdengthgkmhkfHLDQAVeeegSNFSLGERQLLALTRALVRQSKILILDEATSSVD----YEtdgkIQtRIVEEFG 1414
Cdd:COG1129 385 TP--------------SPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakAE----IY-RLIRELA 441
|
250 260 270
....*....|....*....|....*....|....*.
gi 398366407 1415 D--CTILCIAHRLKTIVNY-DRILVLEKGE-VAEFD 1446
Cdd:COG1129 442 AegKAVIVISSELPELLGLsDRILVMREGRiVGELD 477
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
605-787 |
5.56e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.93 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAgSMRKTDGKVEVNGDLL--MCGYPW------------IQNASVRDNIif 670
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSWnsVPLQKWrkafgvipqkvfIFSGTFRKNL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 671 gSPFNKEKYDEVVRVCS---LKADLDILPAGDMTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSrVGKH 747
Cdd:cd03289 98 -DPYGKWSDEEIWKVAEevgLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398366407 748 IMDECLTGMLANKTRILATHQLSLIERASRVIVLgTDGQV 787
Cdd:cd03289 176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVI-EENKV 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
594-797 |
6.21e-07 |
|
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: 52.05 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKtSFRGFK---DLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLmCGYP------------- 657
Cdd:cd03219 4 RGLTK-RFGGLValdDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPpheiarlgigrtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 658 ----WIQNASVRDNIIFGSPFNK-----------------EKYDEVVRVCSLKADLDiLPAGdmteigergiTLSGGQKA 716
Cdd:cd03219 82 qiprLFPELTVLENVMVAAQARTgsglllararreerearERAEELLERVGLADLAD-RPAG----------ELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 717 RINLARSVYKKKDIYLFDDVLSAVdSRVGKHIMDECLTGMLANKTRILAT-HQLSLIER-ASRVIVLgTDGQVdI--GTV 792
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGL-NPEETEELAELIRELRERGITVLLVeHDMDVVMSlADRVTVL-DQGRV-IaeGTP 227
|
....*
gi 398366407 793 DELKA 797
Cdd:cd03219 228 DEVRN 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
600-781 |
6.27e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 52.32 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 600 SFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAM-------------AGS---------------MRKTDGKVEVNGDL 651
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdsgqlniAGHqfdfsqkpsekairlLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 652 lmcgypWiQNASVRDNIIfGSP-----FNKEKYDEvvrvcslKADlDILPAGDMTEIGER-GITLSGGQKARINLARSVY 725
Cdd:COG4161 94 ------W-PHLTVMENLI-EAPckvlgLSKEQARE-------KAM-KLLARLRLTDKADRfPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 726 KKKDIYLFDDVLSAVD----SRVGKHIMDECLTGMlankTRILATHQLSLIER-ASRVIVL 781
Cdd:COG4161 158 MEPQVLLFDEPTAALDpeitAQVVEIIRELSQTGI----TQVIVTHEVEFARKvASQVVYM 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1244-1456 |
6.39e-07 |
|
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: 53.18 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1244 GICGRTGAGKSTIMSALYRLNELTAGKILIDN---VDiSQLGLFdL---RRKLAIIPQDPVLF-RGTIRKNLD------P 1310
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQD-SARGIF-LpphRRRIGYVFQEARLFpHLSVRGNLLygrkraP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1311 FNERTDDelWDALVRGGAIAkdDLpevklqkpdengthgkmhkfhLDQAVEeegsNFSLGERQLLALTRALVRQSKILIL 1390
Cdd:COG4148 107 RAERRIS--FDEVVELLGIG--HL---------------------LDRRPA----TLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 1391 DEATSSVDYETDGKIQ---TRIVEEFgDCTILCIAH------RLKtivnyDRILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:COG4148 158 DEPLAALDLARKAEILpylERLRDEL-DIPILYVSHsldevaRLA-----DHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
597-778 |
7.23e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 597 EKTSFRGFKDLnfdIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTD--GKVEVNG-----------------DLLmcgYP 657
Cdd:PLN03211 80 ERTILNGVTGM---ASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkptkqilkrtgfvtqdDIL---YP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 658 WIqnaSVRDNIIFGS----PFNKEKYDEVVRVCSLKADLDILPAGDmTEIGE---RGItlSGGQKARINLARSVYKKKDI 730
Cdd:PLN03211 154 HL---TVRETLVFCSllrlPKSLTKQEKILVAESVISELGLTKCEN-TIIGNsfiRGI--SGGERKRVSIAHEMLINPSL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398366407 731 YLFDDVLSAVDSRVGKHIMdecLT-GMLANKTRILAThqlSLIERASRV 778
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLV---LTlGSLAQKGKTIVT---SMHQPSSRV 270
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
602-811 |
8.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.43 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVnGDLLMCG-------------------YPWIQ-- 660
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSStskqkeikpvrkkvgvvfqFPESQlf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 661 NASVRDNIIFGSPFNKEKYDEVVRVCSLKADLdilpAGDMTEIGERG-ITLSGGQKARINLARSVYKKKDIYLFDDVLSA 739
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEM----VGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 740 VDSRVGKHIMDECLTGMLANKTRILATHQLS----------LIERAsRVIVLGTDGQVdIGTVDELKARNQTLINLLQFS 809
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDdvadyadyvyLLEKG-HIISCGTPSDV-FQEVDFLKAHELGVPKATHFA 252
|
..
gi 398366407 810 SQ 811
Cdd:PRK13643 253 DQ 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1229-1409 |
8.49e-07 |
|
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: 51.34 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIIPQDPVLFRGTIRKNL 1308
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1309 DPFNERTDDE-LWDALVRGGAIAKDDLPEVKLqkpdengthgkmhkfhldqaveeegsnfSLGERQLLALTRALVRQSKI 1387
Cdd:cd03231 95 RFWHADHSDEqVEEALARVGLNGFEDRPVAQL----------------------------SAGQQRRVALARLLLSGRPL 146
|
170 180
....*....|....*....|..
