|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
222-1542 |
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: 880.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 222 LLSKATYWWMNTLIISAHRKPIDLKAIGKLPIAMRAVTNYVCLKEAYEEQKKKAADHP---------------------- 279
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPvsavygkkdpskpkgssqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 280 -------------NRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNEPknnttrfsETLSSKEFLE 346
Cdd:TIGR00957 289 eevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDP--------MAPDWQGYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 347 NAhvlavLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLF 426
Cdd:TIGR00957 361 TG-----LLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMDLAT 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 427 LCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYA 506
Cdd:TIGR00957 434 YINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 507 WEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAE-AFASLSLFHILVTPLFLL 585
Cdd:TIGR00957 514 WELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEkAFVSLALFNILRFPLNIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 586 STVVRFAVKAIISVQKLNEFLLSDEIGEDSwrtgegtlpfesckkhtgVQSKPInrkQPGryhldnyeqarrlrpaetED 665
Cdd:TIGR00957 594 PMVISSIVQASVSLKRLRIFLSHEELEPDS------------------IERRTI---KPG------------------EG 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 666 VAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvnesepsfeatrsrs 744
Cdd:TIGR00957 635 NSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------------- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 745 rySVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 824
Cdd:TIGR00957 700 --SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 825 NTNIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 899
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIFEhvigpEGVLK-----NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRD 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 900 VELYEHWKTLMNRQDQElekDMEADQTTL------ERKTLRRAMY-----SREAKAQMEDEDEEEEEEEDEDDNMSTVMR 968
Cdd:TIGR00957 853 GAFAEFLRTYAPDEQQG---HLEDSWTALvsgegkEAKLIENGMLvtdvvGKQLQRQLSASSSDSGDQSRHHGSSAELQK 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 969 LRTKMP-WKTC---------------WWYLTSGGFFLLFLMIFSKLLKHSVIVAIDYWLATWTSEySINDPGKADQTFYV 1032
Cdd:TIGR00957 930 AEAKEEtWKLMeadkaqtgqvelsvyWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDD-PMVNGTQNNTSLRL 1008
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1033 ---AGFSILCGAGIFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLES 1109
Cdd:TIGR00957 1009 svyGALGILQGFAVFG---YSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKM 1085
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1110 LTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETR 1189
Cdd:TIGR00957 1086 FMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQER 1165
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1190 FKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLAD 1267
Cdd:TIGR00957 1166 FIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLfaALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSE 1245
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1268 LEVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSG 1347
Cdd:TIGR00957 1246 METNIVAVERLKEYSETEKEA-PWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAG 1324
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1348 KSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMV 1427
Cdd:TIGR00957 1325 KSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFV 1404
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1428 KSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL 1507
Cdd:TIGR00957 1405 SALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM 1484
|
1370 1380 1390
....*....|....*....|....*....|....*
gi 3273501 1508 TADLVIVMKRGNILEYDTPESLLAQEdGVFASFVR 1542
Cdd:TIGR00957 1485 DYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
220-1543 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 757.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 220 VNLLSKATYWWMNTLIISAHRKPIDLKAIGKLPIAMRAVTNYVCLKEAYEEQKKKaadhpnrtPSIWL--AMYRAFGRPI 297
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK--------PKPWLlrALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 298 LLSSTFRYLADLLGFAGPLCISGIVQRV--NEPKNNTTRFSETLSSKEFLEnahvlavllflalilqrTFLQASYYVTI- 374
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPLLLNLLLESMqnGEPAWIGYIYAFSIFVGVVLG-----------------VLCEAQYFQNVm 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 375 ETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSAL 454
Cdd:PLN03130 367 RVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 455 VGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 534
Cdd:PLN03130 445 IGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 535 LSIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEiged 614
Cdd:PLN03130 525 FNSFILNSIPVLVTVVSFGVFTLLGGD-LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEE---- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 615 swrtgegtlpfesckkhtgvqskpinrkqpgRYHLDNyeqarrlRPAETEDVAIKVTNGYFSWGSGL--ATLSNIDIRIP 692
Cdd:PLN03130 600 -------------------------------RVLLPN-------PPLEPGLPAISIKNGYFSWDSKAerPTLSNINLDVP 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 693 TGQLTMIVGQVGCGKSSLLLAILGEMqtlegkvywnnvnesePSFEATRSRSRYSVAYAAQKPWLLNATVEENITFGSSF 772
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAMLGEL----------------PPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPF 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 773 NRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGIL 852
Cdd:PLN03130 706 DPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 853 KFLQddKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLMNR-----QDQELEKDMEADQTT 927
Cdd:PLN03130 786 DELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL-SNNGPLF---QKLMENagkmeEYVEENGEEEDDQTS 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 928 LERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMPWKTCWwyltsGGFFLLFLMIFSKLLKHSVIVAI 1007
Cdd:PLN03130 860 SKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNAL-----GGAWVVMILFLCYVLTEVFRVSS 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1008 DYWLATWTSEYSINDPGKAdqtFYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGL 1087
Cdd:PLN03130 935 STWLSEWTDQGTPKTHGPL---FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGR 1011
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1088 ILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYFIQKYFRVASKDLQELDDSTQLPL 1167
Cdd:PLN03130 1012 IINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPV 1091
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1168 LCHFSETAEGLTTIRAFRHetrfKQRMLELTDT---NNIAYLFLS-AANRWLEVRTDYLGACIV-LTASIA------SIS 1236
Cdd:PLN03130 1092 YAQFGEALNGLSTIRAYKA----YDRMAEINGRsmdNNIRFTLVNmSSNRWLAIRLETLGGLMIwLTASFAvmqngrAEN 1167
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1237 GSSNSGLVGLGLLYALTITNYLNWVVRnLADL-EVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKIHDLCV 1315
Cdd:PLN03130 1168 QAAFASTMGLLLSYALNITSLLTAVLR-LASLaENSLNAVERVGTYIDLPSEA-PLVIENNRPPPGWPSSGSIKFEDVVL 1245
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1316 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILF 1395
Cdd:PLN03130 1246 RYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLF 1325
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1396 SGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1475
Cdd:PLN03130 1326 SGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1476 DMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEDGVFASFVRA 1543
Cdd:PLN03130 1406 DVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
221-1543 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 730.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 221 NLLSKATYWWMNTLIISAHRKPIDLKAIGKLPIAMRAVTNYVCLKEAYEEQkkkaadhpNRTPSIWL--AMYRAFGRPIL 298
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE--------SRRPKPWLlrALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 299 LSSTFRYLADLLGFAGPLCISGIVQRVNEpkNNTTRFSETLSSKEFLenahvlavllflaLILQRTFLQASYYVTI-ETG 377
Cdd:PLN03232 305 LGGIFKIGHDLSQFVGPVILSHLLQSMQE--GDPAWVGYVYAFLIFF-------------GVTFGVLCESQYFQNVgRVG 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 378 INLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGA 457
Cdd:PLN03232 370 FRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGS 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 458 AVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSI 537
Cdd:PLN03232 448 LILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNS 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 538 FMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEigedswr 617
Cdd:PLN03232 528 FILNSIPVVVTLVSFGVFVLLGGD-LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEE------- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 618 tgegtlpfesckkHTGVQSKPInrkQPGRyhldnyeqarrlrPAetedvaIKVTNGYFSWGSGLA--TLSNIDIRIPTGQ 695
Cdd:PLN03232 600 -------------RILAQNPPL---QPGA-------------PA------ISIKNGYFSWDSKTSkpTLSDINLEIPVGS 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 696 LTMIVGQVGCGKSSLLLAILGEMqtlegkvywnnvnesePSFEATRSRSRYSVAYAAQKPWLLNATVEENITFGSSFNRQ 775
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLGEL----------------SHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 776 RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFL 855
Cdd:PLN03232 709 RYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDEL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 856 QDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLM------------NRQDQELEKDMEA 923
Cdd:PLN03232 789 KG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLF---KKLMenagkmdatqevNTNDENILKLGPT 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 924 DQTTLERKTLRRAMYSREAKAQMededeeeeeeededdnMSTVMRLRTKMPWKTCWWYLTS-GGFFLLFLMIFSKLLKHS 1002
Cdd:PLN03232 863 VTIDVSERNLGSTKQGKRGRSVL----------------VKQEERETGIISWNVLMRYNKAvGGLWVVMILLVCYLTTEV 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1003 VIVAIDYWLATWTSEYSIND--PGkadqtFYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFF 1080
Cdd:PLN03232 927 LRVSSSTWLSIWTDQSTPKSysPG-----FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFF 1001
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1081 DTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYFIQKYFRVASKDLQELD 1160
Cdd:PLN03232 1002 HTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLD 1081
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1161 DSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDtNNIAY-LFLSAANRWLEVRTDYLGACIV-LTASIASISGS 1238
Cdd:PLN03232 1082 SVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMD-NNIRFtLANTSSNRWLTIRLETLGGVMIwLTATFAVLRNG 1160
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1239 SNSGLVG----LGLL--YALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKIHD 1312
Cdd:PLN03232 1161 NAENQAGfastMGLLlsYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEA-TAIIENNRPVSGWPSRGSIKFED 1239
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1313 LCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP 1392
Cdd:PLN03232 1240 VHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP 1319
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1393 ILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1472
Cdd:PLN03232 1320 VLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1473 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEDGVFASFVRA 1543
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
303-1543 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 662.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 303 FRYLADLLGFAGPLCISGIVQRVNEPkNNTTRFSETLSSKEFLENAhvlavllflaliLQRTFLQASYYVTIETGINLRG 382
Cdd:PTZ00243 252 FKLLSDVCTLTLPVLLKYFVKFLDAD-NATWGRGLGLVLTLFLTQL------------IQSVCLHRFYYISIRCGLQYRS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 383 ALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVL 462
Cdd:PTZ00243 319 ALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 463 LAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAA 542
Cdd:PTZ00243 399 TLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATSFVNNA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 543 IPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEIG-------EDS 615
Cdd:PTZ00243 479 TPTLMIAVVFTVY-YLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATcstvqdmEEY 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 616 WRTGEGTLP-------FESCKKHTGV-------------------------QSKPINRKQPGRYHLDNYE------QARR 657
Cdd:PTZ00243 558 WREQREHSTacqlaavLENVDVTAFVpvklprapkvktsllsralrmlcceQCRPTKRHPSPSVVVEDTDygspssASRH 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 658 L-----------RPAETED--VAIKVTNGYFSWGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK 724
Cdd:PTZ00243 638 IveggtgggheaTPTSERSakTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 725 VYwnnvnesepsfeATRSrsrysVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGER 804
Cdd:PTZ00243 717 VW------------AERS-----IAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEK 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 805 GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDG 884
Cdd:PTZ00243 780 GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDG 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 885 SVLREGTLKD-IQTkdvELYEHWKT-LMNRQDQElEKDMEADQTTLER-KTLRRAMYSREAKAQMEDEDEEEEEEEDEDD 961
Cdd:PTZ00243 858 RVEFSGSSADfMRT---SLYATLAAeLKENKDSK-EGDADAEVAEVDAaPGGAVDHEPPVAKQEGNAEGGDGAALDAAAG 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 962 NMSTVMRLRTKM-PWKTCWWYLTS-GGFFLLFLMIFSKLLKHSVIVAIDYWLATWTSeysiNDPGKADQTF-YV-AGFSI 1037
Cdd:PTZ00243 934 RLMTREEKASGSvPWSTYVAYLRFcGGLHAAGFVLATFAVTELVTVSSGVWLSMWST----RSFKLSAATYlYVyLGIVL 1009
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1038 LCGAGIFLCLVTSLTVEWMGltaAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLC 1117
Cdd:PTZ00243 1010 LGTFSVPLRFFLSYEAMRRG---SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSI 1086
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1118 LSAIGMISYATPVFLIALAPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLEL 1197
Cdd:PTZ00243 1087 CSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRR 1166
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1198 TDTNNIAYLFLSAANRWLEVRTDYLGACIVLT------ASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQ 1271
Cdd:PTZ00243 1167 LDVVYSCSYLENVANRWLGVRVEFLSNIVVTVialigvIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEAD 1246
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1272 MGAVKKVNSF--------------LTMESENYEGT---------MDPSQVPEHWP---QEGEIKIHDLCVRYENNLKPVL 1325
Cdd:PTZ00243 1247 MNSVERLLYYtdevphedmpeldeEVDALERRTGMaadvtgtvvIEPASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVL 1326
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1326 KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDP 1405
Cdd:PTZ00243 1327 RGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDP 1406
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1406 ECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILI-MDEATASIDMATENILQ 1484
Cdd:PTZ00243 1407 FLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQ 1486
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1485 KVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEDGVFASFVRA 1543
Cdd:PTZ00243 1487 ATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1306-1545 |
1.12e-172 |
|
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: 517.54 E-value: 1.12e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1306 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1385
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSI 1465
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1466 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEDGVFASFVRADM 1545
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
668-885 |
2.33e-154 |
|
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: 467.58 E-value: 2.33e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYS 747
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 827
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 828 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGS 885
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
221-1532 |
4.32e-138 |
|
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: 464.00 E-value: 4.32e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 221 NLLSKATYWWMNTLIISAHRKPIDLKAIGKLPIAMRAVTnyvcLKEAYEEQKKKAADHPNRTPSIWLAMYRAFGRPILLS 300
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADN----LSERLEREWDRELASAKKNPKLLNALRRCFFWRFVFY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 301 STFRYLADLLGFAGPLCISGIVQRVNePKNNTTRfsetlsskeflENAHVLAVLLFLALILQRTFLQASYYVTIETGINL 380
Cdd:TIGR01271 86 GILLYFGEATKAVQPLLLGRIIASYD-PFNAPER-----------EIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 381 RGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVI 460
Cdd:TIGR01271 154 RIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 461 VLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFAlytSLSIFMN 540
Cdd:TIGR01271 232 ILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA---YLRYFYS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 541 AAIPIAAVLATF---VTHAYASGNNLKpaEAFASLSLFHIL-VTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEIG---- 612
Cdd:TIGR01271 309 SAFFFSGFFVVFlsvVPYALIKGIILR--RIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKtley 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 613 ------------EDSWRTGEGTLpFESCKKHTGvqskpiNRKQPgryhldnyeqarrlrpaetedvaikvtNG----YFS 676
Cdd:TIGR01271 387 nltttevemvnvTASWDEGIGEL-FEKIKQNNK------ARKQP---------------------------NGddglFFS 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 677 WGSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVywnnvnesepsfeatrsRSRYSVAYAAQK 754
Cdd:TIGR01271 433 NFSLYVTpvLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------------KHSGRISFSPQT 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 755 PWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 834
Cdd:TIGR01271 496 SWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 835 FSALDIHLSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD---------VELYEH 905
Cdd:TIGR01271 576 FTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfsslllgLEAFDN 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 906 WK----------TLM-------------------------------------------NRQDQELEKDMEADQTT----- 927
Cdd:TIGR01271 654 FSaerrnsilteTLRrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasARKFSFVQMGPQKAQATtieda 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 928 ----LERK------------TLRRA-MYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRT---KM-------------- 973
Cdd:TIGR01271 734 vrepSERKfslvpedeqgeeSLPRGnQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQLQTsfrKKssitqqnelaseld 813
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 974 --------------------------------------PWKTCWWYLTSGG---FFLLF-LMIFSKLLKHSVIVaidYWL 1011
Cdd:TIGR01271 814 iysrrlskdsvyeiseeineedlkecfaderenvfettTWNTYLRYITTNRnlvFVLIFcLVIFLAEVAASLLG---LWL 890
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1012 ATWTSEYSIND-------------------PGKADQTFY--VAGFSILCGAGIF--LCLVTSLtvewmgLTAAKNLHHNL 1068
Cdd:TIGR01271 891 ITDNPSAPNYVdqqhanasspdvqkpviitPTSAYYIFYiyVGTADSVLALGFFrgLPLVHTL------LTVSKRLHEQM 964
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1069 LNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYFIQKY 1148
Cdd:TIGR01271 965 LHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAY 1044
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1149 FRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFK---QRMLELTDTNNIAYLflsAANRWLEVRTDYLGAC 1225
Cdd:TIGR01271 1045 FLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFEtlfHKALNLHTANWFLYL---STLRWFQMRIDIIFVF 1121
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1226 IVLTASIASISGSSNSG-LVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGT------------ 1292
Cdd:TIGR01271 1122 FFIAVTFIAIGTNQDGEgEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSggggkyqlstvl 1201
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1293 -MDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGI 1371
Cdd:TIGR01271 1202 vIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGV 1280
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1372 DISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQ 1451
Cdd:TIGR01271 1281 SWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQ 1360
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1452 LFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1531
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
.