gi 398366407 1388 LILDEATSSVDYETDGKIQTRI 1409
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAM 168
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
605-801 |
1.03e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 52.50 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG-DLLMCGYPWIQNAsvRDNI--IFgSPFN----KE 677
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqDLTALSEKELRKA--RRQIgmIF-QHFNllssRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 678 KYDEVvrvcSLKADLDILPAGdmtEIGER--------GIT---------LSGGQKARINLARSVYKKKDIYLFDDVLSAV 740
Cdd:PRK11153 99 VFDNV----ALPLELAGTPKA---EIKARvtellelvGLSdkadrypaqLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 741 DSRVGKHIMDecltgMLA--NK----TRILATHQLSLIER-ASRVIVLGtDGQ-VDIGTVDELKARNQT 801
Cdd:PRK11153 172 DPATTRSILE-----LLKdiNRelglTIVLITHEMDVVKRiCDRVAVID-AGRlVEQGTVSEVFSHPKH 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
605-787 |
1.24e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSS---LLNAMAGSMRKTDGKVEVNGDLLMCGYPW---------IQN-------ASVR 665
Cdd:PRK13640 24 NDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWdirekvgivFQNpdnqfvgATVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 DNIIFGSPFNKEKYDEVVRVCSlkadlDILPAGDMTE-IGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRV 744
Cdd:PRK13640 104 DDVAFGLENRAVPRPEMIKIVR-----DVLADVGMLDyIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398366407 745 GKHIMDECLTGMLANKTRILA-THQLSLIERASRVIVLgTDGQV 787
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISiTHDIDEANMADQVLVL-DDGKL 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1214-1455 |
1.50e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1214 IFENVDFAYrPGlPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAII 1293
Cdd:PRK10575 13 ALRNVSFRV-PG-RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1294 PQdpvlfrgtirkNLDPFNERTDDELwdalvrggaIAKDDLPevklqkpdengTHGKMHKF------HLDQAVEEEG--- 1364
Cdd:PRK10575 91 PQ-----------QLPAAEGMTVREL---------VAIGRYP-----------WHGALGRFgaadreKVEEAISLVGlkp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1365 ------SNFSLGERQLLALTRALVRQSKILILDEATSSVD----YETDGKIQtRIVEEFGdCTILCIAHRLKTIVNY-DR 1433
Cdd:PRK10575 140 lahrlvDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVH-RLSQERG-LTVIAVLHDINMAARYcDY 217
|
250 260
....*....|....*....|..
gi 398366407 1434 ILVLEKGEVAEFDTPWTLFSQE 1455
Cdd:PRK10575 218 LVALRGGEMIAQGTPAELMRGE 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
605-649 |
1.58e-06 |
|
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: 50.90 E-value: 1.58e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG 649
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG 61
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
604-787 |
2.09e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.93 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDI-----------------KKGEFIMITGPIGTGKSSLLNAMAGsmRKTDGKVEvnGDLLMCGYPWIQN----- 661
Cdd:cd03232 6 WKNLNYTVpvkggkrqllnnisgyvKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT--GEILINGRPLDKNfqrst 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 662 ASVRDNIIFgSPFNKekydevVRVC-SLKADLdilpagdmteigeRGITLSggQKARINLARSVYKKKDIYLFDDVLSAV 740
Cdd:cd03232 82 GYVEQQDVH-SPNLT------VREAlRFSALL-------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 398366407 741 DSRVGKHIMdeCLTGMLANKTR-ILAT-HQLS--LIERASRVIVLGTDGQV 787
Cdd:cd03232 140 DSQAAYNIV--RFLKKLADSGQaILCTiHQPSasIFEKFDRLLLLKRGGKT 188
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1213-1456 |
2.26e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.04 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1213 IIFENVDFAYRPGlPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLglfdLRRKL-A 1291
Cdd:PRK15056 7 IVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1292 IIPQD-------PVLFR-----------GTIRKNLDPFNERTDDelwdalvrggAIAKDDLPEVKLQKPDEngthgkmhk 1353
Cdd:PRK15056 82 YVPQSeevdwsfPVLVEdvvmmgryghmGWLRRAKKRDRQIVTA----------ALARVDMVEFRHRQIGE--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1354 fhldqaveeegsnFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIqTRIVEEFGD--CTILCIAHRLKTIVNY 1431
Cdd:PRK15056 143 -------------LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI-ISLLRELRDegKTMLVSTHNLGSVTEF 208
|
250 260
....*....|....*....|....*
gi 398366407 1432 DRILVLEKGEVAEFDTPWTLFSQED 1456
Cdd:PRK15056 209 CDYTVMVKGTVLASGPTETTFTAEN 233
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
933-1157 |
3.17e-06 |
|
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: 50.62 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 933 FYMGLYSFFVFAafiFMNGQFTILC------AMGIMAsKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNEL 1006
Cdd:cd18572 35 FYRAVLLLLLLS---VLSGLFSGLRggcfsyAGTRLV-RRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1007 TESLRLMTSQFANIVGVCVMCiVYLPWF-----AIAIPFLLVIFVLIADHYQSSGREIKRLEAVQRSFVynnlNEVLGGM 1081
Cdd:cd18572 111 STNLNVFLRNLVQLVGGLAFM-FSLSWRltllaFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVA----EEALSNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1082 DTIKAY----RSQERFLAKSD--FLINKMNEAGYLVVVlqrWVGIFLDMVAIAFALII-TLLCVTRafpisAASVGVLLT 1154
Cdd:cd18572 186 RTVRSFateeREARRYERALDkaLKLSVRQALAYAGYV---AVNTLLQNGTQVLVLFYgGHLVLSG-----RMSAGQLVT 257
|
...
gi 398366407 1155 YVL 1157
Cdd:cd18572 258 FML 260
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
611-795 |
3.24e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 611 IKKGEFIMITGPIGTGKSSLLNAMAGSMRK---TDGKVEVNGDLL-------MCGYP-----WIQNASVRDNIIFGSPF- 674
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIdakemraISAYVqqddlFIPTLTVREHLMFQAHLr 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 675 ---NKEKYDEVVRVCSLKADLDILPAGDmTEIGERGIT--LSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:TIGR00955 128 mprRVTKKEKRERVDEVLQALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398366407 750 dECLTGmLANK--TRILATHQLS--LIERASRVIVLGTDGQVDIGTVDEL 795
Cdd:TIGR00955 207 -QVLKG-LAQKgkTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
594-734 |
3.46e-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: 49.74 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 594 EDLEKTsFR----------GFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDllmcgYPWIQNAS 663
Cdd:COG4778 8 ENLSKT-FTlhlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD-----GGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 664 V---------RDNIIFGSPFNKekydeVV-RVCSLkaDLDILP--------------AGDMTE---IGER-----GITLS 711
Cdd:COG4778 82 AspreilalrRRTIGYVSQFLR-----VIpRVSAL--DVVAEPllergvdreeararARELLArlnLPERlwdlpPATFS 154
|
170 180
....*....|....*....|...