gi 3273501 1532 Q 1532
Cdd:TIGR01271 1441 E 1441
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
299-602 |
2.01e-134 |
|
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: 417.79 E-value: 2.01e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 299 LSSTFRYLADLLGFAGPLCISGIVQRVNE---PKNNTTRFSET--LSSKEFLENAHVLAVLLFLALILQRTFLQASYYVT 373
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEEntySSSNSTDKLSVsyVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 374 IETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSA 453
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 454 LVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYT 533
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 534 SLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 602
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1306-1526 |
2.09e-129 |
|
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: 400.33 E-value: 2.09e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1306 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1385
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSI 1465
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1466 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1526
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
991-1282 |
1.37e-123 |
|
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: 388.11 E-value: 1.37e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 991 FLMIFSKLLKHSVIVAIDYWLATWTSE--------YSINDPGKADQ--TFYVAGFSILCGAGIFLCLVTSLTVEWMGLTA 1060
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEAnhdvasvvFNITSSSLEDDevSYYISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1061 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGV 1140
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1141 AFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTD 1220
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1221 YLGACIVL----TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1282
Cdd:cd18602 242 YLGAVIVFlaalSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
668-885 |
5.54e-104 |
|
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: 329.82 E-value: 5.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLA----TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvnesepsfeatrsr 743
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 744 srySVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 823
Cdd:cd03250 67 ---SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 824 QNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKrTVVLVTHKLQYLTHADWIIAMKDGS 885
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
967-1543 |
8.60e-101 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 335.60 E-value: 8.60e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 967 MRLRTKMPWKTCWWYLtSGGFFLLFLMIFSKLLkHSVIVAIDYWLATWTseysIND---PGKADQTFYVAGFSILCGAGI 1043
Cdd:COG1132 1 MSKSPRKLLRRLLRYL-RPYRGLLILALLLLLL-SALLELLLPLLLGRI----IDAllaGGDLSALLLLLLLLLGLALLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1044 FLC-LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG 1122
Cdd:COG1132 75 ALLsYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1123 MISYATP----VFLIALAPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLEL 1197
Cdd:COG1132 155 VLFVIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEaLAELNG-----RLQESLSGIRVVKAFGREERELERFREA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1198 TDTNNIAYLFLSAANRWLEVRTDYLGACIVLTasiasisgssnsgLVGLG-----------------LLYALTITNYLNW 1260
Cdd:COG1132 230 NEELRRANLRAARLSALFFPLMELLGNLGLAL-------------VLLVGgllvlsgsltvgdlvafILYLLRLFGPLRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1261 VVRNLADLEVQMGAVKKVNSFLTMESENYEGTmDPSQVPehwPQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGI 1340
Cdd:COG1132 297 LANVLNQLQRALASAERIFELLDEPPEIPDPP-GAVPLP---PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1341 CGRTGSGKSSL-SLaFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWE 1416
Cdd:COG1132 372 VGPSGSGKSTLvNL-LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDA--TDEEVEE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1417 ALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTV 1496
Cdd:COG1132 449 AAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTT 528
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 3273501 1497 VTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeDGVFASFVRA 1543
Cdd:COG1132 529 IVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRL 574
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1302-1526 |
4.63e-90 |
|
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: 290.85 E-value: 4.63e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1302 WPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL 1381
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 RSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEiaqlknmvkslpggldatVTEGGENFSVGQRQLFCLARAFVR 1461
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1462 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1526
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
986-1281 |
1.24e-81 |
|
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: 270.53 E-value: 1.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 986 GFFLLFLMIFSKLLkhsvIVAIDYWLATWTSEYSINDPgkADQTFYVAGF-SILCGAGIFLCLVTSLTVEWMGLTAAKNL 1064
Cdd:cd18580 1 VLLLLLLLLLLAFL----SQFSNIWLDWWSSDWSSSPN--SSSGYYLGVYaALLVLASVLLVLLRWLLFVLAGLRASRRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1065 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYF 1144
Cdd:cd18580 75 HDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1145 IQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGA 1224
Cdd:cd18580 155 LQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1225 CIV--LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 1281
Cdd:cd18580 235 LLAlvVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1023-1542 |
1.32e-80 |
|
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: 281.72 E-value: 1.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1023 PGKADQTFYV--AGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSaDTNIID 1100
Cdd:COG2274 188 PNQDLSTLWVlaIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1101 QHIP-PTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAF---YFIQKYFRVASKDLQELDDSTQLpllcHFSETAE 1176
Cdd:COG2274 267 EFLTgSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVllgLLFQPRLRRLSREESEASAKRQS----LLVETLR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1177 GLTTIRAFRHETRFKQRMLELTdtnnIAYLFLSAANRWLEVRTDYLGACIvltasiasisgssnSGLVGLGLLYA----- 1251
Cdd:COG2274 343 GIETIKALGAESRFRRRWENLL----AKYLNARFKLRRLSNLLSTLSGLL--------------QQLATVALLWLgaylv 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1252 ----LTI-----TNYLNWV----VRNLADL--EVQM--GAVKKVNSFLTMESENYEGTmDPSQVPEhwpQEGEIKIHDLC 1314
Cdd:COG2274 405 idgqLTLgqliaFNILSGRflapVAQLIGLlqRFQDakIALERLDDILDLPPEREEGR-SKLSLPR---LKGDIELENVS 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1315 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 1394
Cdd:COG2274 481 FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFL 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1395 FSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEA 1471
Cdd:COG2274 561 FSGTIRENItlgDPDA--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1472 TASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeDGVFASFVR 1542
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQ 708
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
990-1269 |
3.33e-76 |
|
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: 255.10 E-value: 3.33e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 990 LFLMIFSKLLKHSVIVAIDYWLATWTSEYSINDPGKADQT-FYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNL 1068
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1069 LNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYFIQKY 1148
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1149 FRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVL 1228
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 3273501 1229 TASIASISGSSNSG--LVGLGLLYALTITNYLNWVVRNLADLE 1269
Cdd:cd18603 241 FAALFAVLSRDSLSpgLVGLSISYALQITQTLNWLVRMTSELE 283
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
987-1282 |
4.84e-72 |
|
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: 243.14 E-value: 4.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 987 FFLLFLMIFSKLLkhsvIVAIDYWLATWTSEYSIN---DPGKADQTFYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKN 1063
Cdd:cd18604 2 ALLLLLFVLSQLL----SVGQSWWLGIWASAYETSsalPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1064 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFY 1143
Cdd:cd18604 78 LHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1144 FIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLG 1223
Cdd:cd18604 158 YIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1224 ACIVL-TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1282
Cdd:cd18604 238 ALFSFaTAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1306-1532 |
4.94e-72 |
|
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: 240.21 E-value: 4.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1306 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1385
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRK 1462
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIrlgRPNA--TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1463 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1114-1533 |
4.04e-69 |
|
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: 243.90 E-value: 4.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1114 TLLCLSAIGMISYATPVFLIALAPLGVAF-YFIQKYFRVASKD----LQELDDstqlpllcHFSETAEGLTTIRAFRHET 1188
Cdd:COG4988 146 PLLILVAVFPLDWLSGLILLVTAPLIPLFmILVGKGAAKASRRqwraLARLSG--------HFLDRLRGLTTLKLFGRAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1189 RFKQRMLELTDTNNIAYL------FLSAANrwLEVRTdYLGACIVLtasiasisgssnsGLVGLGLLYA-LTITN----- 1256
Cdd:COG4988 218 AEAERIAEASEDFRKRTMkvlrvaFLSSAV--LEFFA-SLSIALVA-------------VYIGFRLLGGsLTLFAalfvl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1257 ------YLNwvVRNLAdleVQ-------MGAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKP 1323
Cdd:COG4988 282 llapefFLP--LRDLG---SFyharangIAAAEKIFALLDAPEP----AAPAGTAPLPAAGPPSIELEDVSFSYPGG-RP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1324 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 1403
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1404 ---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1480
Cdd:COG4988 432 rlgRPDA--SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 3273501 1481 NILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1533
Cdd:COG4988 510 AEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
299-602 |
2.38e-68 |
|
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: 231.99 E-value: 2.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 299 LSSTFRYLADLLGFAGPLCISGIVQRVNEPKNnttrfsetlsskEFLENAHVLAVLLFLALILQRTFLQASYYVTIETGI 378
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD------------EPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 379 NLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAA 458
Cdd:cd18579 69 RVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 459 VIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIF 538
Cdd:cd18579 147 VLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSF 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 539 MNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 602
Cdd:cd18579 227 LFFSTPVLVSLATFATYVL-LGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
987-1282 |
1.61e-65 |
|
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: 224.33 E-value: 1.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 987 FFLLFLMIFSKllkhsviVAIDYWLATWTSEYSIND--PGKADQTFYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 1064
Cdd:cd18605 5 LLSLILMQASR-------NLIDFWLSYWVSHSNNSFfnFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1065 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYF 1144
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1145 IQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGA 1224
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 1225 CIV-----LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1282
Cdd:cd18605 238 LIVtfvalTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
987-1275 |
3.38e-64 |
|
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: 220.42 E-value: 3.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 987 FFLLFLMIFSKLLKhsviVAIDYWLATWTSeysiNDPGKAdQTFYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 1066
Cdd:cd18606 2 PLLLLLLILSQFAQ----VFTNLWLSFWTE----DFFGLS-QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1067 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYFIQ 1146
Cdd:cd18606 73 KALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1147 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 1226
Cdd:cd18606 153 NYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1227 VL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAV 1275
Cdd:cd18606 233 VLivALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSV 283
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1308-1518 |
3.56e-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: 3.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldatvteggenFSVGQRQLFCLARAFVRKSSILI 1467
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1468 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1518
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
986-1282 |
1.75e-61 |
|
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: 213.19 E-value: 1.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 986 GFFLLFLMIFSKLLKHSVIVAIDYWLATW--------------TSEYSINDPGKADQTFYVAGFSILCGAGIFLCLVTSL 1051
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgnttnnvdnSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1052 TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVF 1131
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1132 LIALAPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAA 1211
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 1212 NRWLEVRTDYLGACIVLTASIASISGSSNS--GLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1282
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSIspAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
362-602 |
3.45e-61 |
|
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: 211.56 E-value: 3.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 362 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 441
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 442 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 521
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 522 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQ 600
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 3273501 601 KL 602
Cdd:cd18595 289 RL 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
368-891 |
5.05e-59 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 214.64 E-value: 5.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 368 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFL-FLCPNLWAMPVQIIMGVILLY 446
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 447 NLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVEETRMKE 522
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREerelERFREANEELRRAN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 523 LSSLKTFALYTSLSIFMNAAIpIAAVLAtFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 602
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLG-LALVLL-VGGLLVLSGS-LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 603 NEFLLSDEIGEDswrtGEGTLPFEsckkhtgvqskpinrkqPGRYHLdnyeqarrlrpaETEDVAikvtngyFSWGSGLA 682
Cdd:COG1132 315 FELLDEPPEIPD----PPGAVPLP-----------------PVRGEI------------EFENVS-------FSYPGDRP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 683 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATV 762
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ----IGVVPQDTFLFSGTI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFGS-SFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 841
Cdd:COG1132 431 RENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 3273501 842 lSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:COG1132 511 -TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1308-1539 |
5.21e-57 |
|
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: 197.45 E-value: 5.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSS 1464
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDA--TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1465 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqEDGVFAS 1539
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1308-1538 |
5.65e-57 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 197.45 E-value: 5.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSS 1464
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 1465 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeDGVFA 1538
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYA 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1032-1539 |
5.71e-57 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 208.42 E-value: 5.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1032 VAGFSILCGAGIFlclVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 1111
Cdd:TIGR02203 60 VIGLAVLRGICSF---VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1112 RSTLLCLSAIGMI---SYATPVFLIALAPL-GVAFYFIQKYFRVASKDLQELD-DSTQLpllchFSETAEGLTTIRAFRH 1186
Cdd:TIGR02203 137 RETLTVIGLFIVLlyySWQLTLIVVVMLPVlSILMRRVSKRLRRISKEIQNSMgQVTTV-----AEETLQGYRVVKLFGG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1187 ETRFKQRmleltdtnniaYLFLSAANRWLEVRTDYLGACI-----VLTASIASISGSSNSGLVGLGLLYALTITNYLNWV 1261
Cdd:TIGR02203 212 QAYETRR-----------FDAVSNRNRRLAMKMTSAGSISspitqLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1262 ------VRNLADLEVQM----GAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAY 1331
Cdd:TIGR02203 281 ialirpLKSLTNVNAPMqrglAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1332 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPEcK 1408
Cdd:TIGR02203 355 IEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTE-Q 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1409 CTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1488
Cdd:TIGR02203 434 ADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALE 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1489 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeDGVFAS 1539
Cdd:TIGR02203 514 RLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
365-602 |
1.88e-55 |
|
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: 195.36 E-value: 1.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 365 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 444
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 445 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 524
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 525 SLKTFALYTSLSIFMNAAIPIAAVLATFVThAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 602
Cdd:cd18597 217 YVRKLQILRSILTAVAFSLPVLASMLSFIT-YYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
364-907 |
4.78e-55 |
|
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: 205.84 E-value: 4.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 364 TFLQASYYVTIETGINLRgaLLAMIYNKILRLSTSNL---SMGEMtLGQINNLVAIE---TNQLMWFLFLCPNLWampvq 437
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDL-ASRFRDVESIReflTGSLLTALLDLLFVL----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 438 IIMGVILLYNllGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYA--------WEH 509
Cdd:COG2274 285 IFLIVLFFYS--PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWEN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 510 IFCKSVEetrmKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVTHayasgNNLKPAEAFASLSLFHILVTPLF-LLS 586
Cdd:COG2274 363 LLAKYLN----ARFKLRRLSNLLSTLSGLLQQLATVALLWlgAYLVID-----GQLTLGQLIAFNILSGRFLAPVAqLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 587 TVVRFAvKAIISVQKLNEFLlsdeigedswrtgegTLPFEsckkHTGVQSKPINRKQPGRYHLDNyeqarrlrpaetedv 666
Cdd:COG2274 434 LLQRFQ-DAKIALERLDDIL---------------DLPPE----REEGRSKLSLPRLKGDIELEN--------------- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 aikVTNGYFswGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSrsry 746
Cdd:COG2274 479 ---VSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR---- 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 SVAYAAQKPWLLNATVEENITFG-SSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 825
Cdd:COG2274 550 QIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRN 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 826 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEH 905
Cdd:COG2274 630 PRILILDEATSALDAE-TEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
..
gi 3273501 906 WK 907
Cdd:COG2274 707 VQ 708
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1323-1543 |
1.66e-54 |
|
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: 190.44 E-value: 1.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1323 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 1402
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1403 L---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 1479
Cdd:cd03249 97 IrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 1480 ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeDGVFASFVRA 1543
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKA 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
663-899 |
3.14e-52 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 194.21 E-value: 3.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 663 TEDVAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRS 742
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 RsrysVAYAAQKPWLLNATVEENITFGS-SFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 821
Cdd:COG4988 412 Q----IAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 822 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 899
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1064-1541 |
3.99e-52 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 196.87 E-value: 3.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1064 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRS--TLLCLSAIgMIS---YATPVFLIALAPL 1138
Cdd:TIGR00958 236 IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNlvMLLGLLGF-MLWlspRLTMVTLINLPLV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1139 GVAFYFIQKYFRVASKDLQE-LDDSTQLPLlchfsETAEGLTTIRAFRHE----TRFKQ---RMLELTDTNNIAYLFLSA 1210
Cdd:TIGR00958 315 FLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFAAEegeaSRFKEaleETLQLNKRKALAYAGYLW 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1211 ANRWLE----VRTDYLGACIVLTASIASISgssnsgLVGLgLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL--TM 1284
Cdd:TIGR00958 390 TTSVLGmliqVLVLYYGGQLVLTGKVSSGN------LVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdrKP 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1285 ESENyEGTMDPSQVpehwpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD 1363
Cdd:TIGR00958 463 NIPL-TGTLAPLNL------EGLIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1364 GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGG 1442
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLtDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1443 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILE 1522
Cdd:TIGR00958 616 SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
490
....*....|....*....
gi 3273501 1523 YDTPESLLAQEDgVFASFV 1541
Cdd:TIGR00958 694 MGTHKQLMEDQG-CYKHLV 711
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
364-600 |
4.70e-52 |
|
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: 185.78 E-value: 4.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 364 TFLQASYYVTIETGINLRGALLAMIYNKILRL-----------------STSNLSMGEMTLGQINNLVAIETN---QLMW 423
Cdd:cd18596 54 LLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANrisEFAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 424 FLFLcpnLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK 503
Cdd:cd18596 134 FLHL---LVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 504 LYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLF 583
Cdd:cd18596 211 FFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLN 290
|
250
....*....|....*..
gi 3273501 584 LLSTVVRFAVKAIISVQ 600
Cdd:cd18596 291 VLPELITQLLQAKVSLD 307
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
986-1278 |
7.35e-52 |
|
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: 185.60 E-value: 7.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 986 GFFLLFLMIFSKLLKHSVIVAIDYWLATWTSEY---------------SINDPGKADQTFYVAGFSILCGAGIFLCLVTS 1050
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEeklndttdrvqgensTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1051 LTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPV 1130
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1131 FLIALAPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAY-LFLs 1209
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWfLFL- 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1210 AANRWLEVRTDYLGA--CIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKV 1278
Cdd:cd18601 240 ATSRWLAVRLDALCAlfVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1306-1532 |
1.77e-51 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 183.13 E-value: 1.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1306 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 1385
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSI 1465
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1466 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1045-1533 |
4.83e-51 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 191.47 E-value: 4.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1045 LCLVTSLTVEWMGLTA-AKNLHHN---LLNKIILG----------------PIRFFDTTPLGLILNRFSADTNIIDQHIP 1104
Cdd:PRK10790 61 LGLVAGLAAAYVGLQLlAAGLHYAqslLFNRAAVGvvqqlrtdvmdaalrqPLSAFDTQPVGQLISRVTNDTEVIRDLYV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1105 PTLESLTRSTLLcLSA--IGMISYATPVFLIALA--PLGVAFYFIQKYF------RVASKdLQELDDStqlpllchFSET 1174
Cdd:PRK10790 141 TVVATVLRSAAL-IGAmlVAMFSLDWRMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1175 AEGLTTIRAFRHETRFKQRMLELTDTNNIAylflsaanRWLEVRTD--------YLGACIVLTASIASISGSSNSGlVGL 1246
Cdd:PRK10790 211 INGMSVIQQFRQQARFGERMGEASRSHYMA--------RMQTLRLDgfllrpllSLFSALILCGLLMLFGFSASGT-IEV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1247 GLLYALTitNYLNWVVRNLADLE-----VQMGAVKKVNSFLTMESENYEGTMDPSQVpehwpQEGEIKIHDLCVRYENNl 1321
Cdd:PRK10790 282 GVLYAFI--SYLGRLNEPLIELTtqqsmLQQAVVAGERVFELMDGPRQQYGNDDRPL-----QSGRIDIDNVSFAYRDD- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1322 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 1401
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1402 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 1481
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1482 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1533
Cdd:PRK10790 514 AIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1306-1520 |
1.68e-49 |
|
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: 175.47 E-value: 1.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1306 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1385
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRK 1462
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1463 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1520
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1256-1539 |
3.04e-48 |
|
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: 183.10 E-value: 3.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1256 NYLNWVVR----NLADLEvQMGAVkkvnsfLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAY 1331
Cdd:COG5265 313 NFLGFVYReirqALADME-RMFDL------LDQPPE----VADAPDAPPLVVGGGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1332 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECk 1408
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDA- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1409 cTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1488
Cdd:COG5265 460 -SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1489 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeDGVFAS 1539
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQ 588
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1282-1545 |
2.40e-47 |
|
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: 182.08 E-value: 2.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1282 LTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDI 1361
Cdd:TIGR03797 432 LEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLLG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1362 FD----GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAT 1437
Cdd:TIGR03797 502 FEtpesGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1438 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFA--DRTVVTIAHRVHTILTADLVIVM 1515
Cdd:TIGR03797 582 ISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVL 657
|
250 260 270
....*....|....*....|....*....|
gi 3273501 1516 KRGNILEYDTPESLLAQEdGVFASFVRADM 1545
Cdd:TIGR03797 658 DAGRVVQQGTYDELMARE-GLFAQLARRQL 686
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
303-602 |
4.61e-47 |
|
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: 170.81 E-value: 4.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 303 FRYLADLLGFAGPLCISGIVQRVNEPKNnTTRFSETLSSKEFLENAhvlavllflalilQRTFLQASY-YVTIETGINLR 381
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFLEDSSE-PLSDGYLYALGLVLSSL-------------LGALLSSHYnFQMNKVSLKVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 382 GALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFlflCPNL---WAMPVQIIMGVILLYNLLGSSALVGAA 458
Cdd:cd18598 71 AALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGVAFLAGLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 459 VIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIF 538
Cdd:cd18598 146 FALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVY 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 539 MNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 602
Cdd:cd18598 226 FWATTPVLISILTFATYVL-MGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
668-884 |
2.10e-46 |
|
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: 164.48 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsry 746
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 sVAYAAQKPWLLNATVEENItfgssfnrqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNT 826
Cdd:cd03228 78 -IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 827 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDG 884
Cdd:cd03228 116 PILILDEATSALDPE-TEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1290-1542 |
5.33e-46 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 178.21 E-value: 5.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1290 EGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMV----DIFDGK 1365
Cdd:TIGR03796 460 EPEGSAATSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVaglyQPWSGE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1366 IVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGG 1442
Cdd:TIGR03796 536 ILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGG 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1443 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilqKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNI 1520
Cdd:TIGR03796 614 ANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKV 689
|
250 260
....*....|....*....|..
gi 3273501 1521 LEYDTPESLLAQEdGVFASFVR 1542
Cdd:TIGR03796 690 VQRGTHEELWAVG-GAYARLIR 710
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1316-1533 |
6.96e-46 |
|
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: 165.74 E-value: 6.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1316 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILF 1395
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1396 SGSIRFNL---DPECKCtdDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1472
Cdd:cd03252 89 NRSIRDNIalaDPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1473 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1533
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1024-1538 |
1.35e-45 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 174.82 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1024 GKADQTF------YVAGFSILCGAGIFlclVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTN 1097
Cdd:PRK11176 57 GKADRSVlkwmplVVIGLMILRGITSF---ISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1098 IIDQHIPPTLESLTRSTLLCLSAIGMI---SYATPVFLIALAPL-GVAFYFIQKYFRVASKDLQ----ELDDSTQLPLLC 1169
Cdd:PRK11176 134 QVASSSSGALITVVREGASIIGLFIMMfyySWQLSLILIVIAPIvSIAIRVVSKRFRNISKNMQntmgQVTTSAEQMLKG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1170 H---FSETAEGLTTIRAFRHETRFKQRMLELTDTNN--------IAYLFLSA---ANRWLEVRtDYLGA---CIVLTASi 1232
Cdd:PRK11176 214 HkevLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSisdpiiqlIASLALAFvlyAASFPSVM-DTLTAgtiTVVFSSM- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1233 asisgssnsglvgLGL---LYALTITNylnwvvrnlADLEVQMGAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIK 1309
Cdd:PRK11176 292 -------------IALmrpLKSLTNVN---------AQFQRGMAACQTLFAILDLEQEKDEGKRVIERA------KGDIE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1310 IHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIIL 1389
Cdd:PRK11176 344 FRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1390 QDPILFSGSIRFNLDPEC--KCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILI 1467
Cdd:PRK11176 424 QNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1468 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeDGVFA 1538
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYA 573
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
365-602 |
9.17e-45 |
|
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: 164.27 E-value: 9.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 365 FLQASYYVTIETGINLRGALLAMIYNKILRLStsnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 444
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 445 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 524
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 525 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 602
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAH-VALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
684-935 |
5.00e-43 |
|
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: 158.87 E-value: 5.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVywnnvnesepsfeatrsRSRYSVAYAAQKPWLLNATVE 763
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------------KHSGRISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 843
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 844 DHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHwktLMNRQdqelekdmEA 923
Cdd:cd03291 196 KEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSK---LMGYD--------TF 262
|
250
....*....|....*...
gi 3273501 924 DQTTLERK------TLRR 935
Cdd:cd03291 263 DQFSAERRnsilteTLRR 280
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1277-1543 |
1.48e-42 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 165.90 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1277 KVNSFLTME-----SENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1351
Cdd:PRK13657 305 KLEEFFEVEdavpdVRDPPGAIDLGRV------KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1352 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVK 1428
Cdd:PRK13657 378 INLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRPDA--TDEEMRAAAERAQAHDFIE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1429 SLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT 1508
Cdd:PRK13657 456 RKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN 535
|
250 260 270
....*....|....*....|....*....|....*
gi 3273501 1509 ADLVIVMKRGNILEYDTPESLLAQeDGVFASFVRA 1543
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVAR-GGRFAALLRA 569
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
655-891 |
3.24e-42 |
|
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: 164.55 E-value: 3.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 655 ARRL------RPAETE---------DVAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEM 718
Cdd:COG4987 306 ARRLnelldaPPAVTEpaepapapgGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 719 QTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVEENITFGssfnR-----QRYKAVTDACSLQPDIDLL 793
Cdd:COG4987 386 DPQSGSITLGGVDLRDLDEDDLRRR----IAVVPQRPHLFDTTLRENLRLA----RpdatdEELWAALERVGLGDWLAAL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 794 PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTVVLVTHKLQYLT 873
Cdd:COG4987 458 PDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLE 534
|
250
....*....|....*...
gi 3273501 874 HADWIIAMKDGSVLREGT 891
Cdd:COG4987 535 RMDRILVLEDGRIVEQGT 552
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
668-907 |
6.41e-41 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 151.23 E-value: 6.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSrsryS 747
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLLNATVEENITFG--SSFNRQRYKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 825
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYGrpDATDEEVIEAAKAAQ-IHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 826 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEH 905
Cdd:cd03253 156 PPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
..
gi 3273501 906 WK 907
Cdd:cd03253 233 WK 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1170-1515 |
9.57e-41 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 158.99 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1170 HFSETAEGLTTIRAFRHETRFKQRMLELTD--------TNNIAylFLSAANrwLEVRTDyLGACIVLTAsiasisgssns 1241
Cdd:TIGR02857 185 HFLDRLRGLPTLKLFGRAKAQAAAIRRSSEeyrertmrVLRIA--FLSSAV--LELFAT-LSVALVAVY----------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1242 glVGLGLLY-------ALTI-----TNYLNwvVRNL-ADLEVQMGAVKKVNSFLTMESENyeGTMDPSQVPEHWPQEGEI 1308
Cdd:TIGR02857 249 --IGFRLLAgdldlatGLFVlllapEFYLP--LRQLgAQYHARADGVAAAEALFAVLDAA--PRPLAGKAPVTAAPASSL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1309 KIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1388
Cdd:TIGR02857 323 EFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1389 LQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSI 1465
Cdd:TIGR02857 402 PQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 3273501 1466 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVM 1515
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
365-603 |
1.75e-40 |
|
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: 152.02 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 365 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 444
Cdd:cd18594 55 LHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 445 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 524
Cdd:cd18594 133 LWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 525 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPL-FLLSTVVRFAVKAIISVQKLN 603
Cdd:cd18594 213 LIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVL-TGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
668-891 |
2.62e-40 |
|
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: 149.30 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrys 747
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLLNATVEENITFGSSFNRQ-RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 826
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 827 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:cd03254 159 KILILDEATSNIDTE-TEKLIQEALEKLMKG--RTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1064-1543 |
1.21e-38 |
|
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: 155.67 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1064 LHHNLLNKIILG--------PIRFFDTTPLGLILNRFSADTNIIDqhippTLESLTRSTLLCLSAIGMISYA-----TPV 1130
Cdd:TIGR01193 223 LGQRLSIDIILSyikhlfelPMSFFSTRRTGEIVSRFTDASSIID-----ALASTILSLFLDMWILVIVGLFlvrqnMLL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1131 FLIALAPLGVAFYFIQKYFRVASKDLQELDDSTQLpLLCHFSETAEGLTTIRAFRHE-TRFKQ----------RMLELTD 1199
Cdd:TIGR01193 298 FLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAV-LNSSIIEDLNGIETIKSLTSEaERYSKidsefgdylnKSFKYQK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1200 TNNIAYLFLSAANRWLEVRTDYLGACIVLTASIAsisgssnsglVGLGLLYALTITNYLNwVVRNLADLEVQMGAVK--- 1276
Cdd:TIGR01193 377 ADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLT----------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvan 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1277 -KVNSFLTMESE-NYEGTMDPSQVPEhwpqeGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLA 1354
Cdd:TIGR01193 446 nRLNEVYLVDSEfINKKKRTELNNLN-----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1355 FFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPG 1432
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1433 GLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILTAD 1510
Cdd:TIGR01193 600 GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSD 676
|
490 500 510
....*....|....*....|....*....|...
gi 3273501 1511 LVIVMKRGNILEYDTPESLLAQeDGVFASFVRA 1543
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELLDR-NGFYASLIHN 708
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
678-891 |
1.36e-37 |
|
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: 141.60 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 678 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSrsrySVAYAAQKPWL 757
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR----QIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 LNATVEENITFGSS-FNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:cd03251 88 FNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 837 ALDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:cd03251 168 ALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1303-1502 |
1.80e-37 |
|
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: 149.43 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1303 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1382
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1383 SRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAF 1459
Cdd:TIGR02868 409 RRVSVCAQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3273501 1460 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1502
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
682-890 |
7.98e-37 |
|
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: 138.88 E-value: 7.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 682 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSfeatRSRSRYSVAYAAQKPWLLNAT 761
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD----PADLRRNIGYVPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFGSSF-NRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 840
Cdd:cd03245 94 LRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 3273501 841 HLSDHLMQEgiLKFLQDDKrTVVLVTHKLQYLTHADWIIAMKDGSVLREG 890
Cdd:cd03245 174 NSEERLKER--LRQLLGDK-TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1273-1543 |
8.71e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.45 E-value: 8.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1273 GAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS 1352
Cdd:PRK11174 319 GAAESLVTFLETPLA----HPQQGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1353 ---LAFFRmvdiFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNM 1426
Cdd:PRK11174 394 nalLGFLP----YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1427 VKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI 1506
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 3273501 1507 LTADLVIVMKRGNILE---YDTpeslLAQEDGVFASFVRA 1543
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
684-891 |
3.23e-36 |
|
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: 137.67 E-value: 3.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVE 763
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ----IGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGSsfNRQRYKAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 840
Cdd:cd03249 95 ENIRYGK--PDATDEEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 841 HlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:cd03249 173 E-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1303-1538 |
1.99e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 143.81 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1303 PQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1382
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1383 SRLSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSlPGGLDATVTEGGENFSVGQRQLFCLARAF 1459
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1460 VRKSSILIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEDGVFA 1538
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
662-881 |
4.15e-35 |
|
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: 142.04 E-value: 4.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 662 ETEDVAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesePSFEATR 741
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV----PLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 742 SRSRYSVAYAAQKPWLLNATVEENITFGssfnrQRY------KAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQR 815
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLA-----RPDasdaeiREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 816 ICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAM 881
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAE-TEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
684-903 |
6.80e-35 |
|
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: 134.40 E-value: 6.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSfeaTRSRSRYsVAYAAQK---PWLLna 760
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS---RRELARR-IAYVPQEppaPFGL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITFG--------SSFNRQRYKAVTDACslqpdidllpfgDQTEIG---ERGIN-LSGGQRQRICVARALYQNTNI 828
Cdd:COG1120 91 TVRELVALGryphlglfGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeLSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 829 VFLDDPFSALDIHlsdHlmQEGILKFLQD----DKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQTKDV--E 901
Cdd:COG1120 159 LLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTPELleE 233
|
..
gi 3273501 902 LY 903
Cdd:COG1120 234 VY 235
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1296-1520 |
2.82e-34 |
|
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: 131.82 E-value: 2.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1296 SQVPEHWpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS 1374
Cdd:cd03248 2 SLAPDHL--KGIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1375 KLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLF 1453
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQsCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1520
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
663-905 |
3.92e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.14 E-value: 3.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 663 TEDVAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNesepsfeATRS 742
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-------PRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 RSRysVAYAAQK---PWLLNATVEE--------NITFGSSFNRQRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGG 811
Cdd:COG1121 74 RRR--IGYVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 812 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYL-THADWIIAMKDGsVLREG 890
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVrEYFDRVLLLNRG-LVAHG 220
|
250
....*....|....*..
gi 3273501 891 TLKDIQTKDV--ELYEH 905
Cdd:COG1121 221 PPEEVLTPENlsRAYGG 237
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1308-1520 |
8.26e-34 |
|
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: 128.49 E-value: 8.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIF---DGKIVIDGIDISKLPLHTLRSR 1384
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLrptSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldatvteggenFSVGQRQLFCLARAFVRKSS 1464
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1465 ILIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1520
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
369-576 |
1.14e-33 |
|
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: 132.34 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 369 SYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQL-MWFLFLcPNLWAMPVQIIMGVILLYN 447
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 448 LLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLK 527
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3273501 528 TFALYTSlsifMNAAIPIAA----VLATFVTHAYaSGNNLKPAEAFASLSLFH 576
Cdd:cd18593 217 RTSFLRA----LNMGLFFVSskliLFLTFLAYIL-LGNILTAERVFVTMALYN 264
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1308-1532 |
2.30e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 137.54 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCvrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:PRK10789 316 VNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSIL 1466
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1467 IMDEATASIDMATE-NILQKVVMTAfADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:PRK10789 474 ILDDALSAVDGRTEhQILHNLRQWG-EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
669-884 |
5.23e-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: 127.58 E-value: 5.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 669 KVTNGYFSWGSGL-ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrys 747
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKP--WLLNATVEENITFGSSFN-------RQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICV 818
Cdd:cd03225 77 VGLVFQNPddQFFGPTVEEEVAFGLENLglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 819 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYL-THADWIIAMKDG 884
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
478-1542 |
3.44e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 137.47 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 478 QKSTLDYSTERLKKTNEILKGIKLLKLYAWEHifcksveeTRMKELS-SLKTFALYTSLSIFMNAaIPIAaVLATFVTHA 556
Cdd:PTZ00265 225 KKTSLLYNNNTMSIIEEALVGIRTVVSYCGEK--------TILKKFNlSEKLYSKYILKANFMES-LHIG-MINGFILAS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 557 YASG------------NNLKPAEAFASLSLFHILV---TPLFLLSTV---VRFAVKAIISVQKLNEFLLSDEIGEDSwRT 618
Cdd:PTZ00265 295 YAFGfwygtriiisdlSNQQPNNDFHGGSVISILLgvlISMFMLTIIlpnITEYMKSLEATNSLYEIINRKPLVENN-DD 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 619 GEgTLPfeSCKKhtgVQSKPInrkqpgRYHLDNyeqarrlrpaeTEDVAIkvtngyfswgsglatLSNIDIRIPTGQLTM 698
Cdd:PTZ00265 374 GK-KLK--DIKK---IQFKNV------RFHYDT-----------RKDVEI---------------YKDLNFTLTEGKTYA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 699 IVGQVGCGKSSLLLAILGEMQTLEGKVYwnnVNESEPSFEATRSRSRYSVAYAAQKPWLLNATVEENITFG--------- 769
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDII---INDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlea 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 770 -------SSFNRQRYKAVTDACSLQPDIDL------------------------------------------LPFGDQTE 800
Cdd:PTZ00265 493 lsnyyneDGNDSQENKNKRNSCRAKCAGDLndmsnttdsneliemrknyqtikdsevvdvskkvlihdfvsaLPDKYETL 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 801 IGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTVVLVTHKLQYLTHADWIIA 880
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFV 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 881 MK--------DGSVLREGTLKDIQTKD--------------------------VELYEH----------WKTLMNRQ--- 913
Cdd:PTZ00265 652 LSnrergstvDVDIIGEDPTKDNKENNnknnkddnnnnnnnnnnkinnagsyiIEQGTHdalmknkngiYYTMINNQkvs 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 914 -------DQELEKDM------------EADQTTLERKTLRRAMySREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMP 974
Cdd:PTZ00265 732 skkssnnDNDKDSDMkssaykdsergyDPDEMNGNSKHENESA-SNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKAP 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 975 ------WKTCWWY-----------LTSGGFFLLFLMIFSKLlkhsVIVAIDYW-LATWTSEYSIndpgkadqtfyvagFS 1036
Cdd:PTZ00265 811 nnlrivYREIFSYkkdvtiialsiLVAGGLYPVFALLYAKY----VSTLFDFAnLEANSNKYSL--------------YI 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1037 ILCGAGIFLC-LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDT---TPlGLILNRFSADTNIIDQHIPPTLESLTR 1112
Cdd:PTZ00265 873 LVIAIAMFISeTLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTH 951
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1113 STLLCLSAIGMISYATPVflIALAPLGVAFYFIqKYFRV-----ASKDLQELDDSTQLPLLCHFS-------------ET 1174
Cdd:PTZ00265 952 FIVLFLVSMVMSFYFCPI--VAAVLTGTYFIFM-RVFAIrarltANKDVEKKEINQPGTVFAYNSddeifkdpsfliqEA 1028
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1175 AEGLTTIRAFRHETRFKQRMLELTDTNN------------------IAYLFLSAANRW----------LEVrTDYLGAci 1226
Cdd:PTZ00265 1029 FYNMNTVIIYGLEDYFCNLIEKAIDYSNkgqkrktlvnsmlwgfsqSAQLFINSFAYWfgsflirrgtILV-DDFMKS-- 1105
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1227 VLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNlADLEVQ-MGAVKKVNSFLTmesenyegtmdpsqvpehwpqE 1305
Cdd:PTZ00265 1106 LFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRK-SNIDVRdNGGIRIKNKNDI---------------------K 1163
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1306 GEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD--------------------- 1363
Cdd:PTZ00265 1164 GKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyq 1243
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1364 ---------------------------------GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD-PECKC 1409
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKEDA 1323
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1410 TDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV-- 1487
Cdd:PTZ00265 1324 TREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvd 1403
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1488 MTAFADRTVVTIAHRVHTILTADLVIVM----KRGNILE-YDTPESLLAQEDGVFASFVR 1542
Cdd:PTZ00265 1404 IKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKKYVK 1463
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
668-895 |
3.92e-32 |
|
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: 125.52 E-value: 3.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrys 747
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPW--LLNATVEENITFGssfnrqrykavtdacslqpdidLLPFG-DQTEIGER--------GI---------N 807
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEEDVAFG----------------------PENLGlPREEIRERveealelvGLehladrpphE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 808 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMKDGSV 886
Cdd:COG1122 135 LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRI 212
|
....*....
gi 3273501 887 LREGTLKDI 895
Cdd:COG1122 213 VADGTPREV 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
668-891 |
5.69e-32 |
|
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: 124.91 E-value: 5.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsry 746
Cdd:cd03244 3 IEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 sVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 826
Cdd:cd03244 80 -ISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 827 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:cd03244 159 KILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1308-1522 |
1.20e-31 |
|
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: 122.42 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRLSI 1387
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldatvtegGENFSVGQRQLFCLARAFVRKSSILI 1467
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1468 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILE 1522
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
459-899 |
2.56e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 131.38 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 459 VIVLLAPIQYFIATKLA--------EAQKSTLDYSTerlkKTNEILKGIKLLKLYAWEHI----FCKSVEETRMKELSSL 526
Cdd:TIGR02203 159 IVVVMLPVLSILMRRVSkrlrriskEIQNSMGQVTT----VAEETLQGYRVVKLFGGQAYetrrFDAVSNRNRRLAMKMT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 527 KTFALYTSLSIFMnAAIPIAAVLatFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFL 606
Cdd:TIGR02203 235 SAGSISSPITQLI-ASLALAVVL--FIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 607 lsDEIGEdswrtgegtlpfesckkhtgvqskpinrKQPGRYHLDNYEQARRLRpaetedvAIKVTNGyfswGSGLATLSN 686
Cdd:TIGR02203 312 --DSPPE----------------------------KDTGTRAIERARGDVEFR-------NVTFRYP----GRDRPALDS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 687 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVEENI 766
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ----VALVSQDVVLFNDTIANNI 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 767 TFG--SSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSD 844
Cdd:TIGR02203 427 AYGrtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE-SE 505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 845 HLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 899
Cdd:TIGR02203 506 RLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
663-895 |
2.68e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.43 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 663 TEDVAIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEa 739
Cdd:COG1116 3 AAAPALELRGvskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 740 trsrsrysVAYAAQK----PWLlnaTVEENITFGSSFN----RQRYKAVTDACSLqpdIDLLPFGD----Qteigergin 807
Cdd:COG1116 82 --------RGVVFQEpallPWL---TVLDNVALGLELRgvpkAERRERARELLEL---VGLAGFEDayphQ--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 808 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTHKLQ---YLthADWIIAMKDg 884
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDE-LLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSA- 214
|
250
....*....|.
gi 3273501 885 svlREGTLKDI 895
Cdd:COG1116 215 ---RPGRIVEE 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1308-1534 |
4.50e-31 |
|
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: 122.83 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPI--LFSGSIR---------FNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLA 1456
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpenLGLPREE--IRERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1457 RAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQED 1534
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1309-1518 |
1.41e-30 |
|
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: 118.50 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1309 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1388
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1389 LQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldatvteggenFSVGQRQLFCLARAFVRKSSILIM 1468
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1469 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTA-DLVIVMKRG 1518
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
990-1228 |
1.52e-30 |
|
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: 122.75 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 990 LFLMIFSKLLKHSVIVAIDYWLATWTSEYS-INDPGKADQTFYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNL 1068
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1069 LNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYFIQKY 1148
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1149 FRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVL 1228
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
684-916 |
1.56e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 129.19 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVE 763
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH----LSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFG-SSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 842
Cdd:PRK11174 441 DNVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH- 519
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 843 SDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQE 916
Cdd:PRK11174 520 SEQLVMQALNAASRR--QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT-----LLAHRQE 586
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
668-895 |
1.62e-30 |
|
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: 121.44 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGS-GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsry 746
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 sVAYAAQKPWLLNATVEENITFG-SSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 825
Cdd:cd03252 78 -VGVVLQENVLFNRSIRDNIALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 826 TNIVFLDDPFSALDIHlSDHLMQEGILKFLqdDKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03252 157 PRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
668-904 |
1.74e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 121.73 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQtlEGKVYWNNVNESE-PSFE-ATRsr 743
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrLLPPD--SGEVLVDGLDVATtPSRElAKR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 744 srysVAYAAQKPWL-LNATVEENITFGssfnrqRY------------KAVTDAcslqpdIDLLpfgDQTEIGERGIN-LS 809
Cdd:COG4604 77 ----LAILRQENHInSRLTVRELVAFG------RFpyskgrltaedrEIIDEA------IAYL---DLEDLADRYLDeLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 810 GGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTVVLVTHKLQYLTH-ADWIIAMKDGSVL 887
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
250
....*....|....*....
gi 3273501 888 REGTLKDIQTKDV--ELYE 904
Cdd:COG4604 216 AQGTPEEIITPEVlsDIYD 234
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
684-891 |
2.42e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 128.29 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVE 763
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR----LAVVSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGS-SFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 842
Cdd:PRK10789 407 NNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR- 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 843 SDHlmqeGILKFLQD--DKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:PRK10789 486 TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
670-889 |
2.49e-30 |
|
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: 120.27 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 670 VTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEatrsrsrysVA 749
Cdd:cd03293 6 VSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---------RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 750 YAAQK----PWLlnaTVEENITFGSSFN-------RQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICV 818
Cdd:cd03293 77 YVFQQdallPWL---TVLDNVALGLELQgvpkaeaRERAEELLELVGLSGFENAYP--HQ---------LSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 819 ARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTVVLVTHKLQ---YLthADWIIAM--KDGSVLRE 889
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALD-ALTREQLQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
669-890 |
8.68e-30 |
|
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: 117.15 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 669 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFeatRSRSRYsV 748
Cdd:cd03214 1 EVENLSVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP---KELARK-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 749 AYAAQkpwLLNATveenitfgssfnrqrykavtdacslqpdiDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTN 827
Cdd:cd03214 76 AYVPQ---ALELL-----------------------------GLAHLAD------RPFNeLSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 828 IVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTVVLVTHKL-QYLTHADWIIAMKDGSVLREG 890
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLE--LLRRLARERgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1308-1518 |
8.75e-30 |
|
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: 117.96 E-value: 8.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENN---LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgidisklplhTLRSR 1384
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIILQDPILFSGSIRFN------LDPEckctddRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARA 1458
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpFDEE------RYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1459 FVRKSSILIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRG 1518
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
678-886 |
9.20e-30 |
|
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: 126.40 E-value: 9.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 678 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVY--------WNNvnesepsfeatRSRSRYsVA 749
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqWDR-----------EELGRH-IG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 750 YAAQKPWLLNATVEENItfgssfnrqrykavtdACSLQPD----------------IDLLPFGDQTEIGERGINLSGGQR 813
Cdd:COG4618 410 YLPQDVELFDGTIAENI----------------ARFGDADpekvvaaaklagvhemILRLPDGYDTRIGEGGARLSGGQR 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 814 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSV 886
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA--AIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
382-869 |
1.36e-29 |
|
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: 125.55 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 382 GALLAMIYNKILRLS---TSNLSMGEMtlgqINNLVA-IETNQLMWFLFLCPNLWAMPVQII--MGVILLYNLLGSSALV 455
Cdd:TIGR02868 86 GALRVRVYERLARQAlagRRRLRRGDL----LGRLGAdVDALQDLYVRVIVPAGVALVVGAAavAAIAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 456 GAAVIVLLAPiqyFIATKLAEAQKSTLDYS-TERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 534
Cdd:TIGR02868 162 GLLLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 535 LSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVT-PLFLLSTVVRFAVKAIISVQKLNEFLlsdeigE 613
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeAFAALPAAAQQLTRVRAAAERIVEVL------D 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 614 DSWRTGEGTLPfesckkhtgvQSKPINRKQPGRyhldnyeqarrlrpaETEDVAikvtngyFSWGSGLATLSNIDIRIPT 693
Cdd:TIGR02868 313 AAGPVAEGSAP----------AAGAVGLGKPTL---------------ELRDLS-------AGYPGAPPVLDGVSLDLPP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 694 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVEENITFGSsfn 773
Cdd:TIGR02868 361 GERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFDTTVRENLRLAR--- 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 774 rqryKAVTD--------ACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 845
Cdd:TIGR02868 434 ----PDATDeelwaaleRVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
490 500
....*....|....*....|....