gi 398366407 712 GGQKARINLARSVYKKKDIYLFD 734
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLD 177
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1192-1447 |
3.55e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1192 LEASYRKPEMTPpeswpsmGEIIFE--NVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAG 1269
Cdd:COG3845 242 VLLRVEKAPAEP-------GEVVLEveNLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1270 KILIDNVDISQLGLFDLRRK-LAIIPQDPvLFRG-----TIRKNL-------DPFNERtddelwdALVRGGAIAKDdlpe 1336
Cdd:COG3845 314 SIRLDGEDITGLSPRERRRLgVAYIPEDR-LGRGlvpdmSVAENLilgryrrPPFSRG-------GFLDRKAIRAF---- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1337 vklqkpdengTHGKMHKF-----HLDQAVeeegSNFSLGERQLLALTRALVRQSKILILDEATSSVD-----YetdgkIQ 1406
Cdd:COG3845 382 ----------AEELIEEFdvrtpGPDTPA----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaieF-----IH 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 398366407 1407 TRIVEEF-GDCTILCIAHRLKTIVNY-DRILVLEKGE-VAEFDT 1447
Cdd:COG3845 443 QRLLELRdAGAAVLLISEDLDEILALsDRIAVMYEGRiVGEVPA 486
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
604-771 |
3.56e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG---DLLMCGY--------------PwiqNASVRD 666
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsiKKDLCTYqkqlcfvghrsginP---YLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 667 NIIFGSPFNKE--KYDEVVRVCSLKADLDiLPAGdmteigergiTLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRV 744
Cdd:PRK13540 94 NCLYDIHFSPGavGITELCRLFSLEHLID-YPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....*...
gi 398366407 745 GKHIMDECLTGMLANKTRILATHQ-LSL 771
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQdLPL 190
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
571-807 |
4.21e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 571 GKPSASTNKAKRLDNMLKDRDGPEDLEKTSFRgFKDLNFDIK-KGEFIMI----------------TGPIGTGKSSLLNA 633
Cdd:TIGR00956 730 GEVLGSTDLTDESDDVNDEKDMEKESGEDIFH-WRNLTYEVKiKKEKRVIlnnvdgwvkpgtltalMGASGAGKTTLLNV 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 634 MAGsmRKTDGKVEvNGDLLMCGYPW-----------------IQNASVRDNIIFgSPF--------NKEKY---DEVVRV 685
Cdd:TIGR00956 809 LAE--RVTTGVIT-GGDRLVNGRPLdssfqrsigyvqqqdlhLPTSTVRESLRF-SAYlrqpksvsKSEKMeyvEEVIKL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 686 CSLKADLDILpagdmteIGERGITLSGGQKARINLARSVYKKKDIYLF-DDVLSAVDSRVGKHIMdeCLTGMLANKTR-I 763
Cdd:TIGR00956 885 LEMESYADAV-------VGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSIC--KLMRKLADHGQaI 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 398366407 764 LAT-HQLS--LIERASRVIVLGTDGQV----DIGtvdelkARNQTLINLLQ 807
Cdd:TIGR00956 956 LCTiHQPSaiLFEEFDRLLLLQKGGQTvyfgDLG------ENSHTIINYFE 1000
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
599-815 |
4.94e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.08 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 599 TSFRGFKDLNFDIKKGEFIMITGPIGTGKSSL---LNAM----AGSM---------RKTDGKVEVNGDLLMCGYPWIQN- 661
Cdd:PRK13651 18 TELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdTGTIewifkdeknKKKTKEKEKVLEKLVIQKTRFKKi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 662 -----------------------ASVRDNIIFGsPFN--------KEKYDEVVRVCSLkaDLDILPagdmteigERGITL 710
Cdd:PRK13651 98 kkikeirrrvgvvfqfaeyqlfeQTIEKDIIFG-PVSmgvskeeaKKRAAKYIELVGL--DESYLQ--------RSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 711 SGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTGMLANKTRILATHQL-SLIERASRVIVLgTDGQV-- 787
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFF-KDGKIik 245
|
250 260 270
....*....|....*....|....*....|....*
gi 398366407 788 DIGTVDELKaRNQTLI-------NLLQFSSQNSEK 815
Cdd:PRK13651 246 DGDTYDILS-DNKFLIennmeppKLLNFVNKLEKK 279
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1199-1398 |
5.72e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.19 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1199 PEMTPPeswpsmgeIIFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDI 1278
Cdd:PRK13537 2 PMSVAP--------IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1279 SQLGLFdLRRKLAIIPQ----DPVLfrgTIRKNLDPFNERTDdelwdalVRGGAIAKDDLPEVKLQKpdengthgkmhkf 1354
Cdd:PRK13537 72 PSRARH-ARQRVGVVPQfdnlDPDF---TVRENLLVFGRYFG-------LSAAAARALVPPLLEFAK------------- 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 398366407 1355 hLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVD 1398
Cdd:PRK13537 128 -LENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1210-1401 |
8.65e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEIIF--ENVDFAYRPGLPIvLKNLNLNIKSGEKIGICGRTGAGKSTIMsalyrlneltagKIL--IDNvDIS-----Q 1280
Cdd:PRK11819 2 MAQYIYtmNRVSKVVPPKKQI-LKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagVDK-EFEgearpA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1281 LGLfdlrrKLAIIPQDPVLFRG-TIRKN-----------LDPFNE-----RTDDELWDALVRGGAiakddlpevKLQ-KP 1342
Cdd:PRK11819 68 PGI-----KVGYLPQEPQLDPEkTVRENveegvaevkaaLDRFNEiyaayAEPDADFDALAAEQG---------ELQeII 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 1343 DENGTHGKMHKfhLDQAVE--------EEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYET 1401
Cdd:PRK11819 134 DAADAWDLDSQ--LEIAMDalrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
597-805 |
9.17e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.46 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 597 EKTS--FRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEV----NGDLLMCGYPW-------IQNA- 662
Cdd:PRK13631 33 EKQEneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELItnpyskkIKNFk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 663 --------------------SVRDNIIFGsPFN--------KEKYDEVVRVCSLKAD-LDILPAGdmteigergitLSGG 713
Cdd:PRK13631 113 elrrrvsmvfqfpeyqlfkdTIEKDIMFG-PVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 714 QKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLTGMLANKTRILATHQL-SLIERASRVIVLGTDGQVDIGTV 792
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTP 260
|
250
....*....|...