gi 3273501 846 LMqEGILKflQDDKRTVVLVTHKL 869
Cdd:TIGR02868 510 LL-EDLLA--ALSGRTVVLITHHL 530
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
662-882 |
1.70e-29 |
|
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: 117.63 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 662 ETEDVAikvtngyFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNnvnesepSFEATR 741
Cdd:cd03235 1 EVEDLT-------VSYGGHPV-LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-------GKPLEK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 742 SRSRysVAYAAQK---PWLLNATVEE--------NITFGSSFNRQRYKAVTDAcslqpdidlLPFGDQTEIGERGI-NLS 809
Cdd:cd03235 66 ERKR--IGYVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 810 GGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMK 882
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIY--ELLRELRREGMTILVVTHDLGLVLeYFDRVLLLN 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
662-884 |
1.76e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.22 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 662 ETEDVAIKVTNGYFswgsglatLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEpsFEATR 741
Cdd:COG4619 2 ELEGLSFRVGGKPI--------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 742 SRSRysVAYAAQKPWLLNATVEENITFGSSFNRQRYkavtdacSLQPDIDLLP-FGDQTEIGERGI-NLSGGQRQRICVA 819
Cdd:COG4619 72 WRRQ--VAYVPQEPALWGGTVRDNLPFPFQLRERKF-------DRERALELLErLGLPPDILDKPVeRLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 820 RALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDG 884
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRV-EELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
683-898 |
1.79e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 125.15 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 683 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEaTRSRSrysVAYAAQKPWLLNATV 762
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE-TFGKH---IGYLPQDVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENIT-FGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 841
Cdd:TIGR01842 409 AENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 842 LSDHLMQEgiLKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTK 898
Cdd:TIGR01842 489 GEQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
668-884 |
5.15e-29 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 116.44 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVYWNNVNESEPSfEATRSR 743
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVRVDGTDISKLS-EKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 744 -SRYSVAYAAQKPWLLNA-TVEENITFGSSFNRQRYKAVTDACslqpdIDLLpfgDQTEIGERgIN-----LSGGQRQRI 816
Cdd:cd03255 79 fRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERA-----EELL---ERVGLGDR-LNhypseLSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 817 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDG 884
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
669-884 |
1.06e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.11 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 669 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysV 748
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR----I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 749 AYAAQkpwllnatveenitfgssfnrqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNI 828
Cdd:cd00267 76 GYVPQ------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 829 VFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTHA-DWIIAMKDG 884
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
303-602 |
1.44e-28 |
|
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: 117.32 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 303 FRYLADLLGFAGPLCIS---GIVQRVNEPKNNTTRFSETLSSKEFLENAhvlavllflalilqrTFLQASYYVTIeTGIN 379
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWlllWFDDPVNGPQEHGQVYLSVLGALAILQGI---------------TVFQYSMAVSI-GGIF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 380 LRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAV 459
Cdd:cd18559 69 ASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 460 IVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFM 539
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 540 NAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 602
Cdd:cd18559 227 WCVGPCIVLFASFFAYVSRHSLAgLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
684-836 |
5.05e-28 |
|
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: 111.20 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNA-TV 762
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE----IGYVFQDPQLFPRlTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 763 EENITFGSSFnrQRYKAVTDACSLQPDIDLLPFGDQ--TEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:pfam00005 77 RENLRLGLLL--KGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
676-890 |
6.15e-28 |
|
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: 113.00 E-value: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 676 SWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESepsfeaTRSRSRYSVAYAAQK- 754
Cdd:cd03259 9 TYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT------GVPPERRNIGMVFQDy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 755 ---PWLlnaTVEENITFGSSFN-------RQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQ 824
Cdd:cd03259 82 alfPHL---TVAENIAFGLKLRgvpkaeiRARVRELLELVGLEGLLNRYP--HE---------LSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 825 NTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTHKLQ-YLTHADWIIAMKDGSVLREG 890
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
684-886 |
1.01e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.15 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesePSFEATRSRSRYSVAYAAQKPWLLNATVE 763
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA----DISQWDPNELGDHVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENItfgssfnrqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 843
Cdd:cd03246 94 ENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3273501 844 DHLMQegILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSV 886
Cdd:cd03246 133 RALNQ--AIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
665-889 |
1.36e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.44 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 665 DVAIKVTNGYFSWGSGLAT---LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVYWNNVNESEPSfEAT 740
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVLIDGQDISSLS-ERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 741 RSRSR-YSVAYAAQKPWLL-NATVEENITFGSSFNRQRYKAVTDACslqpdIDLLpfgDQTEIGERgIN-----LSGGQR 813
Cdd:COG1136 80 LARLRrRHIGFVFQFFNLLpELTALENVALPLLLAGVSRKERRERA-----RELL---ERVGLGDR-LDhrpsqLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 814 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFL-QDDKRTVVLVTHKLQYLTHADWIIAMKDGSVLRE 889
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE--LLRELnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1308-1532 |
1.40e-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: 119.24 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI---FDGKIVIDGIDISKLPLHTLRSR 1384
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIILQDPI--LFSGSIRFNLD--PECKCTD-----DRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCL 1455
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAeaLENLGLSraearARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1456 ARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1528
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....
gi 3273501 1529 LLAQ 1532
Cdd:COG1123 230 ILAA 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1309-1518 |
1.41e-27 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 111.79 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1309 KIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1388
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1389 LQDP--ILFSGSIR----FNLDPECKCTDD---RLWEALEIAQLKNMVKSLPggldatvteggENFSVGQRQLFCLARAF 1459
Cdd:cd03225 81 FQNPddQFFGPTVEeevaFGLENLGLPEEEieeRVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1460 VRKSSILIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG 1518
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1308-1523 |
1.94e-27 |
|
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: 112.21 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---R 1382
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1383 SRLSIILQDPILfsgsirfNLDP------------ECKCTDDRLWEALEIAQLKNMVKSLPGG-LDATVTEggenFSVGQ 1449
Cdd:cd03257 82 KEIQMVFQDPMS-------SLNPrmtigeqiaeplRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHE----LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1450 RQLFCLARAFVRKSSILIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTIL-TADLVIVMKRGNILEY 1523
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAkIADRVAVMYAGKIVEE 227
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
991-1276 |
2.24e-27 |
|
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: 113.85 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 991 FLMIFSKLLKHSVIVAIDYWLATWTseysiNDPGKADQT---FYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHN 1067
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWF-----DDPVNGPQEhgqVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1068 LLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLIALaPLGVAFYFIQK 1147
Cdd:cd18559 77 LYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGI-PLGLLYVPVNR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1148 YFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDtNNIAYLFLSAANRWLEVRTDYLGACIV 1227
Cdd:cd18559 156 VYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIV 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 3273501 1228 -LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVK 1276
Cdd:cd18559 235 lFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAE 284
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
668-902 |
3.80e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 111.44 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSfEATRSRSRYS 747
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLS-EAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLLNA-TVEENITFG----SSFNRQRYKAVT----DACSLQPDIDLLPfgdqteigergINLSGGQRQRICV 818
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPlrehTRLSEEEIREIVleklEAVGLRGAEDLYP-----------AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 819 ARALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKfLQDDKR-TVVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDIQ 896
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASG-VIDDLIRS-LKKELGlTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELR 225
|
....*.
gi 3273501 897 TKDVEL 902
Cdd:cd03261 226 ASDDPL 231
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
684-909 |
6.19e-27 |
|
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: 117.88 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVE 763
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR----MALVPQDPVLFAASVM 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGS-SFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhL 842
Cdd:TIGR02204 432 ENIRYGRpDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA-E 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 843 SDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDvELYEHWKTL 909
Cdd:TIGR02204 511 SEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG-GLYARLARL 574
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1308-1529 |
2.40e-26 |
|
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: 108.81 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLH--T 1380
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 LRSRLSIILQDPILFSGSIRFNLD--------PECKCTDDRLWEALEIAQLKNMVKSLPGGLDatvteggenFSVGQRQL 1452
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1453 FCLARAFVRKSSILIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESL 1529
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
368-582 |
2.73e-26 |
|
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: 110.04 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 368 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYN 447
Cdd:pfam00664 60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 448 LLG-SSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSL 526
Cdd:pfam00664 138 YYGwKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAG 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 527 KTFALYTSLSI-FMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPL 582
Cdd:pfam00664 218 IKKAVANGLSFgITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1305-1532 |
5.80e-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: 114.85 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1305 EGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIFD---GKIVIDGIDISKLPlhtl 1381
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVWPptaGSVRLDGADLSQWD---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 RSRLSIIL----QDPILFSGSI-----RFNlDPeckcTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQL 1452
Cdd:COG4618 401 REELGRHIgylpQDVELFDGTIaeniaRFG-DA----DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1453 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1531
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
.
gi 3273501 1532 Q 1532
Cdd:COG4618 556 R 556
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
668-901 |
5.88e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 108.41 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEAtrsrsRYS 747
Cdd:COG4555 2 IEVENLSKKYGKVPA-LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-----RRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWL-LNATVEENITFGSSFN---RQRYKAVTDacSLQPDIDLLPFGDQTeIGErginLSGGQRQRICVARALY 823
Cdd:COG4555 76 IGVLPDERGLyDRLTVRENIRYFAELYglfDEELKKRIE--ELIELLGLEEFLDRR-VGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 824 QNTNIVFLDDPFSALDIhLSDHLMQEgILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVE 901
Cdd:COG4555 149 HDPKVLLLDEPTNGLDV-MARRLLRE-ILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
668-895 |
6.15e-26 |
|
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: 108.16 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWN--NVNESEPSfeatrsRSR 745
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgeDIREQDPV------ELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 746 YSVAYAAQKPWLL-NATVEENITFGSSFNR-QRYKAVTDACSLQPDIDLLPfgdqTEIGER-GINLSGGQRQRICVARAL 822
Cdd:cd03295 75 RKIGYVIQQIGLFpHMTVEENIALVPKLLKwPKEKIRERADELLALVGLDP----AEFADRyPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 823 YQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTVVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
654-903 |
1.44e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 113.07 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 654 QARRLRPAETEDVAIKVTN---GYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN 729
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNlskRYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 730 VNESEPSFEATRSRSRySVAYAAQKPWL-LNA--TVEENITFGSSFNR-----QRYKAVT---DACSLQPD-IDLLPFGd 797
Cdd:COG1123 327 KDLTKLSRRSLRELRR-RVQMVFQDPYSsLNPrmTVGDIIAEPLRLHGllsraERRERVAellERVGLPPDlADRYPHE- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 798 qteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TVVLVTHKL---Q 870
Cdd:COG1123 405 ----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvR 469
|
250 260 270
....*....|....*....|....*....|...
gi 3273501 871 YLthADWIIAMKDGSVLREGTLKDIQTKDVELY 903
Cdd:COG1123 470 YI--ADRVAVMYDGRIVEDGPTEEVFANPQHPY 500
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
684-895 |
2.33e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.30 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYwnnVNESEPSFEATRSRSRysVAYAAQKPWL-LNATV 762
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR---VLGEDVARDPAEVRRR--IGYVPQEPALyPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFGSSF-------NRQRYKAVTDACSLQPDIDllpfgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDDPF 835
Cdd:COG1131 91 RENLRFFARLyglprkeARERIDELLELFGLTDAAD-----------RKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 836 SALDIHLSDHLMQegILKFLQDDKRTVVLVTHklqYLTHA----DWIIAMKDGSVLREGTLKDI 895
Cdd:COG1131 160 SGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDEL 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
675-895 |
2.38e-25 |
|
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: 113.68 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 675 FSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSfeatRSRSRYSVAYAAQK 754
Cdd:TIGR01193 481 YSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID----RHTLRQFINYLPQE 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 755 PWLLNATVEENITFGSSFN--RQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 832
Cdd:TIGR01193 557 PYIFSGSILENLLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 833 DPFSALDIhLSDHLMQEGILkFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:TIGR01193 637 ESTSNLDT-ITEKKIVNNLL-NLQD--KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
668-884 |
2.66e-25 |
|
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: 104.19 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRys 747
Cdd:cd03229 1 LELKNVSKRYGQKTV-LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLL-NATVEENITFGssfnrqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNT 826
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 827 NIVFLDDPFSALDIhlsdhLMQEGILKFLQD----DKRTVVLVTHKLQYLTH-ADWIIAMKDG 884
Cdd:cd03229 120 DVLLLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
668-899 |
2.69e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 112.80 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVYWNNVNESEPSFEATRSRs 744
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDID--EGEILLDGHDLRDYTLASLRNQ- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 745 rysVAYAAQKPWLLNATVEENITFGSSFNRQRY---KAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 821
Cdd:PRK11176 419 ---VALVSQNVHLFNDTIANNIAYARTEQYSREqieEAARMAYAMD-FINKMDNGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 822 LYQNTNIVFLDDPFSALDIHlSDHLMQEGiLKFLQDDkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 899
Cdd:PRK11176 495 LLRDSPILILDEATSALDTE-SERAIQAA-LDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
668-903 |
2.89e-25 |
|
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: 106.11 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRS-RSRy 746
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlRRQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 sVAYAAQKPWLLN-ATVEENITFG---------SSFNRQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRI 816
Cdd:cd03256 80 -IGMIFQQFNLIErLSVLENVLSGrlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 817 CVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTVVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVM-DLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
....*....
gi 3273501 896 QTKDV-ELY 903
Cdd:cd03256 233 TDEVLdEIY 241
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
684-890 |
3.84e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.93 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEpsFEATRSRSrysVAYAAQKPWLLNATVE 763
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD--LEKALSSL---ISVLNQRPYLFDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENItfgssfnrqrykavtdacslqpdidllpfgdqteigerGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 843
Cdd:cd03247 93 NNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3273501 844 DHLMqEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREG 890
Cdd:cd03247 135 RQLL-SLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1325-1473 |
7.68e-25 |
|
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: 101.96 E-value: 7.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1325 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG-SIRFNL 1403
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1404 DPECKCT-------DDRLWEALEiaQLknmvkSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1473
Cdd:pfam00005 81 RLGLLLKglskrekDARAEEALE--KL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
684-886 |
1.03e-24 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 104.09 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVE 763
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK----VSLVGQEPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFG-SSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 842
Cdd:cd03248 106 DNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE- 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 3273501 843 SDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSV 886
Cdd:cd03248 185 SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
664-886 |
1.15e-24 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 103.65 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 664 EDVAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRS 742
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 rsrySVAYAAQKPWLLNATVEENI-TFGSSFNRQRYKAVtdacslqpdidllpfgdqtEIGERGINLSGGQRQRICVARA 821
Cdd:cd03369 83 ----SLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYGAL-------------------RVSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 822 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDkrTVVLVTHKLQYLTHADWIIAMKDGSV 886
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1308-1533 |
1.54e-24 |
|
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: 104.17 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVIDGIDISKLPLHtLRS 1383
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMlaglLKPDSGSILIDGEDVRKEPRE-ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQDPILFSG-SIRFNL----------DPECKCTDDRLWEALEiaqlknmvksLPGGLDATVteggENFSVGQRQL 1452
Cdd:COG4555 75 QIGVLPDERGLYDRlTVRENIryfaelyglfDEELKKRIEELIELLG----------LEEFLDRRV----GELSTGMKKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1453 FCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLL 1530
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELR 220
|
...
gi 3273501 1531 AQE 1533
Cdd:COG4555 221 EEI 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
668-895 |
2.07e-24 |
|
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: 103.41 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVYWNNVNESEPSFEATRS 742
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 RSRysVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDAC---SLQpDIDLLP-FGDQTEIGErginLSGGQRQRICV 818
Cdd:cd03260 80 RRR--VGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERveeALR-KAALWDeVKDRLHALG----LSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 819 ARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFlqDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
667-895 |
2.10e-24 |
|
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: 104.11 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvneSEPSFEATRSR 743
Cdd:COG1124 1 MLEVRNlsvSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG---RPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 744 SRySVAYAAQKPWL-LNA--TVEENIT-----FGSSFNRQRYKAVTDACSLQPDI-DLLPfgDQteigerginLSGGQRQ 814
Cdd:COG1124 78 RR-RVQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYP--HQ---------LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 815 RICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKR----TVVLVTHKLQYLTH-ADWIIAMKDGSVLRE 889
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEE 220
|
....*.
gi 3273501 890 GTLKDI 895
Cdd:COG1124 221 LTVADL 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
684-895 |
2.55e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 110.60 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLE-GKVYWNNVN--ESEPSFeatrsrSRYSVAYAAQKPWLLNA 760
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLT-KLLQRLYTPQhGQVLVDGVDlaIADPAW------LRRQMGVVLQENVLFSR 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITF---GSSFNRQRYkAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 837
Cdd:TIGR01846 546 SIRDNIALcnpGAPFEHVIH-AAKLAGAHD-FISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 838 LDIHlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:TIGR01846 624 LDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1308-1532 |
5.73e-24 |
|
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: 108.07 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLK---PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTL 1381
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 RSRLSIILQDPilfSGSirfnLDPECKCTDDrLWEALEI------AQLKNMVKSLPG--GLDATVTE--GGEnFSVGQRQ 1451
Cdd:COG1123 341 RRRVQMVFQDP---YSS----LNPRMTVGDI-IAEPLRLhgllsrAERRERVAELLErvGLPPDLADryPHE-LSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1452 LFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1524
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*...
gi 3273501 1525 TPESLLAQ 1532
Cdd:COG1123 488 PTEEVFAN 495
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
680-876 |
5.84e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.77 E-value: 5.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVywnnvnesepsfeaTRSRSRySVAYAAQK---PW 756
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------------RRAGGA-RVAYVPQRsevPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 757 LLNATVEENITFG--------SSFNRQRYKAVTDACSlqpDIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNI 828
Cdd:NF040873 69 SLPLTVRDLVAMGrwarrglwRRLTRDDRAAVDDALE---RVGLADLAGR-QLGE----LSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3273501 829 VFLDDPFSALDIHLSDHLmqEGILKFLQDDKRTVVLVTHKLQYLTHAD 876
Cdd:NF040873 141 LLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDLELVRRAD 186
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1534 |
6.04e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.15 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPI-LFSGS-----IRFNLdpECKCTD-----DRLWEALEIAQLKNMVKSLPggldatvteggENFSVGQRQLFCLA 1456
Cdd:PRK13632 88 IFQNPDnQFIGAtveddIAFGL--ENKKVPpkkmkDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1457 RAFVRKSSILIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQED 1534
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
374-913 |
8.12e-24 |
|
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: 108.89 E-value: 8.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 374 IETGINlrGALLAMIYNKILRL--------STSNLSMGEMTLGQINNLVAIET-NQLMWFLFLCPNLWAMpvqiimgviL 444
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLGLM---------F 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 445 LYNLlgSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK--------LYAWEHIFCKSVE 516
Cdd:TIGR03797 272 YYSW--KLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 517 ---ETRMKE--LSSLKT-FALYTSLSIFMNAAIPIAAV---LATFVTHAYASGNNLKPAEAFASlSLFHIL-VTPLFlls 586
Cdd:TIGR03797 350 lelSAQRIEnlLTVFNAvLPVLTSAALFAAAISLLGGAglsLGSFLAFNTAFGSFSGAVTQLSN-TLISILaVIPLW--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 587 tvvrfavkaiisvqklnefllsdeigedswrtgEGTLPFesckkhtgVQSKP---INRKQPGRYHldnyeqarrlrpaet 663
Cdd:TIGR03797 426 ---------------------------------ERAKPI--------LEALPevdEAKTDPGKLS--------------- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 664 edVAIKVTNGYFSWG-SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRS 742
Cdd:TIGR03797 450 --GAIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 RsrysVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 822
Cdd:TIGR03797 528 Q----LGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 823 YQNTNIVFLDDPFSALdihlsDHLMQEGILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVEL 902
Cdd:TIGR03797 604 VRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLF 678
|
570
....*....|.
gi 3273501 903 YEhwktLMNRQ 913
Cdd:TIGR03797 679 AQ----LARRQ 685
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
684-890 |
1.13e-23 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 101.04 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYsVAYAAQKPWL-LNA-- 760
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKE-IQMVFQDPMSsLNPrm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITFGSSFNRQRYKAVT-------DACSLQPDIDLL---PFGdqteigerginLSGGQRQRICVARALYQNTNIVF 830
Cdd:cd03257 100 TIGEQIAEPLRIHGKLSKKEArkeavllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 831 LDDPFSALDIHLSDHLMQegILKFLQDDK-RTVVLVTHKL---QYLthADWIIAMKDGSVLREG 890
Cdd:cd03257 169 ADEPTSALDVSVQAQILD--LLKKLQEELgLTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
663-902 |
1.94e-23 |
|
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: 100.82 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 663 TEDVAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRS 742
Cdd:COG1127 1 MSEPMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 -RSRYSVAYaaQKPWLLNA-TVEENITFG----SSFN----RQRYKAVTDACSLQPDIDLLPfgdqteiGErginLSGGQ 812
Cdd:COG1127 80 lRRRIGMLF--QGGALFDSlTVFENVAFPlrehTDLSeaeiRELVLEKLELVGLPGAADKMP-------SE----LSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 813 RQRICVARALYQNTNIVFLDDPFSALDIHLS---DHLMQEgilkfLQDD-KRTVVLVTHKLQYL-THADWIIAMKDGSVL 887
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSaviDELIRE-----LRDElGLTSVVVTHDLDSAfAIADRVAVLADGKII 221
|
250
....*....|....*
gi 3273501 888 REGTLKDIQTKDVEL 902
Cdd:COG1127 222 AEGTPEELLASDDPW 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
668-886 |
2.61e-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: 98.24 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNesePSFEATRSRSRys 747
Cdd:cd03230 1 IEVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD---IKKEPEEVKRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLL-NATVEENItfgssfnrqrykavtdacslqpdidllpfgdqteigergiNLSGGQRQRICVARALYQNT 826
Cdd:cd03230 75 IGYLPEEPSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 827 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYL-THADWIIAMKDGSV 886
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
684-905 |
3.15e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.12 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVE 763
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ----VALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGSSF-NRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 842
Cdd:TIGR00958 573 ENIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE- 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 843 SDHLMQEgiLKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTkDVELYEH 905
Cdd:TIGR00958 652 CEQLLQE--SRSRAS--RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME-DQGCYKH 709
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
686-895 |
3.25e-23 |
|
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: 101.18 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYSVAYAAQKPWLL-NATVEE 764
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 765 NITFGSSFN----RQRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD- 839
Cdd:cd03294 122 NVAFGLEVQgvprAEREERAAEALEL---VGLEGWEHK-YPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDp 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 840 -IHLSdhlMQEGILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03294 194 lIRRE---MQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1031-1282 |
4.13e-23 |
|
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: 102.19 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1031 YVAGFSILCGAGIF--LCLVTSLtvewmgLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLE 1108
Cdd:cd18600 76 YVGVADSLLAMGFFrgLPLVHTL------ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1109 SLTRSTLLCLSAIGMISYATPVFLIALAPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHET 1188
Cdd:cd18600 150 DFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQP 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1189 RFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGAC-IVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLAD 1267
Cdd:cd18600 230 YFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIfFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSID 309
|
250
....*....|....*
gi 3273501 1268 LEVQMGAVKKVNSFL 1282
Cdd:cd18600 310 VDSLMRSVSRIFKFI 324
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1308-1531 |
5.69e-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: 99.88 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1385
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPIlfsGSI--RFNLD-----P----ECKCTDDRLWEALEIAQL-KNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVDrilaePlrihGLPDREERIAELLEQVGLpPSFLDRYPHQL-----------SGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1528
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
...
gi 3273501 1529 LLA 1531
Cdd:COG1124 226 LLA 228
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
684-891 |
8.06e-23 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 105.80 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesePSFEATRSRSRYSVAYAAQKPWLLNATVE 763
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGI----PREEIPREVLANSVAMVDQDIFLFEGTVR 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITF--GSSFNRQRYKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-- 839
Cdd:TIGR03796 571 DNLTLwdPTIPDADLVRACKDAA-IHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDpe 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3273501 840 --IHLSDHLMQEGIlkflqddkrTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:TIGR03796 650 teKIIDDNLRRRGC---------TCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
662-904 |
8.84e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.83 E-value: 8.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 662 ETEDVAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEAT 740
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 741 RSRsrysVAYAAQKP--WLLNATVEENITFGSSFNRQRYKA----VTDACSlqpDIDLLPFGDQTEigergINLSGGQRQ 814
Cdd:PRK13648 82 RKH----IGIVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEmhrrVSEALK---QVDMLERADYEP-----NALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 815 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TVVLVTHKLQYLTHADWIIAMKDGSVLREGTLK 893
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLD--LVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
250
....*....|.
gi 3273501 894 DIQTKDVELYE 904
Cdd:PRK13648 228 EIFDHAEELTR 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1308-1533 |
1.04e-22 |
|
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: 98.96 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1385
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLlrALA--GLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPIL-FSGSIR--------------FNLDPEckctDDRL-WEALEIAQLKNMVkslpgglDATVTEggenFSVGQ 1449
Cdd:COG1120 78 AYVPQEPPApFGLTVRelvalgryphlglfGRPSAE----DREAvEEALERTGLEHLA-------DRPVDE----LSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1450 RQLFCLARAFVRKSSILIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYD 1524
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQG 220
|
....*....
gi 3273501 1525 TPESLLAQE 1533
Cdd:COG1120 221 PPEEVLTPE 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
667-905 |
1.39e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.30 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVYWNN--VNESEPsfeatrsR 743
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT-SGEILIGGrdVTDLPP-------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 744 SRySVAYAAQKPWLL-NATVEENITFGSSFNR----QRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICV 818
Cdd:COG3839 74 DR-NIAMVFQSYALYpHMTVYENIAFPLKLRKvpkaEIDRRVREAAEL---LGLEDLLDR-----KPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 819 ARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqt 897
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMRAE-IKRLHRRLGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPE---- 219
|
....*...
gi 3273501 898 kdvELYEH 905
Cdd:COG3839 220 ---ELYDR 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
686-890 |
5.74e-22 |
|
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: 95.82 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPtGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNV--NESEPSFEATRSRSRysVAYAAQKPWLL-NATV 762
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLPPQQRK--IGLVFQQYALFpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFGSSFNRQRYKAVtdacSLQPDIDLLpfgDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 841
Cdd:cd03297 93 RENLAFGLKRKRNREDRI----SVDELLDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3273501 842 LSDHLMQEgILKFLQDDKRTVVLVTHKL---QYLthADWIIAMKDGSVLREG 890
Cdd:cd03297 166 LRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
684-895 |
7.82e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 98.68 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtLE----GKVYWNNvnesEPSFEATRSRSRYsVAYAAQKPWLL- 758
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNG----RDLFTNLPPRERR-VGFVFQHYALFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 NATVEENITFG---SSFNRQRYKA-VTDACSLqpdIDLLPFGD----QteigerginLSGGQRQRICVARALYQNTNIVF 830
Cdd:COG1118 89 HMTVAENIAFGlrvRPPSKAEIRArVEELLEL---VQLEGLADrypsQ---------LSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 831 LDDPFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:COG1118 157 LDEPFGALDAKVRKELRRW-LRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
684-867 |
1.32e-21 |
|
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: 94.47 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPsfeatRSRSRYSVAYAAQKPWLLNA-TV 762
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-----REDYRRRLAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITF-----GSSFNRQRYKAVTDACSLQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 837
Cdd:COG4133 93 RENLRFwaalyGLRADREAIDEALEAVGLAGLADL-PVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 3273501 838 LDI--------HLSDHLMQEGIlkflqddkrtVVLVTH 867
Cdd:COG4133 162 LDAagvallaeLIAAHLARGGA----------VLLTTH 189
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
684-897 |
2.17e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvnESEPSFEAtRSRSRYsVAYAAQKPWLLNA-TV 762
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD--KPISMLSS-RQLARR-LALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFGSS--------FNRQRYKAVTDACslqpdidllpfgDQTEIGE----RGINLSGGQRQRICVARALYQNTNIVF 830
Cdd:PRK11231 94 RELVAYGRSpwlslwgrLSAEDNARVNQAM------------EQTRINHladrRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 831 LDDPFSALDIHLSDHLMqeGILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQT 897
Cdd:PRK11231 162 LDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
660-870 |
5.70e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.46 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 660 PAETEDVAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVYWNNVNESE 734
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLA-VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 735 PSFEATRSRSRYSVAYaaQKPWLLNATVEENITFGSSFNRqrYKavtdacslqpdidllpfGDQTEIGER---------- 804
Cdd:PRK14243 82 PDVDPVEVRRRIGMVF--QKPNPFPKSIYDNIAYGARING--YK-----------------GDMDELVERslrqaalwde 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 805 --------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDhLMQEGILKFLQDDkRTVVLVTHKLQ 870
Cdd:PRK14243 141 vkdklkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD-PIST-LRIEELMHELKEQ-YTIIIVTHNMQ 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
659-870 |
1.13e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.18 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 659 RPAETEDVAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVYWNNVNES 733
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 734 EPSFEATRSRSRysVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDacslqpdidllpfgdqtEIGER--------- 804
Cdd:COG1117 82 DPDVDVVELRRR--VGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELD-----------------EIVEEslrkaalwd 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 805 ---------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH---LMQEgiLKflqdDKRTVVLVTHKLQ 870
Cdd:COG1117 143 evkdrlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKieeLILE--LK----KDYTIVIVTHNMQ 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1308-1524 |
1.17e-20 |
|
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: 92.20 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1383
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLErpdsGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCL 1455
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKLRGVPKAEiraRVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1456 ARAFVRKSSILIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1524
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1309-1521 |
1.37e-20 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 90.96 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1309 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1388
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1389 LQdpILfsgsirfnldpeckctddrlwEALEIAQLKN-MVKSLPGGldatvteggenfsvgQRQLFCLARAFVRKSSILI 1467
Cdd:cd03214 79 PQ--AL---------------------ELLGLAHLADrPFNELSGG---------------ERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1468 MDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILTADLVIVMKRGNIL 1521
Cdd:cd03214 121 LDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
674-867 |
1.39e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.00 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 674 YFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSfeATRsrsrysvAYAAQ 753
Cdd:COG4525 13 YPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--ADR-------GVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 754 K----PWLlnaTVEENITFGSSFN----RQRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGGQRQRICVARALYQN 825
Cdd:COG4525 84 KdallPWL---NVLDNVAFGLRLRgvpkAERRARAEELLAL---VGLADFARRR-IWQ----LSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 3273501 826 TNIVFLDDPFSALDIhLSDHLMQEGILKFLQDDKRTVVLVTH 867
Cdd:COG4525 153 PRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
660-891 |
2.61e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.82 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 660 PAETEDVAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFE 738
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 739 ATRSrsrySVAYAAQKPWLLNATVEENITFGS-SFNRQRYKAVTDACSLQpdiDLLPfGDQ---TEIGERGINLSGGQRQ 814
Cdd:PRK11160 411 ALRQ----AISVVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLE---KLLE-DDKglnAWLGEGGRQLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 815 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILEL-LAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
667-895 |
3.35e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 96.13 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVYWNNVNESEPSfEATRS 742
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELS-EALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 RSrysVAYAAQKPW--LLNATVEENITFGSsfnrqRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVA 819
Cdd:COG1123 83 RR---IGMVFQDPMtqLNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 820 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTVVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 895
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILD--LLRELQRERgTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1245-1532 |
4.14e-20 |
|
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: 95.91 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1245 GLGLLYaltITNYLNwVVRNLAD----LE----VQMGAVKKVnsFLTM---------ESEnyegtmdPSQVPEHWPQEGE 1307
Cdd:COG4172 207 GMALLL---ITHDLG-VVRRFADrvavMRqgeiVEQGPTAEL--FAAPqhpytrkllAAE-------PRGDPRPVPPDAP 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 --IKIHDLCVRYENN---LKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDGIDISKL 1376
Cdd:COG4172 274 plLEARDLKVWFPIKrglFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1377 P---LHTLRSRLSIILQDPilFsGSirfnLDPeckctddRL------WEALEI-------AQLKNMVKSLPG--GLDATV 1438
Cdd:COG4172 353 SrraLRPLRRRMQVVFQDP--F-GS----LSP-------RMtvgqiiAEGLRVhgpglsaAERRARVAEALEevGLDPAA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1439 -----TEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFA---------------DRTVV- 1497
Cdd:COG4172 419 rhrypHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehglaylfishDLAVVr 490
|
330 340 350
....*....|....*....|....*....|....*
gi 3273501 1498 TIAHRvhtiltadlVIVMKRGNILEYDTPESLLAQ 1532
Cdd:COG4172 491 ALAHR---------VMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
667-873 |
4.24e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.64 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQT---LEGKVYWNNVNESEPSFEATR 741
Cdd:PRK14258 7 AIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELESevrVEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 742 SRSRYSVAYAaqKPWLLNATVEENITFGSSFNRQRYKAVTDAC--SLQPDIDLLpfgDQTE--IGERGINLSGGQRQRIC 817
Cdd:PRK14258 86 LRRQVSMVHP--KPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIveSALKDADLW---DEIKhkIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 818 VARALYQNTNIVFLDDPFSALDIHLS---DHLMQEGILKflqdDKRTVVLVTHKLQYLT 873
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVS 215
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
699-909 |
4.91e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 92.94 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 699 IVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEpsfeatRSRSRYSVAYAAQKPWLL-NATVEENITFGSSF----N 773
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN------VPPHLRHINMVFQSYALFpHMTVEENVAFGLKMrkvpR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 774 RQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLK 853
Cdd:TIGR01187 75 AEIKPRVLEALRL---VQLEEFADR-----KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE--LK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 854 FLQDD-KRTVVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEHWKTL 909
Cdd:TIGR01187 145 TIQEQlGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPE-------EIYEEPANL 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
663-895 |
5.46e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.59 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 663 TEDVAIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATR 741
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 742 SRsrysVAYAAQKP--WLLNATVEENITFG---SSFNRQRYKAVTDACSLQPDI-DLLPFGDQteigergiNLSGGQRQR 815
Cdd:PRK13632 83 KK----IGIIFQNPdnQFIGATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMeDYLDKEPQ--------NLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 816 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKD 894
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKK--IMVDLRKTrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
.
gi 3273501 895 I 895
Cdd:PRK13632 229 I 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
684-891 |
6.02e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 93.24 E-value: 6.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVYWN--NVNESEPSfeatrsrsRYSVAYAAQK----PW 756
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLDgrDVTGLPPE--------KRNVGMVFQDyalfPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 757 LlnaTVEENITFGSSFNR----QRYKAVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFL 831
Cdd:COG3842 92 L---TVAENVAFGLRMRGvpkaEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 832 DDPFSALDIHLSDHLMQEgiLKFLQDD-KRTVVLVTHKlQY--LTHADWIIAMKDGSVLREGT 891
Cdd:COG3842 160 DEPLSALDAKLREEMREE--LRRLQRElGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
668-886 |
9.84e-20 |
|
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: 89.24 E-value: 9.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWN--NVNESEPsfeatrsrSR 745
Cdd:cd03301 1 VELENVTKRFGNVTA-LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrDVTDLPP--------KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 746 YSVAYAAQKPWLL-NATVEENITFGSSFNRQRY----KAVTDACSLQpDIDLLpfgdqteIGERGINLSGGQRQRICVAR 820
Cdd:cd03301 72 RDIAMVFQNYALYpHMTVYDNIAFGLKLRKVPKdeidERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 821 ALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTH-KLQYLTHADWIIAMKDGSV 886
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAE-LKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
686-923 |
9.97e-20 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 95.34 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEpsfeATRSRSRYSVAYAAQKPWLLNATVEEN 765
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINT----VTRESLRKSIATVFQDAGLFNRSIREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 766 ITFG-SSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSD 844
Cdd:TIGR01192 429 IRLGrEGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVE-TE 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 845 HLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEA 923
Cdd:TIGR01192 508 ARVKNAIDALRKN--RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPATKPLRK 584
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
664-868 |
1.05e-19 |
|
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: 89.64 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 664 EDVAIKVTNgyfsWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVYWNNVnesepsfEAT 740
Cdd:cd03234 7 WDVGLKAKN----WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ-------PRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 741 RSRSRYSVAYAAQKPWLL-NATVEENITFGSSF-----NRQRYKAVTDACSLQPDIDLLPFGdqteiGERGINLSGGQRQ 814
Cdd:cd03234 76 PDQFQKCVAYVRQDDILLpGLTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3273501 815 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHK 868
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
687-905 |
2.10e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 91.71 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 687 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNV--NESEPSFEATRSRSRysVAYAAQKPWLL-NATVE 763
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlFDSRKGIFLPPEKRR--IGYVFQEARLFpHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGSSFNRQRYKAVTDACSlqpdIDLLPFGdqtEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 842
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFERV----IELLGIG---HLLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 843 SDHLMQegILKFLQDDKRT-VVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQ-TKDVELYEH 905
Cdd:TIGR02142 167 KYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWaSPDLPWLAR 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1308-1532 |
3.00e-19 |
|
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: 88.41 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLK--PVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---L 1378
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsGSVLVDGTDLTLLSgkeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1379 HTLRSRLSIILQDPILFS-----GSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQR 1450
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1451 QLFCLARAFVRKSSILIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTP 1526
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 3273501 1527 ESLLAQ 1532
Cdd:cd03258 226 EEVFAN 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
684-881 |
3.15e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 88.23 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVE 763
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ----VSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGSSFNRQRykavtdacsLQPDI---DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALD 839
Cdd:PRK10247 99 DNLIFPWQIRNQQ---------PDPAIfldDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 3273501 840 IHlSDHLMQEGILKFLQDDKRTVVLVTHKLQYLTHADWIIAM 881
Cdd:PRK10247 170 ES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1308-1520 |
3.25e-19 |
|
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: 87.93 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYEN--NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTL 1381
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGGLDrptsGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 ----RSRLSIILQD---------------PILFSGSIRfnldPECKctdDRLWEALEIAQLKNMVKSLPGGLdatvtegg 1442
Cdd:cd03255 77 aafrRRHIGFVFQSfnllpdltalenvelPLLLAGVPK----KERR---ERAEELLERVGLGDRLNHYPSEL-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1443 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1518
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
..
gi 3273501 1519 NI 1520
Cdd:cd03255 217 KI 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
678-900 |
4.18e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.89 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 678 GSGLATLS-NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvnesepsfeatRSRSRYSVAYAAQKPW 756
Cdd:PRK10253 16 GYGKYTVAeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG-----------EHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 757 LL--NATVEENITFGSSFNRQRYKAvtdacslQP--------DIDLLPFGDQ----TEIGERGIN-LSGGQRQRICVARA 821
Cdd:PRK10253 85 LLaqNATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 822 LYQNTNIVFLDDPFSALDIhlsDHlmQEGILKFLQDDKR----TVVLVTHKL----QYLTHadwIIAMKDGSVLREGTLK 893
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnqacRYASH---LIALREGKIVAQGAPK 229
|
....*..
gi 3273501 894 DIQTKDV 900
Cdd:PRK10253 230 EIVTAEL 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
667-891 |
6.63e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.47 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSrsry 746
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 SVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 826
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 827 NIVFLDDPFSALDIHlsdhlMQEGILKFLQ--DDKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:PRK10790 496 QILILDEATANIDSG-----TEQAIQQALAavREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
686-899 |
8.74e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.12 E-value: 8.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNesepsfeatrsrsrYSVAYAAQKP---------- 755
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD--------------LTALPPAERPvsmlfqennl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 756 -WLLnaTVEENITFG-------SSFNRQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQNTN 827
Cdd:COG3840 83 fPHL--TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 828 IVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKD 899
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLD--LVDELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
684-886 |
1.03e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.43 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesePSFEAtRSRSRYSVAYAAQKPWllnATVE 763
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA----PLAEA-REDTRLMFQDARLLPW---KKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGSSFN-RQRYKAVTDACSLQPdidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhL 842
Cdd:PRK11247 100 DNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-L 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 3273501 843 SDHLMQEGILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSV 886
Cdd:PRK11247 168 TRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
683-918 |
1.62e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 683 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ---TLEGKVYWNNVNESEPSFEATRSRSRYSVAYaaQKPWL 757
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHNIYSPRTDTVDLRKEIGMVF--QQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 LNATVEENITFGSSFNRQRYKAVTDAcSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 835
Cdd:PRK14239 98 FPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 836 SALDiHLSDHLMQEGILKFlqDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIqtkdvelyehwktLMNRQD 914
Cdd:PRK14239 177 SALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM-------------FMNPKH 240
|
....