gi 398366407 793 DELkARNQTLINL 805
Cdd:PRK13631 261 YEI-FTDQHIINS 272
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
979-1170 |
9.22e-06 |
|
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: 49.41 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 979 PMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAI----AIPFLLV---IFVLIADH 1051
Cdd:cd18546 86 SLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALvalaALPPLALatrWFRRRSSR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1052 YQSSGREikRLEAVQRSFVynnlnEVLGGMDTIKAYR----SQERFLAKSDflinkmneaGY--LVVVLQRWVGIFLDMV 1125
Cdd:cd18546 166 AYRRARE--RIAAVNADLQ-----ETLAGIRVVQAFRrerrNAERFAELSD---------DYrdARLRAQRLVAIYFPGV 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 1126 AIAFALIITLLCVTRAFPISA--ASVGVLLTYVL----------QLPGLLNTILRAM 1170
Cdd:cd18546 230 ELLGNLATAAVLLVGAWRVAAgtLTVGVLVAFLLylrrffapiqQLSQVFDSYQQAR 286
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1229-1288 |
9.95e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.11 E-value: 9.95e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLG---LFDLRR 1288
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRR 85
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1230-1447 |
1.19e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD-LRRKLAIIPQD----PVLfrgTI 1304
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1305 RKNLdpfnertddeLWDAL-VRGGAIAKDDLPEVKLQKPDENGthgkmhkfhLDQAVEEEGSNFSLGERQLLALTRALVR 1383
Cdd:PRK11288 97 AENL----------YLGQLpHKGGIVNRRLLNYEAREQLEHLG---------VDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1384 QSKILILDEATSSVDY-ETDgkIQTRIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGE-VAEFDT 1447
Cdd:PRK11288 158 NARVIAFDEPTSSLSArEIE--QLFRVIRELRAegRVILYVSHRMEEIFALcDAITVFKDGRyVATFDD 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1191-1398 |
1.19e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1191 PLEASYRKPEMTPPeswPSMGeiiFENVDFAYrpGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIMsalyrlnELTAGK 1270
Cdd:PRK10636 297 PFHFSFRAPESLPN---PLLK---MEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLI-------KLLAGE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1271 ILidnvdiSQLGLFDLRR--KLAIIPQDPVLFRgtirknldpfneRTDDELWDALVRggaIAKDDLpEVKLQkpDENGTH 1348
Cdd:PRK10636 362 LA------PVSGEIGLAKgiKLGYFAQHQLEFL------------RADESPLQHLAR---LAPQEL-EQKLR--DYLGGF 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398366407 1349 GkmhkFHLDQaVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVD 1398
Cdd:PRK10636 418 G----FQGDK-VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1210-1459 |
1.62e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.69 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1210 MGEIIFENVDFAYRPGLPiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDlrRK 1289
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1290 LAIIPQDPVLF-RGTIRKNLDpfnertddelWDALVRGgaiakddlpevklqkpdengthgkMHKFHLDQAVEE-----E 1363
Cdd:PRK11650 78 IAMVFQNYALYpHMSVRENMA----------YGLKIRG------------------------MPKAEIEERVAEaarilE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1364 GSNF--------SLGERQLLALTRALVRQSKILILDEATSSVDYETdgKIQTRiVEefgdctILCIAHRLKTIVNY---- 1431
Cdd:PRK11650 124 LEPLldrkprelSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKL--RVQMR-LE------IQRLHRRLKTTSLYvthd 194
|
250 260 270
....*....|....*....|....*....|....*.
gi 398366407 1432 --------DRILVLEKGEVAEFDTPWTLFSQEDSIF 1459
Cdd:PRK11650 195 qveamtlaDRVVVMNGGVAEQIGTPVEVYEKPASTF 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1230-1441 |
1.80e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDIS--------QLGLFDLRRKLAIIPQDPVLfr 1301
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskealENGISMVHQELNLVLQRSVM-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1302 gtirknldpfnertdDELWDALVRGGAIAKDdlpevklqkpdengtHGKMHK--------FHLDQAVEEEGSNFSLGERQ 1373
Cdd:PRK10982 92 ---------------DNMWLGRYPTKGMFVD---------------QDKMYRdtkaifdeLDIDIDPRAKVATLSVSQMQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 1374 LLALTRALVRQSKILILDEATSSVDyETDGKIQTRIVEEFGD--CTILCIAHRLKTIVNY-DRILVLEKGE 1441
Cdd:PRK10982 142 MIEIAKAFSYNAKIVIMDEPTSSLT-EKEVNHLFTIIRKLKErgCGIVYISHKMEEIFQLcDEITILRDGQ 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
607-804 |
1.92e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.11 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 607 LNFDIKKGEFIMITGPIGTGKSSLLNAMaGSMRKTDGKVEVNGDLLMCGY----------------------PWIQNASV 664
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQniyerrvnlnrlrrqvsmvhpkPNLFPMSV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 665 RDNIIFGSPF----NKEKYDEVVRVCSLKADL-DILPagdmTEIGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSA 739
Cdd:PRK14258 105 YDNVAYGVKIvgwrPKLEIDDIVESALKDADLwDEIK----HKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 740 VDSRVGKHIMDECLTGMLANK-TRILATHQLSLIERASRVIVLGTDGQVDIGTVDELKARNQTLIN 804
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGLTKKIFNS 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
605-787 |
2.54e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.82 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLlmcgypwIQNASVRD-----NIIFGSPFNK--- 676
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA-------ITDDNFEKlrkhiGIVFQNPDNQfvg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 677 --EKYDevvrvCSLKADLDILPAGDMTEIGERGIT--------------LSGGQKARINLARSVYKKKDIYLFDDVLSAV 740
Cdd:PRK13648 99 siVKYD-----VAFGLENHAVPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 398366407 741 DSRVGKHIMDecLTGMLA---NKTRILATHQLSLIERASRVIVLgTDGQV 787
Cdd:PRK13648 174 DPDARQNLLD--LVRKVKsehNITIISITHDLSEAMEADHVIVM-NKGTV 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1239-1428 |
2.67e-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: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1239 SGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFDLRRKLAIipqdpvlfrgtirknldpfnertdde 1318
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1319 lwdalvrggaiakddlpevklqkpdengthgkmhkfhldqavEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVD 1398
Cdd:smart00382 55 ------------------------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLD 92
|
170 180 190
....*....|....*....|....*....|....*..
gi 398366407 1399 YETDGKIQTRIV-------EEFGDCTILCIAHRLKTI 1428
Cdd:smart00382 93 AEQEALLLLLEElrlllllKSEKNLTVILTTNDEKDL 129
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
604-802 |
2.77e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.54 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPWIQNASVRDNIIFGSPFNKEKYDEVV 683
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 684 RVCSLKADLDILPAGDMTEIGER-----GIT---------LSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHIM 749
Cdd:PRK13636 102 QDVSFGAVNLKLPEDEVRKRVDNalkrtGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 750 D---ECLTGMlaNKTRILATHQLSLIE-RASRVIVLGTDGQVDIGTVDELKARNQTL 802
Cdd:PRK13636 182 KllvEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1229-1456 |
2.91e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.92 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLFD----------------LRRKLAI 1292
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1293 IPQDP--VLFRGTIRKNldpfnertddelwdalVRGGAIAkddlpeVKLQKPDENgthgKMHKFHL------DQAVEEEG 1364
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKD----------------IMFGPVA------LGVKKSEAK----KLAKFYLnkmgldDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1365 SNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE-EFGDCTILCIAHRLKTIVNY-DRILVLEKGEV 1442
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMEHVLEVaDEVIVMDKGKI 254
|
250
....*....|....
gi 398366407 1443 AEFDTPWTLFSQED 1456
Cdd:PRK13631 255 LKTGTPYEIFTDQH 268
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1230-1454 |
3.01e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1230 LKNLN---LNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDI---SQLGLFDLRRKLAIIPQDPvlF--- 1300
Cdd:PRK11308 28 VKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP--Ygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1301 --RGTIRKNL-DPFNERTDDelwDALVRGgAIAKDDLPEVKLqKPDENGTHGKMhkfhldqaveeegsnFSLGERQLLAL 1377
Cdd:PRK11308 106 npRKKVGQILeEPLLINTSL---SAAERR-EKALAMMAKVGL-RPEHYDRYPHM---------------FSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1378 TRALVRQSKILILDEATSSVDYEtdgkIQTRIV-------EEFGdCTILCIAHRLkTIVNY--DRILVLEKGEVAEFDTP 1448
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVS----VQAQVLnlmmdlqQELG-LSYVFISHDL-SVVEHiaDEVMVMYLGRCVEKGTK 239
|
....*.
gi 398366407 1449 WTLFSQ 1454
Cdd:PRK11308 240 EQIFNN 245
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
892-1096 |
3.04e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 47.83 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 892 WGFIALPLYAILVVGTT---FCSLFSSVWLSYWTENKFKNRPPSFYMGLYsFFVFAAFIFMnGQFTILCAMGIMASKW-L 967
Cdd:cd18578 8 WPLLLLGLIGAIIAGAVfpvFAILFSKLISVFSLPDDDELRSEANFWALM-FLVLAIVAGI-AYFLQGYLFGIAGERLtR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 968 NLR--AVKRILHTPMSYID----TTplGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFAI----A 1037
Cdd:cd18578 86 RLRklAFRAILRQDIAWFDdpenST--GALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALvglaT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1038 IPFLLVIFVLiaDHYQSSGREIKRLEAVQRSFVYnnLNEVLGGMDTIKAYRSQERFLAK 1096
Cdd:cd18578 164 VPLLLLAGYL--RMRLLSGFEEKNKKAYEESSKI--ASEAVSNIRTVASLTLEDYFLEK 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
605-778 |
3.33e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.14 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAM-----AGSMRKTDGKVEVNG------DL----------LMCGYP-WIQNA 662
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGrniyspDVdpievrrevgMVFQYPnPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 663 SVRDNIIFGSPFN-----KEKYDEVVRVCSLKADLdilpagdMTEIGER----GITLSGGQKARINLARSVYKKKDIYLF 733
Cdd:PRK14267 101 TIYDNVAIGVKLNglvksKKELDERVEWALKKAAL-------WDEVKDRlndyPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 398366407 734 DDVLSAVDSrVGKHIMDECLTGMLANKTRILATHQLSlieRASRV 778
Cdd:PRK14267 174 DEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSPA---QAARV 214
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
979-1183 |
3.87e-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: 47.51 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 979 PMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVG-VCVMciVYLPW------FAIAIPFLLVIFVLiadh 1051
Cdd:cd18564 101 SLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGmLGVM--FWLDWqlaliaLAVAPLLLLAARRF---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1052 yqssGREIKRLEAVQRSF---VYNNLNEVLGGMDTIKAYRSQE----RFLAKSDflinKMNEAGYLVVVLQRWVGIFLDM 1124
Cdd:cd18564 175 ----SRRIKEASREQRRRegaLASVAQESLSAIRVVQAFGREEheerRFARENR----KSLRAGLRAARLQALLSPVVDV 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1125 V-AIAFALIITL--LCVTRafpiSAASVGVLL---TY-------VLQLPGLLNTILRAMTqtendmnSAERL 1183
Cdd:cd18564 247 LvAVGTALVLWFgaWLVLA----GRLTPGDLLvflAYlknlykpVRDLAKLTGRIAKASA-------SAERV 307
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
606-781 |
4.89e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.55 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 606 DLNFDIKKGEFIMITGPIGTGKSSL---LNAMAGSmrkTDGKVEVNGD---------------------LLMCGYPWIQN 661
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLlrvLNLLEMP---RSGTLNIAGNhfdfsktpsdkairelrrnvgMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 662 ASVRDNIIfgspfnkekyDEVVRVCSL-------KADlDILPAGDMTEIGER-GITLSGGQKARINLARSVYKKKDIYLF 733
Cdd:PRK11124 97 LTVQQNLI----------EAPCRVLGLskdqalaRAE-KLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 398366407 734 DDVLSAVD----SRVGKHIMDECLTGMlankTRILATHQLSLIER-ASRVIVL 781
Cdd:PRK11124 166 DEPTAALDpeitAQIVSIIRELAETGI----TQVIVTHEVEVARKtASRVVYM 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
604-788 |
6.18e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.50 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVN-----------GDLLMCGYPWIQNASVRDNIIFgS 672
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvrdkdGQLKVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 673 PFNKEKYDEVVRVCsLKADLDILPAGDmTEIGER--------GIT----------LSGGQKARINLARSVYKKKDIYLFD 734
Cdd:PRK10619 100 HFNLWSHMTVLENV-MEAPIQVLGLSK-QEARERavkylakvGIDeraqgkypvhLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 735 DVLSAVDSR-VGK--HIMDEcltgmLAN--KTRILATHQLSLIERASRVIVLGTDGQVD 788
Cdd:PRK10619 178 EPTSALDPElVGEvlRIMQQ-----LAEegKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
605-650 |
6.40e-05 |
|
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: 45.60 E-value: 6.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAG--SMRKTDGKVEVNGD 650
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE 64
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
967-1097 |
7.27e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 46.42 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 967 LNLRAVKRILHTPMSYIDTTPLGRILNRFtkdtdsldNELtESLR-LMTSQFANI------VGVCVMCIVYLPWFAIAIP 1039
Cdd:cd18566 77 LSNAAFEHLLSLPLSFFEREPSGAHLERL--------NSL-EQIReFLTGQALLAlldlpfVLIFLGLIWYLGGKLVLVP 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 1040 -FLLVIFVLIA--DHYQSSGREIKRLEAVQRSfvYNNLNEVLGGMDTIKA-------YRSQERFLAKS 1097
Cdd:cd18566 148 lVLLGLFVLVAilLGPILRRALKERSRADERR--QNFLIETLTGIHTIKAmamepqmLRRYERLQANA 213
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
619-795 |
8.16e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 619 ITGPIGTGKSSLLNAMAGSMRKTDGkVEVNGDLLMCG-----YPWIQNASVRDNIIFG--SPFNKEKYDEV---VRVCSL 688
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGrsifnYRDVLEFRRRVGMLFQrpNPFPMSIMDNVlagVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 689 --KADLDILPAGDMTEIG----------ERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRVGKHImDECLTGM 756
Cdd:PRK14271 131 vpRKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 398366407 757 LANKTRILATHQLSLIERASRVIVLGTDGQ-VDIGTVDEL 795
Cdd:PRK14271 210 ADRLTVIIVTHNLAQAARISDRAALFFDGRlVEEGPTEQL 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1198-1257 |
1.13e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1198 KPEMTPPESWPSMGEIIFENVDFAYrPGLPIVLKNLNLNIKSGEKIGICGRTGAGKSTIM 1257
Cdd:PLN03073 494 KFEFPTPDDRPGPPIISFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTIL 552
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1216-1454 |
1.15e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.62 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYRPG--LPIVLKNLNLNIKSGEKIGICGRTGAGKS-TIMSALYRLN----ELTAGKILIDNVDI---SQLGLFD 1285
Cdd:PRK15134 9 ENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPsppvVYPSGDIRFHGESLlhaSEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 LR-RKLAIIPQDPVLfrgtirkNLDPFNErTDDELWDALV--RG--GAIAKDDLpevkLQKPDENGTH---GKMHKF-Hl 1356
Cdd:PRK15134 89 VRgNKIAMIFQEPMV-------SLNPLHT-LEKQLYEVLSlhRGmrREAARGEI----LNCLDRVGIRqaaKRLTDYpH- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1357 dqaveeegsNFSLGERQLLALTRALVRQSKILILDEATSSVDYETDGKIQTRIVE---EFGdCTILCIAHRLKtIVNY-- 1431
Cdd:PRK15134 156 ---------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqqELN-MGLLFITHNLS-IVRKla 224
|
250 260
....*....|....*....|...