gi 3273501 915 QELE 918
Cdd:PRK14239 241 KETE 244
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1308-1518 |
1.67e-18 |
|
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: 84.55 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHT--L 1381
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAGLEepdsGSILIDGEDLTDLEDELppL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 RSRLSIILQDPILFSGsirfnldpeckctddrlweaLEIAQlkNMVKSLPGGldatvteggenfsvgQRQLFCLARAFVR 1461
Cdd:cd03229 75 RRRIGMVFQDFALFPH--------------------LTVLE--NIALGLSGG---------------QQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1462 KSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILT-ADLVIVMKRG 1518
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1308-1522 |
1.71e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLHTLR 1382
Cdd:PRK14247 4 IEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1383 SRLSIILQ--DPI----LFSG---SIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLpggLDATVTEggenFSVGQRQL 1452
Cdd:PRK14247 82 RRVQMVFQipNPIpnlsIFENvalGLKLNrLVKSKKELQERVRWALEKAQLWDEVKDR---LDAPAGK----LSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1453 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtiltADLVIVMKRGNILE 1522
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
680-870 |
1.87e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEatrsrsRYSV-AYAAQKPWLl 758
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE------RGVVfQNEGLLPWR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 naTVEENITFGssfnrQRYKAVTDACSLQPDIDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSA 837
Cdd:PRK11248 86 --NVQDNVAFG-----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|...
gi 3273501 838 LDIHLSDHlMQEGILKFLQDDKRTVVLVTHKLQ 870
Cdd:PRK11248 159 LDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1323-1531 |
2.24e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.96 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1323 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI---DISKLPlhTLRSRLSIILQDP-ILFSG- 1397
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQ--GIRKLVGIVFQNPeTQFVGr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1398 SIRFNL--DPECKCTddrlwEALEIAQLKNMVKSlPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1475
Cdd:PRK13644 94 TVEEDLafGPENLCL-----PPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1476 DMAT-ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1531
Cdd:PRK13644 168 DPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
675-890 |
2.71e-18 |
|
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: 84.52 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 675 FSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVYWNNVNESEPSFeatrsrsRYSVAYAA 752
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSF-------RKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 753 QKPWLL-NATVEENITFgssfnrqrykavtdACSLQpdidllpfgdqteigergiNLSGGQRQRICVARALYQNTNIVFL 831
Cdd:cd03213 89 QDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 832 DDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTHA--DWIIAMKDGSVLREG 890
Cdd:cd03213 136 DEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1323-1518 |
3.20e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 85.08 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1323 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR----LSIILQDPILFSGS 1398
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1399 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM- 1477
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIh 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3273501 1478 ATENILQKVVMTAFAD--RTVVTIAHRVHTILTADLVIVMKRG 1518
Cdd:cd03290 175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
684-891 |
3.46e-18 |
|
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: 90.26 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVYWNNVNESEPSFEATRSrsrySVAYAAQKPWLLNAT 761
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRILIDGQDIRDVTQASLRA----AIGIVPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFGS-SFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 840
Cdd:COG5265 448 IAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 841 HlSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:COG5265 528 R-TERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
684-887 |
3.54e-18 |
|
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: 86.12 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRsrysVAYAAQKPWLLNATVE 763
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR----LSIILQDPILFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLS 843
Cdd:cd03288 113 FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM-AT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 3273501 844 DHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVL 887
Cdd:cd03288 192 ENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
668-909 |
3.94e-18 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 85.37 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESE-PSFEatrsRSRY 746
Cdd:cd03300 1 IELENVSKFYGGFVA-LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHK----RPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 SV--AYAaqkpwLL-NATVEENITFGSSFNR----QRYKAVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICV 818
Cdd:cd03300 76 TVfqNYA-----LFpHLTVFENIAFGLRLKKlpkaEIKERVAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 819 ARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTVVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIq 896
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLE--LKRLQKElGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI- 218
|
250
....*....|...
gi 3273501 897 tkdvelYEHWKTL 909
Cdd:cd03300 219 ------YEEPANR 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
684-895 |
4.19e-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: 85.08 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEatrsrsRYSVAYAAQKPWLL-NATV 762
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------KRDISYVPQNYALFpHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFGssFNRQRYKAVTDACSLQpdidllpfgdqtEIGER-GIN---------LSGGQRQRICVARALYQNTNIVFLD 832
Cdd:cd03299 89 YKNIAYG--LKKRKVDKKEIERKVL------------EIAEMlGIDhllnrkpetLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 833 DPFSALDIHLSDHLMQEgiLKFLQDDKRTVVL-VTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03299 155 EPFSALDVRTKEKLREE--LKKIRKEFGVTVLhVTHDFeEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
688-890 |
4.21e-18 |
|
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: 84.47 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 688 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVN--ESEPSfeatrsrsRYSVAYAAQKPWLL-NATVEE 764
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvtAAPPA--------DRPVSMLFQENNLFaHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 765 NITFGSSFN-------RQRYKAVTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVFLDDPFSA 837
Cdd:cd03298 90 NVGLGLSPGlkltaedRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3273501 838 LDIHLSDHlMQEGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREG 890
Cdd:cd03298 159 LDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
667-895 |
9.07e-18 |
|
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: 84.31 E-value: 9.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSfeaTRSRSry 746
Cdd:cd03296 2 SIEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 sVAYAAQKPWLL-NATVEENITFGSSFNRQRYKAVTDACSLQPDiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQ 824
Cdd:cd03296 76 -VGFVFQHYALFrHMTVFDNVAFGLRVKPRSERPPEAEIRAKVH-ELLKLVQLDWLADRYPAqLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 825 NTNIVFLDDPFSALDIHLSDHLmqEGILKFLQDDKR-TVVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKEL--RRWLRRLHDELHvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
684-895 |
9.64e-18 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 84.17 E-value: 9.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVYWNNVNESEPSFEATRSRSRySVAYAAQKPWLLNA-T 761
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT-SGSVLVDGTDLTLLSGKELRKARR-RIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITF-----GSSfNRQRYKAVTDacslqpdidLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPF 835
Cdd:cd03258 99 VFENVALpleiaGVP-KAEIEERVLE---------LLELVGLEDKADAYPaQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 836 SALDIHLSDhlmqeGILKFLQDDKR----TVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03258 169 SALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
680-867 |
1.18e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFeatrsrsRYSVAYA----AQKP 755
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-------AEACHYLghrnAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 756 WLlnaTVEENITFGSSFNRQRYKAVTDACS---LQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 832
Cdd:PRK13539 87 AL---TVAENLEFWAAFLGGEELDIAAALEavgLAPLAHL-PFG----------YLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3273501 833 DPFSALDIH--------LSDHLMQEGIlkflqddkrtVVLVTH 867
Cdd:PRK13539 153 EPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1308-1520 |
1.51e-17 |
|
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: 81.68 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVIDGIDISKLPlHTLRS 1383
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIilglLKPDSGEIKVLGKDIKKEP-EEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQDPILFSG-SIRFNLDpeckctddrlwealeiaqlknmvkslpggldatvteggenFSVGQRQLFCLARAFVRK 1462
Cdd:cd03230 74 RIGYLPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1463 SSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1520
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1303-1502 |
1.63e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.94 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1303 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVI-DGIDISKLP 1377
Cdd:COG4178 358 SEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAIaglwPYGSGRIARpAGARVLFLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1378 lhtlrsrlsiilQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNmvksLPGGLDaTVTEGGENFSVGQRQLFC 1454
Cdd:COG4178 433 ------------QRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH----LAERLD-EEADWDQVLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3273501 1455 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1502
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
686-897 |
1.69e-17 |
|
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: 85.92 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN---VNESEPSFEATRSRSrysVAYAAQK----PWLl 758
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIFLPPHRRR---IGYVFQEarlfPHL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 naTVEENITFGssfnRQRYKAVTDACSLQPDIDLLpfgdqtEIG---ERGI-NLSGGQRQRICVARALYQNTNIVFLDDP 834
Cdd:COG4148 93 --SVRGNLLYG----RKRAPRAERRISFDEVVELL------GIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 835 FSALDIHLSDHLMQegILKFLQDDKRT-VVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 897
Cdd:COG4148 161 LAALDLARKAEILP--YLERLRDELDIpILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1308-1522 |
1.85e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 83.17 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffrMVDIFD-GKIVIDGIDISKLP---LH 1379
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILG---GLDRPTsGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1380 TLRSR-LSIILQDpilfsgsirFNLDPE-----------------CKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteg 1441
Cdd:COG1136 82 RLRRRhIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQL------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1442 genfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFAD---RTVVTIAHRVHTILTADLVIVMKR 1517
Cdd:COG1136 146 ----SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTIVMVTHDPELAARADRVIRLRD 219
|
....*
gi 3273501 1518 GNILE 1522
Cdd:COG1136 220 GRIVS 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
684-895 |
2.13e-17 |
|
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: 82.87 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVN-ESEPSFEatrsRSRYSVAYAAQKPWLL-NAT 761
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHE----RARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFGSSFNRQRykavtdacSLQPDID----LLPfgdqtEIGER----GINLSGGQRQRICVARALYQNTNIVFLDD 833
Cdd:cd03224 92 VEENLLLGAYARRRA--------KRKARLErvyeLFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 834 PFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03224 159 PSEGLAPKIVEEIFE--AIRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
684-891 |
2.95e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVN-ESEPSFEATRSRsrysvAYAAQK-----PWl 757
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPlADWSPAELARRR-----AVLPQHsslsfPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 lnaTVEENITFG---SSFNRQRYKAVTDACSLQpdIDLLPFGD---QTeigerginLSGGQRQRICVARALYQNTN---- 827
Cdd:PRK13548 92 ---TVEEVVAMGrapHGLSRAEDDALVAAALAQ--VDLAHLAGrdyPQ--------LSGGEQQRVQLARVLAQLWEpdgp 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 828 --IVFLDDPFSALDIHLSDHLMQegILK-FLQDDKRTVVLVTHKL----QYlthADWIIAMKDGSVLREGT 891
Cdd:PRK13548 159 prWLLLDEPTSALDLAHQHHVLR--LARqLAHERGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1308-1533 |
3.51e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 82.83 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFR----MVDIFDGKIVIDGidiskLPLHTLRS 1383
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTL----LKailgLLPPTSGTVRLFG-----KPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQD-------PIL--------FSGSIRF--NLDPECKctdDRLWEALE---IAQLKN-MVKSLpggldatvtegg 1442
Cdd:COG1121 76 RIGYVPQRaevdwdfPITvrdvvlmgRYGRRGLfrRPSRADR---EAVDEALErvgLEDLADrPIGEL------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1443 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGnI 1520
Cdd:COG1121 141 ---SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRG-L 216
|
250
....*....|...
gi 3273501 1521 LEYDTPESLLAQE 1533
Cdd:COG1121 217 VAHGPPEEVLTPE 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
668-886 |
3.67e-17 |
|
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: 80.55 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNnvnesepsfeatrsrsrys 747
Cdd:cd03216 1 LELRGITKRFGGVKA-LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 vayaaqkpwllnatvEENITFGSSFNRQRykavtdacslqpdidllpfgdqteigeRGIN----LSGGQRQRICVARALY 823
Cdd:cd03216 61 ---------------GKEVSFASPRDARR---------------------------AGIAmvyqLSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 824 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQ-YLTHADWIIAMKDGSV 886
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1308-1534 |
4.87e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.11 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYEN-----NLKpvlkhvkayIKPGQKVGICGRTGSGKSSLS--LAFFRMVDifDGKIVIDGIDISKLPLHT 1380
Cdd:COG3840 2 LRLDDLTYRYGDfplrfDLT---------IAAGERVAILGPSGAGKSTLLnlIAGFLPPD--SGRILWNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 lrsR-LSIILQDPILFSG-SIRFN----LDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQ 1451
Cdd:COG3840 71 ---RpVSMLFQENNLFPHlTVAQNiglgLRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQL-----------SGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1452 LFCLARAFVRKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1528
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*.
gi 3273501 1529 LLAQED 1534
Cdd:COG3840 217 LLDGEP 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
668-899 |
4.88e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVN-ESEPSFEATRSrsry 746
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvEALSARAASRR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 sVAYAAQKPWL-LNATVEENITFGSSFNRQRYKAVTDACSLQPDiDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQ 824
Cdd:PRK09536 79 -VASVPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 825 NTNIVFLDDPFSALDIHlsdHLMQE-GILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKD 899
Cdd:PRK09536 157 ATPVLLLDEPTASLDIN---HQVRTlELVRRLVDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1308-1534 |
4.93e-17 |
|
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: 82.23 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1384
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIILQDpilfsgsirFNLDPECKCTDDRLWEALeiAQlKNMVKSLPG-----------------GLDATVTEGGENFSV 1447
Cdd:cd03256 80 IGMIFQQ---------FNLIERLSVLENVLSGRL--GR-RSTWRSLFGlfpkeekqralaalervGLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1448 GQRQLFCLARAFVRKSSILIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNI 1520
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
250
....*....|....
gi 3273501 1521 LeYDTPESLLAQED 1534
Cdd:cd03256 224 V-FDGPPAELTDEV 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
668-886 |
5.34e-17 |
|
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: 81.30 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYfswGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATrSRSRYS 747
Cdd:cd03292 4 INVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAI-PYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLL-NATVEENITF-------GSSFNRQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVA 819
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 820 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTH-KLQYLTHADWIIAMKDGSV 886
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMN--LLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
675-891 |
6.69e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 675 FSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVYWNNVNESEpsfeATRSRSRYSVAYAAQ 753
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDpQSGRILIDGTDIRT----VTRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 754 KPWLLNATVEENITFG--SSFNRQRYKAVTDACSLqpD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 830
Cdd:PRK13657 417 DAGLFNRSIEDNIRVGrpDATDEEMRAAAERAQAH--DfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 831 LDDPFSALDIHLSDHLmQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT 891
Cdd:PRK13657 495 LDEATSALDVETEAKV-KAALDELMKG--RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
676-888 |
7.31e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.32 E-value: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 676 SWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYSVAY 750
Cdd:PRK10535 13 SYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMniLGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 751 aaQKPWLL-NATVEENITF-----GSSFNRQRYKAvtdacslqpdIDLLP-FGDQTEIGERGINLSGGQRQRICVARALY 823
Cdd:PRK10535 93 --QRYHLLsHLTAAQNVEVpavyaGLERKQRLLRA----------QELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 824 QNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSVLR 888
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
684-915 |
7.54e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEM---QTLEGKV-YWNNVNESEPSFEATRSRSRYSVAYAAQKPWLLN 759
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIeLLGRTVQREGRLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 A-TVEENITFG------------SSFNRQRYKAVTDACSlqpDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNT 826
Cdd:PRK09984 100 RlSVLENVLIGalgstpfwrtcfSWFTREQKQRALQALT---RVGMVHFAHQ-----RVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 827 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTVVLVTHKLQY-LTHADWIIAMKDGSVLREGTlkdIQTKDVELYEH 905
Cdd:PRK09984 172 KVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS---SQQFDNERFDH 247
|
250
....*....|
gi 3273501 906 WKTLMNRQDQ 915
Cdd:PRK09984 248 LYRSINRVEE 257
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
684-867 |
8.18e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.99 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVYWNNVNESEPSFEATRsrsrysVAYAAQKPWLL-N 759
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAEQRR------IGILFQDDLLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 ATVEENITFG--SSFNR-QRYKAVTDAcsLQpDIDLLPFGDQTeIGErginLSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:COG4136 91 LSVGENLAFAlpPTIGRaQRRARVEQA--LE-EAGLAGFADRD-PAT----LSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|.
gi 3273501 837 ALDIHLSDHlMQEGILKFLQDDKRTVVLVTH 867
Cdd:COG4136 163 KLDAALRAQ-FREFVFEQIRQRGIPALLVTH 192
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1308-1534 |
8.32e-17 |
|
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: 81.39 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFR-MVDIF---DGKIVIDGIDISKL---PLHT 1380
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTL----LRlIVGLLrpdSGEVLIDGEDISGLseaELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 LRSRLSIILQDPILFSG-----SIRFNLDPECKCTDdrlWEALEIAQLK-NMVkSLPGGLDATVTEggenFSVGQRQLFC 1454
Cdd:cd03261 75 LRRRMGMLFQSGALFDSltvfeNVAFPLREHTRLSE---EEIREIVLEKlEAV-GLRGAEDLYPAE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1455 LARAFVRKSSILIMDEATASID-MATENI------LQKVVmtafaDRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTP 1526
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIddlirsLKKEL-----GLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTP 221
|
....*...
gi 3273501 1527 ESLLAQED 1534
Cdd:cd03261 222 EELRASDD 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1308-1517 |
1.17e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.59 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENN--LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGidiskLPLHTL 1381
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLErptsGEVLVDG-----EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 RSRLSIILQDPILFS-GSIRFN--LDPECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:cd03293 72 GPDRGYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAreraeELLELVGLSGFENAYPHQL-----------SGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKR 1517
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
662-889 |
1.33e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 81.78 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 662 ETEDVAIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEAT 740
Cdd:TIGR02769 4 EVRDVTHTYRTGGLFGAKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 741 RSRSR-----YSVAYAAQKP-----WLLNATVEENITFGSSFNRQRYKAVTDACSLQPDI-DLLPfgdqteigergINLS 809
Cdd:TIGR02769 84 RAFRRdvqlvFQDSPSAVNPrmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLP-----------RQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 810 GGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TVVLVTHKLQYLTH-ADWIIAMKDG 884
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKG 227
|
....*
gi 3273501 885 SVLRE 889
Cdd:TIGR02769 228 QIVEE 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1325-1542 |
1.34e-16 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 81.54 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1325 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILFS---- 1396
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLPhrtv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1397 -GSIRFNLDPECKCTDDRL---WEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1472
Cdd:cd03294 120 lENVAFGLEVQGVPRAEREeraAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1473 ASIDMATENILQKVVMTAFAD--RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQ--EDGVfASFVR 1542
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNpaNDYV-REFFR 262
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
668-890 |
1.56e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.48 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNesepsfeaTRSRSRYS 747
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD--------LSRLKRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQK-------PWLL-NATVEENITF-------GSSFNRQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQ 812
Cdd:COG2884 74 IPYLRRRigvvfqdFRLLpDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 813 RQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTHADW-IIAMKDGSVLREG 890
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIME--LLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1304-1532 |
1.89e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1304 QEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 1383
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQDPI-LFSGS-----IRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFC 1454
Cdd:PRK13635 82 QVGMVFQNPDnQFVGAtvqddVAFGLENIGVPREEmveRVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1455 LARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1308-1531 |
2.01e-16 |
|
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: 79.79 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1387
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 IL--QDPILFSG-SIRFNLD-PECKCTDDRLWEALEIA-----QLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARA 1458
Cdd:cd03224 78 GYvpEGRRIFPElTVEENLLlGAYARRRAKRKARLERVyelfpRLKERRKQLAGTL-----------SGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1459 FVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1531
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALeIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
684-895 |
2.32e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYSVAYAAQKP--WLLNAT 761
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFG-SSFNRQRYKAVTDACSLqpdidLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALD 839
Cdd:PRK13646 103 VEREIIFGpKNFKMNLDEVKNYAHRL-----LMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 840 IHLSDHLMQegILKFLQ-DDKRTVVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK13646 178 PQSKRQVMR--LLKSLQtDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
668-904 |
2.37e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.25 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSW--GSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSR 743
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 744 SRYSVAYAAQKPWLLNATVEENITFGSSfNR--------QRYKAVTDACSLQPDI--DLLPFgdqteigergiNLSGGQR 813
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFGPI-NLglseeeieNRVKRAMNIVGLDYEDykDKSPF-----------ELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 814 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGT 891
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK--IKELHKEyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
250
....*....|...
gi 3273501 892 LKDIqTKDVELYE 904
Cdd:PRK13637 229 PREV-FKEVETLE 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
667-890 |
2.38e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.08 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVywnnVNESEPSFEATRSRSry 746
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI----SILGQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 sVAYAAQKP---WLLNATVEENITFG-----------SSFNRQRykaVTDACSlqpDIDLLPFgDQTEIGErginLSGGQ 812
Cdd:PRK15056 80 -VAYVPQSEevdWSFPVLVEDVVMMGryghmgwlrraKKRDRQI---VTAALA---RVDMVEF-RHRQIGE----LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 813 RQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKdGSVLREG 890
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK-GTVLASG 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
668-884 |
2.38e-16 |
|
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: 79.50 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRys 747
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLL-NATVEENITFG--SSFNRQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQ 824
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLApiKVKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 825 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDG 884
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLD--VMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
665-904 |
2.76e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.00 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 665 DVAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSS---LLLAILGEMQTLEGKVYWNNVNESEPSFEAT 740
Cdd:PRK13640 3 DNIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 741 RSRsrysVAYAAQKP--WLLNATVEENITFGSSfNRQ--RYKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRI 816
Cdd:PRK13640 83 REK----VGIVFQNPdnQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 817 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILK--LIRKLKKKNNlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
....*....