gi 398366407 1432 DRILVLEKGEVAEFDTPWTLFSQ 1454
Cdd:PRK15134 225 DRVAVMQNGRCVEQNRAATLFSA 247
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
587-816 |
1.17e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 587 LKDRDGPEDLEKTsFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLLMCGYPWIQNASVR- 665
Cdd:PRK13546 24 MKDALIPKHKNKT-FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 -DNIIFGSPFNKEKYDEVVRVCSlkadlDILPAGDMTE-IGERGITLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSR 743
Cdd:PRK13546 103 iENIEFKMLCMGFKRKEIKAMTP-----KIIEFSELGEfIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366407 744 VGKHIMDECLTGMLANKTRILATHQLSLIERASRVIVLGTDGQV-DIGTVDELKARNQTLINLLQFSSQNSEKE 816
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLkDYGELDDVLPKYEAFLNDFKKKSKAEQKE 251
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
598-802 |
1.18e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.56 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 598 KTSFRGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGDLL----------MCGYPW------IQN 661
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkenirevrkFVGLVFqnpddqIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 662 ASVRDNIIFGsPFN--------KEKYDEVVRVCSLKADLDILPAgdmteigergiTLSGGQKARINLARSVYKKKDIYLF 733
Cdd:PRK13652 94 PTVEQDIAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 734 DDVLSAVDSRVGKHIMD-----ECLTGMlankTRILATHQLSLI-ERASRVIVLGTDGQVDIGTVDELKARNQTL 802
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDflndlPETYGM----TVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1229-1284 |
1.28e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.40 E-value: 1.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSAL-----YRLNEltaGKILIDNVDI--------SQLGLF 1284
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKILE---GDILFKGESIldlepeerAHLGIF 87
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
895-1143 |
1.29e-04 |
|
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: 45.54 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 895 IALPLYAIlVVGTTFcSLFSSVWLSYWTENKFKNRppsfyMGLYSFFVFAAFIfmnGQFtILCAMGIMASKWLNLRAVKR 974
Cdd:cd18577 13 AALPLMTI-VFGDLF-DAFTDFGSGESSPDEFLDD-----VNKYALYFVYLGI---GSF-VLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 975 I--------LHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFA----IAIPFLL 1042
Cdd:cd18577 82 IrkrylkalLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTlvllATLPLIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1043 VIFVLIAdhYQSSGREIKRLEAVQRSfvYNNLNEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAG-------------- 1108
Cdd:cd18577 162 IVGGIMG--KLLSKYTKKEQEAYAKA--GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGikkglvsglglgll 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 398366407 1109 ----YLVVVLQRWVGIFL---------DMVAIAFALIITLLCVTRAFP 1143
Cdd:cd18577 238 ffiiFAMYALAFWYGSRLvrdgeispgDVLTVFFAVLIGAFSLGQIAP 285
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
604-741 |
1.41e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.84 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGdllmcgypwiQNASVRDNIIFGSPFNkekydevv 683
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG----------KTATRGDRSRFMAYLG-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 684 RVCSLKADLDIL-----------------PAGDMTEIGERGIT------LSGGQKARINLARSVYKKKDIYLFDDVLSAV 740
Cdd:PRK13543 89 HLPGLKADLSTLenlhflcglhgrrakqmPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
.
gi 398366407 741 D 741
Cdd:PRK13543 169 D 169
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
926-1138 |
1.56e-04 |
|
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: 45.58 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 926 FKNRPPSFYMGLYSFFVFAAF------IFMN--GQFTIlcamgimasKWLNLRAVKRILHTPMSYIDTTPLGRILNRFTK 997
Cdd:cd18573 36 FGLSLKTFALALLGVFVVGAAanfgrvYLLRiaGERIV---------ARLRKRLFKSILRQDAAFFDKNKTGELVSRLSS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 998 DT----DSLDNELTESLR-LMTSqfanIVGVCVMCIV--YLPWFAIAI-PFLLVIFVLiadhYqssGREIKRLeavQRSf 1069
Cdd:cd18573 107 DTsvvgKSLTQNLSDGLRsLVSG----VGGIGMMLYIspKLTLVMLLVvPPIAVGAVF----Y---GRYVRKL---SKQ- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366407 1070 VYNNL-------NEVLGGMDTIKAYRSQERFLAKSDFLINKMNEAGYLVVVLQrwvGIFldMVAIAFALIITLLCV 1138
Cdd:cd18573 172 VQDALadatkvaEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALAS---GLF--FGSTGFSGNLSLLSV 242
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
605-649 |
1.58e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.46 E-value: 1.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 398366407 605 KDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG 649
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1217-1454 |
2.18e-04 |
|
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: 45.83 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1217 NVDFAYRPGLPIVLKNLNLNIKSGEKIGICGRTGAGKS-TIMSALyRL----NELTAGKILIDNVDISQLGLFDLRR--- 1288
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLlpdpAAHPSGSILFDGQDLLGLSERELRRirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1289 -KLAIIPQDPV-----LFrgTIRKNLdpfNERTddELWDALVRGGAIAK--DDLPEVKLQKPDEngthgKMHKF-HldQa 1359
Cdd:COG4172 92 nRIAMIFQEPMtslnpLH--TIGKQI---AEVL--RLHRGLSGAAARARalELLERVGIPDPER-----RLDAYpH--Q- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1360 veeegsnFSLGERQLLALTRALVRQSKILILDEATSSVDYeTdgkIQTRIVE-------EFGdCTILCIAHRLkTIV-NY 1431
Cdd:COG4172 157 -------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-T---VQAQILDllkdlqrELG-MALLLITHDL-GVVrRF 223
|
250 260
....*....|....*....|....