gi 3273501 896 QTKDVELYE 904
Cdd:PRK13640 231 FSKVEMLKE 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1335-1520 |
4.51e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 78.69 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1335 GQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhTLRSRLSIILQDPILFS-----GSIRFNLDP 1405
Cdd:cd03298 24 GEITAIVGPSGSGKSTL----LNLIAGFEtpqsGRVLINGVDVTAAP--PADRPVSMLFQENNLFAhltveQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1406 ECKCT-DDRlwEALEIAQ----LKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1480
Cdd:cd03298 98 GLKLTaEDR--QAIEVALarvgLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3273501 1481 NILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNI 1520
Cdd:cd03298 165 AEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1308-1521 |
4.68e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 78.95 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTl 1381
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGLlepdAGFATVDGFDVVKEPAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 RSRLSIilqdpilFSGSIRFNldpeckctdDRL--WEALEI---------AQLKNMVKSLPGGLD--ATVTEGGENFSVG 1448
Cdd:cd03266 77 RRRLGF-------VSDSTGLY---------DRLtaRENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1449 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1521
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
668-902 |
4.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSfEATRSRSRYS 747
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS-KLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQKPWLLNATVEENITFGSSfnrqrykavtDACslQPDIDLLPFGDQTeIGERGI---------NLSGGQRQRICV 818
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFGPE----------NLC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 819 ARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGT----LKD 894
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEpenvLSD 225
|
....*...
gi 3273501 895 IQTKDVEL 902
Cdd:PRK13644 226 VSLQTLGL 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1309-1520 |
4.81e-16 |
|
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: 78.73 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1309 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRL--- 1385
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIgyv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 ---SIILQD-PILFSGSIRFNLDPEC------KCTD-DRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFC 1454
Cdd:cd03235 74 pqrRSIDRDfPISVRDVVLMGLYGHKglfrrlSKADkAKVDEALERVGLSELADRQIGEL-----------SGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1455 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILT-ADLVIVMKRGNI 1520
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1308-1544 |
5.22e-16 |
|
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: 79.27 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPILFSG-SIRFNLD--------PECKcTDDRLWEALEIAQL--KNMVKSLPGGLdatvteggenfSVGQRQLFCLA 1456
Cdd:cd03295 80 VIQQIGLFPHmTVEENIAlvpkllkwPKEK-IRERADELLALVGLdpAEFADRYPHEL-----------SGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1457 RAFVRKSSILIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESL 1529
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 3273501 1530 LAQEDGVF-ASFVRAD 1544
Cdd:cd03295 224 LRSPANDFvAEFVGAD 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
684-895 |
5.66e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEAtrsRSRYSV--AYAaqkpwLL-NA 760
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN---RHVNTVfqSYA-----LFpHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITFGSSF----NRQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:PRK09452 102 TVFENVAFGLRMqktpAAEITPRVMEALRM---VQLEEFAQR-----KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 837 ALDIHLSDHLMQEgiLKFLQddkR----TVVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK09452 174 ALDYKLRKQMQNE--LKALQ---RklgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
680-897 |
7.34e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 78.63 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNES-EPSFEatrsRSRYSVAYAAQKPWLL 758
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITgLPPHE----IARLGIGRTFQIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 -NATVEENI----------TFGSSFNRQRYKAVTDACSlqpdiDLLpfgDQTEIGERG----INLSGGQRQRICVARALY 823
Cdd:cd03219 88 pELTVLENVmvaaqartgsGLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 824 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQT 897
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVVMsLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
688-886 |
8.47e-16 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 77.98 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 688 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESepsfeaTRSRSRYSVAYAAQKPWLL-NATVEENI 766
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT------GLAPYQRPVSMLFQENNLFaHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 767 TFG-------SSFNRQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALD 839
Cdd:TIGR01277 92 GLGlhpglklNAEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3273501 840 IHLSDHlMQEGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSV 886
Cdd:TIGR01277 161 PLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
680-905 |
8.68e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 8.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESE-PSFEatRSRSRYSVAYAAqkpwLL 758
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQ--RPINMMFQSYAL----FP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 NATVEENITFGSSFNRQRYKAVTDACSlqpdiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 837
Cdd:PRK11607 105 HMTVEQNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 838 LDIHLSDHlMQEGILKFLQDDKRTVVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEH 905
Cdd:PRK11607 180 LDKKLRDR-MQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE-------EIYEH 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1308-1476 |
9.20e-16 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 77.52 E-value: 9.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPLHtLRS 1383
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQDPILFSG-SIRFNLD-----PECKCTDDRLWEALEIAQLknmvkslPGGLDATVteggENFSVGQRQLFCLAR 1457
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAVGL-------AGLADLPV----RQLSAGQKRRVALAR 144
|
170
....*....|....*....
gi 3273501 1458 AFVRKSSILIMDEATASID 1476
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALD 163
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
684-895 |
1.01e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSfeatrSRSRySVAYAAQKPWLL-NATV 762
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-----ARDR-KVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFGSSF--NRQR-YKAVTDACSLQpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 838
Cdd:PRK10851 92 FDNIAFGLTVlpRRERpNAAAIKAKVTQ----LLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 839 DIHLSDHLmQEGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK10851 168 DAQVRKEL-RRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
684-891 |
1.19e-15 |
|
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: 77.55 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNnvnesEPSFEATRSRSRYSVAYAAQK---PWLLna 760
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-----GYSIRTDRKAARQSLGYCPQFdalFDEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITFGS---SFNRQRYKAVTDA----CSLQPDIDllpfgdqTEIGergiNLSGGQRQRICVARALYQNTNIVFLDD 833
Cdd:cd03263 91 TVREHLRFYArlkGLPKSEIKEEVELllrvLGLTDKAN-------KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 834 PFSALdihlsDHLMQEGILKFLQDDK--RTVVLVTHKLQ---YLthADWIIAMKDGSVLREGT 891
Cdd:cd03263 160 PTSGL-----DPASRRAIWDLILEVRkgRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1308-1506 |
1.60e-15 |
|
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: 77.06 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1384
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIILQDPILFSG-----SIRFNLdpECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFC 1454
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyeNVAFAL--EVTGVPPREIrkrvpAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 1455 LARAFVRKSSILIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRVHTI 1506
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHRVIAL 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
672-903 |
1.79e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 672 NGYFSWGSGLATlSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN--VNESEPsfeATRSRSRYSVA 749
Cdd:PRK11000 8 NVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrMNDVPP---AERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 750 YAAQkPWLlnaTVEENITFG-------SSFNRQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARAL 822
Cdd:PRK11000 84 YALY-PHL---SVAENMSFGlklagakKEEINQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 823 YQNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTVVLVTH-KLQYLTHADWIIAMKDGSVLREGtlkdiqtKDVE 901
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG-------KPLE 220
|
..
gi 3273501 902 LY 903
Cdd:PRK11000 221 LY 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
665-890 |
2.55e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 665 DVAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYwnnVNESEPSfEATRSRS 744
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVK---VMGREVN-AENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 745 RYSVAYAAQKP--WLLNATVEENITFG--------SSFNRqRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQ 814
Cdd:PRK13647 78 RSKVGLVFQDPddQVFSSTVWDDVAFGpvnmgldkDEVER-RVEEALKAVRMWDFRDKPPY-----------HLSYGQKK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 815 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQY-LTHADWIIAMKDGSVLREG 890
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1308-1522 |
2.70e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 76.63 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1384
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIILQD-PILFSGSIRFNL----------DPECKctdDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgksRKEIR---RRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTILTADL-VIVMKRGNILE 1522
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1322-1521 |
2.87e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 76.05 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1322 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRSRLSIILQDPILFSgsi 1399
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1400 rfnldpeckctDDRLWEALEI-AQLknmvKSLPGgldatvteggenfsvGQRQLFCLARAFVRKSSILIMDEATASIDMA 1478
Cdd:cd03213 96 -----------TLTVRETLMFaAKL----RGLSG---------------GERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3273501 1479 TENILQKVVMtAFAD--RTVVTIAHRVHTILTA--DLVIVMKRGNIL 1521
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
743-909 |
3.63e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.61 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 RSRYSVAyaAQKPWLLNATVEENITFG-SSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 821
Cdd:PTZ00265 1295 RNLFSIV--SQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 822 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTVVLVTHKLQYLTHADWIIAM----KDGS-VLREGTLKDIQ 896
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGTHEELL 1451
|
170
....*....|...
gi 3273501 897 TKDVELYEHWKTL 909
Cdd:PTZ00265 1452 SVQDGVYKKYVKL 1464
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1340-1541 |
3.64e-15 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 78.30 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1340 ICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtLRSrLSIILQDPILF-----SGSIRFNL--DPECKCT 1410
Cdd:TIGR01187 1 LLGPSGCGKTTLlrLLAGFEQPD--SGSIMLDGEDVTNVPPH-LRH-INMVFQSYALFphmtvEENVAFGLkmRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1411 -DDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID------MATE--N 1481
Cdd:TIGR01187 77 iKPRVLEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1482 ILQKVVMtafadrTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQEDGVF-ASFV 1541
Cdd:TIGR01187 146 IQEQLGI------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
684-895 |
7.48e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.08 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN--VNESEPSFEATRSRSRYSVAYAAQKPWLLNAT 761
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivVSSTSKQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFG-SSFNRQRYKAVTDACSlqpdiDLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALD 839
Cdd:PRK13643 102 VLKDVAFGpQNFGIPKEKAEKIAAE-----KLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 840 IHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK13643 177 PKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1308-1541 |
8.12e-15 |
|
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: 75.45 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlkpVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPlhTLRSRL 1385
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLleTIAGFIKPD--SGKILLNGKDITNLP--PEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPILFSG-SIRFNLDPECKctdDRLWEALEI-AQLKNMVKSLpgGLDATVTEGGENFSVGQRQLFCLARAFVRKS 1463
Cdd:cd03299 74 SYVPQNYALFPHmTVYKNIAYGLK---KRKVDKKEIeRKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1464 SILIMDEATASIDMATENILQKVVMTAF--ADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLL--AQEDGVfA 1538
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFkkPKNEFV-A 227
|
...
gi 3273501 1539 SFV 1541
Cdd:cd03299 228 EFL 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
686-895 |
8.43e-15 |
|
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: 79.34 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVYWNNVNESEPSFEATRS-RSRYSVA----YAAQKPWLlna 760
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPlRRRMQVVfqdpFGSLSPRM--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITFGSSFNR------QRYKAVTDAcsLQpDIDLLPfgdqtEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDD 833
Cdd:COG4172 380 TVGQIIAEGLRVHGpglsaaERRARVAEA--LE-EVGLDP-----AARHRYPHeFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 834 PFSALDIHLsdhlmQEGILKFLQDDKRtvvlvTHKLQYL--TH--------ADWIIAMKDGSVLREGTLKDI 895
Cdd:COG4172 452 PTSALDVSV-----QAQILDLLRDLQR-----EHGLAYLfiSHdlavvralAHRVMVMKDGKVVEQGPTEQV 513
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1536 |
9.27e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPI-LFSGSI-----RFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARA 1458
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDEmhrRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1459 FVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEDGV 1536
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1534 |
9.46e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.43 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRL 1385
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALE---IAQLKNmvkslpggldatvtEGGENFSVGQRQLF 1453
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKrtgIEHLKD--------------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1454 CLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLL 1530
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
....
gi 3273501 1531 AQED 1534
Cdd:PRK13636 231 AEKE 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1308-1534 |
1.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.92 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTLR 1382
Cdd:PRK13650 5 IEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDGLleaeSGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1383 SRLSIILQDPI-LFSGS-----IRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:PRK13650 81 HKIGMVFQNPDnQFVGAtveddVAFGLENkgiPHEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1454 CLARAFVRKSSILIMDEATASID--------MATENILQKVVMTafadrtVVTIAHRVHTILTADLVIVMKRGNILEYDT 1525
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQMT------VISITHDLDEVALSDRVLVMKNGQVESTST 223
|
....*....
gi 3273501 1526 PESLLAQED 1534
Cdd:PRK13650 224 PRELFSRGN 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
668-896 |
1.69e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.28 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAT----LSNIDIRIPTGQLTMIVGQVGCGKSS-------LLLAILGEM-----------QTLEGKV 725
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIewifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 726 YWNNVNESEPSFEATRS----RSRYSVAYAAQKPWLLNATVEENITFGS-SFNRQRYKAVTDACSLQPDIDLlpfgDQTE 800
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKikeiRRRVGVVFQFAEYQLFEQTIEKDIIFGPvSMGVSKEEAKKRAAKYIELVGL----DESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 801 IGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQY-LTHADWII 879
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTI 236
|
250 260
....*....|....*....|.
gi 3273501 880 AMKDGSVLREG----TLKDIQ 896
Cdd:PRK13651 237 FFKDGKIIKDGdtydILSDNK 257
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1308-1532 |
1.88e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENN----LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP-LHTLR 1382
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1383 SRLSIILQDP------ILFSGSIRF---NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:PRK13633 85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILTADLVIVMKRGNILEYDTPE 1527
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 3273501 1528 SLLAQ 1532
Cdd:PRK13633 230 EIFKE 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
684-905 |
2.14e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.44 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYSVAYAAQKP--WLLNAT 761
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFPehQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFG-SSFN------RQRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDD 833
Cdd:PRK13634 103 VEKDICFGpMNFGvseedaKQKAREMIELVGLPEELlARSPF-----------ELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 834 PFSALDIHLSDHLMqEGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVELYEH 905
Cdd:PRK13634 172 PTAGLDPKGRKEMM-EMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1308-1532 |
2.15e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 75.86 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVlkhvKA------YIKPGQKVGICGRTGSGKSSLSLAFFRMVD---IFDGKIVIDGIDISKLPL 1378
Cdd:COG0444 2 LEVRNLKVYFPTRRGVV----KAvdgvsfDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1379 HTLRS----RLSIILQDPIlfsGSirfnLDPeCKCTDDRLWEALEI------AQLKNMVKSLpggLDAT-VTEGGE---- 1443
Cdd:COG0444 78 KELRKirgrEIQMIFQDPM---TS----LNP-VMTVGDQIAEPLRIhgglskAEARERAIEL---LERVgLPDPERrldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1444 ---NFSVGQRQLFCLARAFVRKSSILIMDEATASIDmATeniLQKVVMTAFADR------TVVTIAHRVHTIL-TADLVI 1513
Cdd:COG0444 147 yphELSGGMRQRVMIARALALEPKLLIADEPTTALD-VT---IQAQILNLLKDLqrelglAILFITHDLGVVAeIADRVA 222
|
250
....*....|....*....
gi 3273501 1514 VMKRGNILEYDTPESLLAQ 1532
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1308-1534 |
2.23e-14 |
|
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: 74.12 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaFFRMVDIF---DGKIVIDGIDISKLPLHTlRSR 1384
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTT---FYMIVGLVkpdSGKILLDGQDITKLPMHK-RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIIL--QDPILFSG-SIRFNL--------DPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:cd03218 75 LGIGYlpQEASIFRKlTVEENIlavleirgLSK-KEREEKLEELLEEFHITHLRKSKASSL-----------SGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1454 CLARAFVRKSSILIMDEATASID-MATENIlQKVVMTaFADRTV-VTIA-HRVHTIL-TADLVIVMKRGNILEYDTPESL 1529
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDpIAVQDI-QKIIKI-LKDRGIgVLITdHNVRETLsITDRAYIIYEGKVLAEGTPEEI 220
|
....*
gi 3273501 1530 LAQED 1534
Cdd:cd03218 221 AANEL 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
667-908 |
2.34e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVYWNNVNESEPSFEATR 741
Cdd:PRK14267 4 AIETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 742 SRSRYSVAYAAQKPWLlNATVEENITFGSSFNR---------QRYKAVTDACSLQPDIdllpfgdQTEIGERGINLSGGQ 812
Cdd:PRK14267 83 VRREVGMVFQYPNPFP-HLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 813 RQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTVVLVTHK-LQYLTHADWIIAMKDGSVLREG- 890
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANID-PVGTAKIEELLFELKKE--YTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGp 231
|
250
....*....|....*...
gi 3273501 891 TLKDIQTKDVELYEHWKT 908
Cdd:PRK14267 232 TRKVFENPEHELTEKYVT 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1308-1534 |
2.71e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.08 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNL---KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLR 1382
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1383 SRLSIILQDP------------ILFsGSIRFNL-DPECKctdDRLWEALEIAqlknmvkslpgGLDATVTEGGENF--SV 1447
Cdd:PRK13637 83 KKVGLVFQYPeyqlfeetiekdIAF-GPINLGLsEEEIE---NRVKRAMNIV-----------GLDYEDYKDKSPFelSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1448 GQRQLFCLARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1524
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
250
....*....|
gi 3273501 1525 TPESLLAQED 1534
Cdd:PRK13637 228 TPREVFKEVE 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
668-895 |
2.83e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.73 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYwnnVNESEPSFEATR-SRSRY 746
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL---IKGEPIKYDKKSlLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 747 SVAYAAQKP--WLLNATVEENITFGS---SFNRQRY-KAVTDACSlqpdidllpfgdqtEIGERGI------NLSGGQRQ 814
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGPlnlGLSKEEVeKRVKEALK--------------AVGMEGFenkpphHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 815 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYL-THADWIIAMKDGSVLREGTLK 893
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPK 222
|
..
gi 3273501 894 DI 895
Cdd:PRK13639 223 EV 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
684-908 |
3.52e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.18 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVYWNNvnESEPSFEATRSRSRYSVAYAAQKPwLL 758
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVYLDG--QDIFKMDVIELRRRVQMVFQIPNP-IP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 NATVEENITFGSSFNR---------QRYKAVTDACSLQPDIdllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIV 829
Cdd:PRK14247 96 NLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 830 FLDDPFSALDIHLSDHLmqEGILKFLQDDKrTVVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIQTKDV-ELYEHWK 907
Cdd:PRK14247 169 LADEPTANLDPENTAKI--ESLFLELKKDM-TIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRhELTEKYV 245
|
.
gi 3273501 908 T 908
Cdd:PRK14247 246 T 246
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1303-1518 |
4.27e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.97 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1303 PQEGEIKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGidiskL 1376
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDG-----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1377 PLHTLRSRLSIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdatvteggenf 1445
Cdd:COG1116 74 PVTGPGPDRGVVFQEPALLpwltvLDNVALGLElrgvpkAERR---ERARELLELVGLAGFEDAYPHQL----------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1446 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKRG 1518
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDeAVFLADRVVVLSAR 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1325-1530 |
4.45e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.23 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1325 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSIILQDpilfsgsir 1400
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1401 FNLDPECKCTDDRLWeALEIAQLKNMVKSlPGGLDATVTEGGENF--------SVGQRQLFCLARAFVRKSSILIMDEAT 1472
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1473 ASID--MATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLL 1530
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
684-895 |
5.27e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYSVAYAAQKPWLL-NATV 762
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFGSSFN----RQRYKAVTDACSlQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLDDPFSAL 838
Cdd:PRK10070 124 LDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 839 DIHLSDHlMQEGILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK10070 196 DPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1308-1533 |
5.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.07 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMV-------DIFDGKIVIDGIDISKLPLHT 1380
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLInglllpdDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 LRSRLSIILQDPI-LFSGS-----IRFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDATVTEGgENFSVGQRQLFC 1454
Cdd:PRK13640 82 IREKVGIVFQNPDnQFVGAtvgddVAFGLE-------NRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1455 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 3273501 1533 E 1533
Cdd:PRK13640 234 V 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
664-895 |
5.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.11 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 664 EDVAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN--VNESEPSFEATR 741
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 742 SrsrySVAYAAQKP--WLLNATVEENITFGssfnrqrykavtdACSLQpdidlLPfgdQTEIGER--------GIN---- 807
Cdd:PRK13636 82 E----SVGMVFQDPdnQLFSASVYQDVSFG-------------AVNLK-----LP---EDEVRKRvdnalkrtGIEhlkd 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 808 -----LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTVVLVTHKLQYLT-HADWIIAM 881
Cdd:PRK13636 137 kpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM-KLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVM 215
|
250
....*....|....