gi 398366407 1432 -DRILVLEKGEVAEFDTPWTLFSQ 1454
Cdd:COG4172 224 aDRVAVMRQGEIVEQGPTAELFAA 247
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
602-646 |
3.97e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.76 E-value: 3.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 398366407 602 RGFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVE 646
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1220-1401 |
3.98e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1220 FAYRPglpiVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILID-NVDISQLglfdlrrklaiiPQDPv 1298
Cdd:PRK11147 13 FSDAP----LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqDLIVARL------------QQDP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1299 lfrgtirknldPFNERTD---------DELWDALVRGGAIAKD---DLPE------VKLQ-KPD-------ENGTHGKMH 1352
Cdd:PRK11147 76 -----------PRNVEGTvydfvaegiEEQAEYLKRYHDISHLvetDPSEknlnelAKLQeQLDhhnlwqlENRINEVLA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 398366407 1353 KFHLDQavEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVDYET 1401
Cdd:PRK11147 145 QLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
607-652 |
4.59e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 43.68 E-value: 4.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 398366407 607 LNFDIKKGEFIMITGPIGTGKSSLLNAMAGsMRKTDGKVEVNGDLL 652
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPL 59
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
925-1091 |
5.00e-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: 43.84 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 925 KFKNrpPSFYMGLYSFFVFAAFIFMNGQFTIlcamgIMASkwLNLR----AVKRILHTPMSYIDTTPLGRILNRFTKDTD 1000
Cdd:cd18784 34 KFSR--AIIIMGLLAIASSVAAGIRGGLFTL-----AMAR--LNIRirnlLFRSIVSQEIGFFDTVKTGDITSRLTSDTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1001 SLDNELTESLRLMTSQFANIVGVCVMcIVYLPW-----FAIAIPFLLVIFVLIADHYqssgreiKRL-EAVQRSFVYNN- 1073
Cdd:cd18784 105 TMSDTVSLNLNIFLRSLVKAIGVIVF-MFKLSWqlslvTLIGLPLIAIVSKVYGDYY-------KKLsKAVQDSLAKANe 176
|
170
....*....|....*....
gi 398366407 1074 -LNEVLGGMDTIKAYRSQE 1091
Cdd:cd18784 177 vAEETISSIRTVRSFANED 195
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
596-786 |
5.33e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 42.68 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 596 LEKTSFRGFKDLNFDIKKG---EFIMITGPIGTGKSSLLNAM-------AGSMRKTDGKVEVNGDllmcGYPWIQNASVR 665
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGgsnSFNAIVGPNGSGKSNIVDAIcfvlggkAAKLRRGSLLFLAGGG----VKAGINSASVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 666 ---DNIIFgspfnkekydevvrvcslkadldILPAGDMTEIgergitLSGGQKARINL----ARSVYKKKDIYLFDDVLS 738
Cdd:cd03239 77 itfDKSYF-----------------------LVLQGKVEQI------LSGGEKSLSALalifALQEIKPSPFYVLDEIDA 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398366407 739 AVD----SRVGKHIMDecltgmLANKTR--ILATHQLSLIERASRVI-VLGTDGQ 786
Cdd:cd03239 128 ALDptnrRRVSDMIKE------MAKHTSqfIVITLKKEMFENADKLIgVLFVHGV 176
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1351-1398 |
5.82e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 5.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 398366407 1351 MHKFHLDQAVEEEGSNFSLGERQLLALTRALVRQSKILILDEATSSVD 1398
Cdd:NF033858 382 LERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
607-652 |
6.75e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.00 E-value: 6.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 398366407 607 LNFDIKKGEFIMITGPIGTGKSSLLNAMAGsMRKTDGKVEVNGDLL 652
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPL 59
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
601-634 |
7.97e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 42.10 E-value: 7.97e-04
10 20 30
....*....|....*....|....*....|....
gi 398366407 601 FRGFKDLNFDIKKGeFIMITGPIGTGKSSLLNAM 634
Cdd:pfam13476 6 FRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
613-779 |
8.78e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 613 KGEFIMITGPIGTGKSSLLNAMAgsmrktdgkvevngdlLMCGYpwiqnASVRDNiifgspfnkeKYDEVVRVCslkadl 692
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG----------------LALGG-----AQSATR----------RRSGVKAGC------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 693 dILPAGDMTEIGERgITLSGGQKARINLA----RSVYKKKDIYLFDDVLSAVDSRVGKHIMDECLtGMLANKTR-ILATH 767
Cdd:cd03227 63 -IVAAVSAELIFTR-LQLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQALAEAIL-EHLVKGAQvIVITH 139
|
170
....*....|..
gi 398366407 768 QLSLIERASRVI 779
Cdd:cd03227 140 LPELAELADKLI 151
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1216-1448 |
1.21e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.51 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1216 ENVDFAYRPGlpIVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALyrLNELTA----------GKILIDNVDISQLGLFD 1285
Cdd:PRK13547 5 DHLHVARRHR--AILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTGggaprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1286 LRRKLAIIPQ-----------DPVLF-RGTIRKNLDPFNERTDDELWDALVRGGAiakddlpevklqkpdengthgkmhk 1353
Cdd:PRK13547 81 LARLRAVLPQaaqpafafsarEIVLLgRYPHARRAGALTHRDGEIAWQALALAGA------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1354 fhlDQAVEEEGSNFSLGERQLLALTRAL---------VRQSKILILDEATSSVDYETdgkiQTRIVEEFGDCT------I 1418
Cdd:PRK13547 136 ---TALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAH----QHRLLDTVRRLArdwnlgV 208
|
250 260 270
....*....|....*....|....*....|.
gi 398366407 1419 LCIAHRLKTIVNY-DRILVLEKGEVAEFDTP 1448
Cdd:PRK13547 209 LAIVHDPNLAARHaDRIAMLADGAIVAHGAP 239
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1228-1398 |
1.40e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.71 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1228 IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQLGLfDLRRKLAIIPQ----DPVLfrgT 1303
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHqpgiKTEL---T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1304 IRKNLDpFNER-----TDDELWDALVRGGAIAKDDLPeVKlqkpdengthgkmhkfHLdqaveeegsnfSLGERQLLALT 1378
Cdd:PRK13538 91 ALENLR-FYQRlhgpgDDEALWEALAQVGLAGFEDVP-VR----------------QL-----------SAGQQRRVALA 141
|
170 180
....*....|....*....|
gi 398366407 1379 RALVRQSKILILDEATSSVD 1398
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAID 161
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
974-1098 |
1.53e-03 |
|
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: 42.14 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 974 RILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGVCVMCIVYLPWFA----IAIPFLLVIFVL-- 1047
Cdd:cd18778 82 KLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLAlltlIPIPFLALGAWLys 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 398366407 1048 --IADHYQSSGREIKRLEAVqrsfvynnLNEVLGGMDTIKAYRSQE----RFLAKSD 1098
Cdd:cd18778 162 kkVRPRYRKVREALGELNAL--------LQDNLSGIREIQAFGREEeeakRFEALSR 210
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
974-1093 |
1.96e-03 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 42.09 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 974 RILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESLRLMTSQFANIVGvCVMCIVYLPW----FAIA-IPFLLVIFVLI 1048
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIG-GVVLLFFISWkltlLMLAtVPVVVLVAVLF 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 398366407 1049 adhyqssGREIKRL-----EAVQRSFVYnnLNEVLGGMDTIKAYrSQERF 1093
Cdd:cd18576 157 -------GRRIRKLskkvqDELAEANTI--VEETLQGIRVVKAF-TREDY 196
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
974-1122 |
2.08e-03 |
|
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: 41.81 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 974 RILHTPMSYIDTTPLGRILNRFTkDTDSLDNELTESlrlMTSQFANIVGVcVMCIVYLPWFA--------IAIPFLLVIF 1045
Cdd:cd18782 84 HLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGT---ALTTLLDVLFS-VIYIAVLFSYSplltlvvlATVPLQLLLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1046 VLIADHYQssgREIKRLEAvQRSFVYNNLNEVLGGMDTIKA--------YRSQERFLA--KSDFLINKMNEAGY------ 1109
Cdd:cd18782 159 FLFGPILR---RQIRRRAE-ASAKTQSYLVESLTGIQTVKAqnaelkarWRWQNRYARslGEGFKLTVLGTTSGslsqfl 234
|
170
....*....|....*
gi 398366407 1110 --LVVVLQRWVGIFL 1122
Cdd:cd18782 235 nkLSSLLVLWVGAYL 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1229-1280 |
2.43e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.10 E-value: 2.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 398366407 1229 VLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYR--LNELTAGKILIDNVDISQ 1280
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGR 98
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
933-1115 |
2.79e-03 |
|
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: 41.62 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 933 FYMGLYSFFVFAAFIfMNGQFTILCAMGIMAskwlNLRA--VKRILHTPMSYIDTTPLGRILNRFTKDTDSLDNELTESL 1010
Cdd:cd18548 43 LLMLLLALLGLIAGI-LAGYFAAKASQGFGR----DLRKdlFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 1011 RLMTSQFANIVGVCVMCIVYLPW----FAIAIPFLLVIFVLIadhyqsSGREIKRLEAVQRSfvYNNLNEV----LGGMD 1082
Cdd:cd18548 118 RMLVRAPIMLIGAIIMAFRINPKlaliLLVAIPILALVVFLI------MKKAIPLFKKVQKK--LDRLNRVvrenLTGIR 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 398366407 1083 TIKAYRSQ----ERFLAKSDFLINKMNEAGYLVVVLQ 1115
Cdd:cd18548 190 VIRAFNREdyeeERFDKANDDLTDTSLKAGRLMALLN 226
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
989-1096 |
5.54e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD 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. 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: 350029 [Multi-domain] Cd Length: 290 Bit Score: 40.54 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 989 GRILNRFTKDTDSLDNELtesLRLMTSQFANIVGVCVMCIVyLPWFAIAIPFLLVIFVLIAD-------HYqsSGREIKR 1061
Cdd:cd18585 92 GDLLNRIVADIDTLDNLY---LRVLSPPVVALLVILATILF-LAFFSPALALILLAGLLLAGvvipllfYR--LGKKIGQ 165
|
90 100 110
....*....|....*....|....*....|....*
gi 398366407 1062 LEAVQRSFVYNNLNEVLGGMDTIKAYRSQERFLAK 1096
Cdd:cd18585 166 QLVQLRAELRTELVDGLQGMAELLIFGALERQRQQ 200
|
|
| HMG-box_UBF1_rpt4 |
cd22001 |
fourth high mobility group (HMG)-box found in upstream-binding factor 1 (UBF1) and similar ... |
161-193 |
5.60e-03 |
|
fourth high mobility group (HMG)-box found in upstream-binding factor 1 (UBF1) and similar proteins; UBF1, also called UBTF, nucleolar transcription factor 1, or auto-antigen NOR-90, is a nucleolar transcription factor that recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element. UBF1 contains six HMG-box domains. This model corresponds to the fourth one.
Pssm-ID: 438817 [Multi-domain] Cd Length: 66 Bit Score: 36.89 E-value: 5.60e-03
10 20 30
....*....|....*....|....*....|....*...
gi 398366407 161 MIYYFEKTRKKYRKRHPEATEEEVM-----ENAKLPKH 193
Cdd:cd22001 10 MFIYSKEKRSKLKKKHPELSEQELTrllakKYNELPDK 47
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1204-1252 |
6.62e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 6.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 398366407 1204 PESWPSMGEIIFENVDF-AYRPGLP--IVLKNLNLNIKSGEKIGICGRTGAG 1252
Cdd:NF040905 247 PERTPKIGEVVFEVKNWtVYHPLHPerKVVDDVSLNVRRGEIVGIAGLMGAG 298
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
604-664 |
6.66e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 6.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEvngdllmcgypWIQNASV 664
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-----------WSENANI 384
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
604-650 |
7.08e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.13 E-value: 7.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 398366407 604 FKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNGD 650
Cdd:PRK11831 23 FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE 69
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1228-1280 |
8.11e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 40.09 E-value: 8.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 398366407 1228 IVLKNLNLNIKSGEKIGICGRTGAGKSTIMSALYRLNELTAGKILIDNVDISQ 1280
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP 67
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
603-671 |
8.47e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.37 E-value: 8.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398366407 603 GFKDLNFDIKKGEFIMITGPIGTGKSSLLNAMAGSMRKTDGKVEVNG---------DLLMCGYPWIQNASVRDNIIFG 671
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqDGLANGIVYISEDRKRDGLVLG 344
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
698-852 |
8.91e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366407 698 GD-MTEIGERgitLSGGQKARINLARSVYKKKDIYLFDDVLSAVDSRvgkhiMDECLTGMLAN--KTRILATHQLSLIER 774
Cdd:PRK10636 421 GDkVTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDfeGALVVVSHDRHLLRS 492
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398366407 775 ASRVIVLGTDGQVDIGTVDeLKARNQTLINLLQFSSQNSEKEDEEQEAVVAGELGQLKYESEVKELTE-LKKKATEMSQ 852
Cdd:PRK10636 493 TTDDLYLVHDGKVEPFDGD-LEDYQQWLSDVQKQENQTDEAPKENNANSAQARKDQKRREAELRTQTQpLRKEIARLEK 570
|
|
| |