gi 3273501 882 KDGSVLREGTLKDI 895
Cdd:PRK13636 216 KEGRVILQGNPKEV 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
680-867 |
5.54e-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: 72.53 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRsrsrySVAYAAQKPWLLN 759
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-----GLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 A-TVEENITFGSSFNRQryKAVTDACSlqpDIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 837
Cdd:cd03231 87 TlSVLENLRFWHADHSD--EQVEEALA---RVGLNGFED------RPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 3273501 838 LDI--------HLSDHLMQEGIlkflqddkrtVVLVTH 867
Cdd:cd03231 156 LDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1308-1520 |
6.78e-14 |
|
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: 72.56 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRL 1385
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDpilfsgsirFNLDPECK----CTDDRLW-------EALEIA-------QLKNMVKSLPGGLdatvteggenfSV 1447
Cdd:cd03262 79 GMVFQQ---------FNLFPHLTvlenITLAPIKvkgmskaEAEERAlellekvGLADKADAYPAQL-----------SG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1448 GQRQLFCLARAFVRKSSILIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRGNI 1520
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
680-867 |
9.46e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNnvneSEPSFEATRSRSRySVAYAAQKPWLLN 759
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN----GTPLAEQRDEPHE-NILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 A-TVEENITFGSSFNRQRYKAVTDACslqpdidllpfgdqTEIGERGIN------LSGGQRQRICVARALYQNTNIVFLD 832
Cdd:TIGR01189 87 ElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 3273501 833 DPFSALDI--------HLSDHLMQEGIlkflqddkrtVVLVTH 867
Cdd:TIGR01189 153 EPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
684-885 |
9.70e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.00 E-value: 9.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtlegkvYWnnvnesePSFEATRSR-SRYSVAYAAQKPWLLNATV 762
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG---------LW-------PYGSGRIARpAGARVLFLPQRPYLPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITF---GSSFNRQRYKAVTDACSLQPDIDLLpfgDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALD 839
Cdd:COG4178 443 REALLYpatAEAFSDAELREALEAVGLGHLAERL---DEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3273501 840 IHLSDHLMQEgILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGS 885
Cdd:COG4178 518 EENEAALYQL-LREELPG--TTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1323-1532 |
1.20e-13 |
|
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: 73.35 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1323 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1402
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1403 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN- 1481
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1482 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
684-879 |
1.38e-13 |
|
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: 70.26 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtlegkvYWnnvnesePSFEATRSRSRYS-VAYAAQKPWLLNATV 762
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG---------LW-------PWGSGRIGMPEGEdLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFgssfnrqrykavtdacslqpdidllPFGDqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 842
Cdd:cd03223 81 REQLIY-------------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 3273501 843 SDHLMQegilkFLQDDKRTVVLVTHKLQYLTHADWII 879
Cdd:cd03223 127 EDRLYQ-----LLKELGITVISVGHRPSLWKFHDRVL 158
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
680-893 |
1.42e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.48 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesepSFEATRSRS---------RYSVAY 750
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDI-----TIDTARSLSqqkglirqlRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 751 AAQKPWLL-NATVEENITFGSSFNRQ--RYKAVTDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQNTN 827
Cdd:PRK11264 90 VFQNFNLFpHRTVLENIIEGPVIVKGepKEEATARARELLAKVGLA--GKETSYPRR---LSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 828 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLK 893
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLN--TIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1306-1541 |
1.72e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 73.57 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1306 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLaffRMV----DIFDGKIVIDGIDISKLPlhTL 1381
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTL-L---RMIagleDPTSGEILIGGRDVTDLP--PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 RSRLSIILQDPILF-SGSIRFNL----------DPEckcTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQR 1450
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIafplklrkvpKAE---IDRRVREAAELLGLEDLLDRKPKQL-----------SGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1451 QLFCLARAFVRKSSILIMDEATASID------MATE--NILQKVVMTafadrTV-VTiaHRVHTILT-ADLVIVMKRGNI 1520
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TIyVT--HDQVEAMTlADRIAVMNDGRI 212
|
250 260
....*....|....*....|..
gi 3273501 1521 LEYDTPESLLAQEDGVF-ASFV 1541
Cdd:COG3839 213 QQVGTPEELYDRPANLFvAGFI 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1320-1530 |
1.75e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.39 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1320 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI------DISKLPLHTLRSRLSIILQDPI 1393
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1394 LFSG-SIRFNLDPECKC---TDDRLWEALEIAQLKN--MVKSLPGGLDATVTEggenFSVGQRQLFCLARAFVRKSSILI 1467
Cdd:PRK14246 101 PFPHlSIYDNIAYPLKShgiKEKREIKKIVEECLRKvgLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 1468 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLL 1530
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1308-1521 |
2.31e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 70.68 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQkVGICGRTGSGKSSL--SLA-FFRMVDifdGKIVIDGIDISKLPlHTLRSR 1384
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTLmrILAtLTPPSS---GTIRIDGQDVLKQP-QKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIILQDpilFSGSIRFnldpeckctddRLWEALE-IAQLKNMVKSlpgGLDATVTEGGEN-------------FSVGQR 1450
Cdd:cd03264 74 IGYLPQE---FGVYPNF-----------TVREFLDyIAWLKGIPSK---EVKARVDEVLELvnlgdrakkkigsLSGGMR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1451 QLFCLARAFVRKSSILIMDEATASID----MATENILQKVVmtafADRTVVTIAHRVHTI-LTADLVIVMKRGNIL 1521
Cdd:cd03264 137 RRVGIAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG----EDRIVILSTHIVEDVeSLCNQVAVLNKGKLV 208
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
684-895 |
2.39e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 71.18 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQtlEGKVYWNNVNESEPSFEATRSRSRysVAYAAQK----Pwl 757
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTITVDGEDLTDSKKDINKLRRK--VGMVFQQfnlfP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 lNATVEENITFG--SSFNRQRYKAVTDAcslqpdIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVFL 831
Cdd:COG1126 91 -HLTVLENVTLApiKVKKMSKAEAEERA------MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 832 DDPFSALDIHLSdhlmQE--GILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 895
Cdd:COG1126 161 DEPTSALDPELV----GEvlDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1308-1518 |
2.76e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 69.38 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSRLS 1386
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1387 IILQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldatvteggenFSVGQRQLFCLARAFVRKSSIL 1466
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1467 IMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRG 1518
Cdd:cd03216 105 ILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFeIADRVTVLRDG 158
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
688-869 |
3.43e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 688 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNEsepsfeATRSRSRYSVAYAAQKPWLLN-ATVEENI 766
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDH------TTTPPSRRPVSMLFQENNLFShLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 767 TFG-------SSFNRQRYKAVTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD 839
Cdd:PRK10771 93 GLGlnpglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190
....*....|....*....|....*....|....
gi 3273501 840 ihlsDHLMQEgILKFLQD--DKR--TVVLVTHKL 869
Cdd:PRK10771 162 ----PALRQE-MLTLVSQvcQERqlTLLMVSHSL 190
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
684-890 |
4.17e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN-----VNESEPSFEATRS------RSRYSVAYAA 752
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDGQLKVADKnqlrllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 753 QKPWlLNATVEENI------TFGSSFNRQRYKAVTdacslqpdidllpFGDQTEIGERG-----INLSGGQRQRICVARA 821
Cdd:PRK10619 101 FNLW-SHMTVLENVmeapiqVLGLSKQEARERAVK-------------YLAKVGIDERAqgkypVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 822 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREG 890
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1308-1529 |
4.37e-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: 72.44 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtlRSRL 1385
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLlrMIAGFETPD--SGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFC 1454
Cdd:COG3842 80 GMVFQDYALFphltvAENVAFGLRmrgvpkAEIR---ARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1455 LARAFVRKSSILIMDEATASID------MATE--NILQKVVMTAFadrtVVTiaHRVHTILT-ADLVIVMKRGNILEYDT 1525
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDaklreeMREElrRLQRELGITFI----YVT--HDQEEALAlADRIAVMNDGRIEQVGT 219
|
....
gi 3273501 1526 PESL 1529
Cdd:COG3842 220 PEEI 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
685-867 |
5.15e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 685 SNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWN--NVNESEPSFeatrsrsRYSVAY----AAQKPWLl 758
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgePIRRQRDEY-------HQDLLYlghqPGIKTEL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 naTVEENITFgssfnrqrykavtdACSLQPDIDllpfGDQT-----EIGERGI------NLSGGQRQRICVARALYQNTN 827
Cdd:PRK13538 90 --TALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3273501 828 IVFLDDPFSALDI--------HLSDHLMQEGIlkflqddkrtVVLVTH 867
Cdd:PRK13538 150 LWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1245-1522 |
5.52e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1245 GLGLLYaltITNYLNwVVRNLADLEVQMGAVKKV--NSFLTMESE----------NYEGTMDPSQVPEhwPQEGEIKIHD 1312
Cdd:PRK15134 207 NMGLLF---ITHNLS-IVRKLADRVAVMQNGRCVeqNRAATLFSApthpytqkllNSEPSGDPVPLPE--PASPLLDVEQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1313 LCVRYE---------NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGidiskLPLHTL-- 1381
Cdd:PRK15134 281 LQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDG-----QPLHNLnr 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 ------RSRLSIILQDPilfSGSIRFNLDPEckctdDRLWEALEI-------AQLKNMVKSLPG--GLD-ATVTEGGENF 1445
Cdd:PRK15134 355 rqllpvRHRIQVVFQDP---NSSLNPRLNVL-----QIIEEGLRVhqptlsaAQREQQVIAVMEevGLDpETRHRYPAEF 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1446 SVGQRQLFCLARAFVRKSSILIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVHTILT-ADLVIVMKR 1517
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQ 501
|
....*
gi 3273501 1518 GNILE 1522
Cdd:PRK15134 502 GEVVE 506
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
670-895 |
6.11e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 71.92 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 670 VTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLllailGEMQTL-----EGKVYWNNVNESEPSFEATRSRs 744
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTL-----ARLLTMietptGGELYYQGQDLLKADPEAQKLL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 745 RYSVAYAAQKPW-LLN------ATVEE----NITFGSSFNRQRYKAVTDACSLQPD-IDLLP--FgdqteigerginlSG 810
Cdd:PRK11308 91 RQKIQIVFQNPYgSLNprkkvgQILEEplliNTSLSAAERREKALAMMAKVGLRPEhYDRYPhmF-------------SG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 811 GQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKF---LQDDKRTV-VLVTHKLQYLTH-ADWIIAMKDGS 885
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLmmdLQQELGLSyVFISHDLSVVEHiADEVMVMYLGR 232
|
250
....*....|
gi 3273501 886 VLREGTLKDI 895
Cdd:PRK11308 233 CVEKGTKEQI 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
668-884 |
6.24e-13 |
|
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: 67.47 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNnvnesepsfeatrsrSRYS 747
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------STVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 748 VAYAAQkpwllnatveenitfgssfnrqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTN 827
Cdd:cd03221 65 IGYFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 828 IVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDG 884
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEE-----ALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1323-1533 |
8.31e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.79 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1323 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1402
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1403 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-N 1481
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1482 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1533
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
671-897 |
1.02e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.10 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 671 TNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSR----- 745
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRdiqmv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 746 YSVAYAAQKP-----WLLNATVEENITFGSSFNRQRYKAVTDACSLQPDI-DLLPfgdqteigergINLSGGQRQRICVA 819
Cdd:PRK10419 95 FQDSISAVNPrktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRP-----------PQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 820 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTV-VLVTHKL---QYLTHAdwIIAMKDGSVLREGTLKDI 895
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIR--LLKKLQQQFGTAcLFITHDLrlvERFCQR--VMVMDNGQIVETQPVGDK 239
|
..
gi 3273501 896 QT 897
Cdd:PRK10419 240 LT 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
684-921 |
1.05e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.42 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKvYWNNVNESEPSfEATRSRSRYSVAYAAQKPWLL 758
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIqltngLIISETGQTIVGD-YAIPANLKKIK-EVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 NATVEENITFGS---SFNRQR-YKAVTDACSLQPdidlLPfgdqTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDD 833
Cdd:PRK13645 105 QETIEKDIAFGPvnlGENKQEaYKKVPELLKLVQ----LP----EDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 834 PFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGT----------LKDIQTKDVEL 902
Cdd:PRK13645 177 PTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSpfeifsnqelLTKIEIDPPKL 255
|
250
....*....|....*....
gi 3273501 903 YEHWKTLMNRQDQELEKDM 921
Cdd:PRK13645 256 YQLMYKLKNKGIDLLNKNI 274
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
668-890 |
1.29e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 68.76 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGqLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesepsfEATRSRS--R 745
Cdd:cd03264 1 LQLENLTKRYGKKRA-LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ-------DVLKQPQklR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 746 YSVAYAAQKP-WLLNATVEENITF-----GSSfNRQRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVA 819
Cdd:cd03264 72 RRIGYLPQEFgVYPNFTVREFLDYiawlkGIP-SKEVKARVDEVLEL---VNLGDRAKK-KIGS----LSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 820 RALYQNTNIVFLDDPFSALD----IHLSDHLMQEGilkflqdDKRTVVLVTHKLQ-YLTHADWIIAMKDGSVLREG 890
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
684-904 |
1.69e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.77 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYSVAYAAQKP--WLLNAT 761
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPesQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFG-SSFNRQRYKAVTDACSlqpdiDLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALD 839
Cdd:PRK13649 103 VLKDVAFGpQNFGVSQEEAEALARE-----KLALVGISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 840 IHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIqTKDVELYE 904
Cdd:PRK13649 178 PKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDI-FQDVDFLE 240
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1543 |
1.84e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.38 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARA 1458
Cdd:PRK13647 84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1459 FVRKSSILIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPeSLLAQ 1532
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
250
....*....|.
gi 3273501 1533 EDGVFASFVRA 1543
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
680-900 |
2.02e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.05 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVYWNnvnesEPSFEATRSRS-RYSVAYAAQK-PW 756
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPpSEGEILLD-----AQPLESWSSKAfARKVAYLPQQlPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 757 LLNATVEENITFG--------SSFNRQRYKAVTDACSLqpdIDLLPFGdqteigERGIN-LSGGQRQRICVARALYQNTN 827
Cdd:PRK10575 97 AEGMTVRELVAIGrypwhgalGRFGAADREKVEEAISL---VGLKPLA------HRLVDsLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 828 IVFLDDPFSALDI-HLSDHLMQegILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKDV 900
Cdd:PRK10575 168 CLLLDEPTSALDIaHQVDVLAL--VHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1308-1502 |
2.55e-12 |
|
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: 66.41 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIdgidisklplhTLRS 1383
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGM-----------PEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQDPILFSGSIRfnldpeckctddrlwEALeiaqlknmvkSLPGGldatvteggENFSVGQRQLFCLARAFVRKS 1463
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR---------------EQL----------IYPWD---------DVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 3273501 1464 SILIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1502
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1308-1533 |
2.64e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlkpvLK-HVKAYIKPGQKVGICGRTGSGKSSL-SL-AFFRMVDifDGKIVIDGIDisklplHTL--- 1381
Cdd:PRK10771 2 LKLTDITWLYHH-----LPmRFDLTVERGERVAILGPSGAGKSTLlNLiAGFLTPA--SGSLTLNGQD------HTTtpp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 -RSRLSIILQDPILFSG-SIRFN----LDPECKCTDDRLWEALEIAQ---LKNMVKSLPGGLdatvteggenfSVGQRQL 1452
Cdd:PRK10771 69 sRRPVSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1453 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRV---HTILTADLVIVmkRGNILeYDTP- 1526
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLedaARIAPRSLVVA--DGRIA-WDGPt 214
|
....*..
gi 3273501 1527 ESLLAQE 1533
Cdd:PRK10771 215 DELLSGK 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
684-895 |
2.75e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAIL--------GEMqTLEGKVYwnnvnesepSFEATRSRSRYSVAYAAQKP 755
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLM-KILsgvyqpdsGEI-LLDGEPV---------RFRSPRDAQAAGIAIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 756 WLL-NATVEENITFGSSFNR----------QRYKAVTDacSLQPDIDLlpfgdQTEIGErginLSGGQRQRICVARALYQ 824
Cdd:COG1129 89 NLVpNLSVAENIFLGREPRRgglidwramrRRARELLA--RLGLDIDP-----DTPVGD----LSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 825 NTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
684-871 |
2.99e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.20 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIlGEMQTLEG--------KVYWNNVNESEPSFEAtrsrsrysvAYAAQKP 755
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSgdlivdglKVNDPKVDERLIRQEA---------GMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 756 WLL-NATVEENITFGSSFNRQRYKAVTDACSLqpdiDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVF 830
Cdd:PRK09493 87 YLFpHLTALENVMFGPLRVRGASKEEAEKQAR----ELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 3273501 831 LDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQY 871
Cdd:PRK09493 160 FDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGF 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1308-1520 |
4.82e-12 |
|
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: 66.89 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPlhtLRS 1383
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIagleEPTSGRIYIGGRDVTDLP---PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 R-LSIILQDPILFS-----GSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:cd03301 72 RdIAMVFQNYALYPhmtvyDNIAFGLKlrkvPK-DEIDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1454 CLARAFVRKSSILIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNI 1520
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
686-895 |
5.16e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 69.36 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWN--NVNESepsfeATRSRSRYSV--AYAAqkpwLLNAT 761
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgeDVTHR-----SIQQRDICMVfqSYAL----FPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFG-------SSFNRQRykaVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDD 833
Cdd:PRK11432 95 LGENVGYGlkmlgvpKEERKQR---VKEALEL---VDLAGFED------RYVDqISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 834 PFSALDIHLSDHlMQEGILKFLQDDKRTVVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK11432 163 PLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
668-920 |
9.03e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.19 E-value: 9.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFsW--GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN---VNESEPSFEATRS 742
Cdd:PRK15079 20 IKDGKQWF-WqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 743 rsrySVAYAAQKPWL-LNA--TVEENI-----TFGSSFNRQ----RYKAVTDACSLQPDIdllpfgdqteigergIN--- 807
Cdd:PRK15079 99 ----DIQMIFQDPLAsLNPrmTIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNL---------------INryp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 808 --LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TVVLVTHKLQYLTH-ADWIIA 880
Cdd:PRK15079 160 heFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 3273501 881 MKDGSVLREGTlkdiqtkDVELYEH-----WKTLMNR---QDQELEKD 920
Cdd:PRK15079 235 MYLGHAVELGT-------YDEVYHNplhpyTKALMSAvpiPDPDLERN 275
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
676-905 |
1.03e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.33 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 676 SWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN--VNESEPsfeATRSrsrysVA---- 749
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEP---ADRD-----IAmvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 750 -YAaqkpwlL--NATVEENITFGSSfNR--------QRYKAVTDACSLQPDIDLLPfgdqteigeRgiNLSGGQRQRICV 818
Cdd:PRK11650 84 nYA------LypHMSVRENMAYGLK-IRgmpkaeieERVAEAARILELEPLLDRKP---------R--ELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 819 ARALYQNTNiVFL-DDPFSALDIHLSDHLMQEgiLKFLQddKR---TVVLVTH-KLQYLTHADWIIAMKDGSVLREGTlk 893
Cdd:PRK11650 146 GRAIVREPA-VFLfDEPLSNLDAKLRVQMRLE--IQRLH--RRlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT-- 218
|
250
....*....|..
gi 3273501 894 diqtkDVELYEH 905
Cdd:PRK11650 219 -----PVEVYEK 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1308-1506 |
1.04e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.98 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHT 1380
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 LRSRLSIILQDPILFSGSIRFNLDPECKCT--------DDRLWEALEIAQLKNMVKSlpggldaTVTEGGENFSVGQRQL 1452
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleiDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1453 FCLARAFVRKSSILIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1506
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1308-1522 |
1.09e-11 |
|
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: 65.63 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLHtLRSRL 1385
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAktIMGHPKYEVTEGEILFKGEDITDLPPE-ERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIIL--QDPILFSGsirfnldpeckctddrlwealeiAQLKNMVKSLpggldatvtegGENFSVGQRQLFCLARAFVRKS 1463
Cdd:cd03217 78 GIFLafQYPPEIPG-----------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1464 SILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAH--RVHTILTADLVIVMKRGNILE 1522
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1308-1534 |
1.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.14 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDP--ILFS---------GSIRFNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLA 1456
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEET--VAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1457 RAFVRKSSILIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLA 1531
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 3273501 1532 QED 1534
Cdd:PRK13652 228 QPD 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
684-902 |
1.22e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.03 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEpsfEATRSRSRYSVAYAAQKP--WLLNAT 761
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD---EENLWDIRNKAGMVFQNPdnQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFGSsfnrqrykavtDACSLQPDidllpfgdqtEIGERGIN-----------------LSGGQRQRICVARALYQ 824
Cdd:PRK13633 103 VEEDVAFGP-----------ENLGIPPE----------EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 825 NTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVEL 902
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI-FKEVEM 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
681-912 |
1.71e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 681 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-----YWNNVNESEPSFEATRSRS-------RYSV 748
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNHELITNPYSKKiknfkelRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 749 AYAAQKP--WLLNATVEENITFG-------SSFNRQRYKAVTDACSLQPD-IDLLPFGdqteigerginLSGGQRQRICV 818
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 819 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQT 897
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQ--LILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEIFT 265
|
250
....*....|....*
gi 3273501 898 kDVELYEHWKTLMNR 912
Cdd:PRK13631 266 -DQHIINSTSIQVPR 279
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
662-886 |
1.86e-11 |
|
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: 66.42 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 662 ETEDVAIKVTNGyfswgsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL------GEMQtLEGkVYWNNVnesep 735
Cdd:cd03289 4 TVKDLTAKYTEG------GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQ-IDG-VSWNSV----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 736 sfeaTRSRSRYSVAYAAQKPWLLNATVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQR 815
Cdd:cd03289 71 ----PLQKWRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 816 ICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTVVLVTHKLQYLTHADWIIAMKDGSV 886
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1308-1536 |
2.52e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1386
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1387 IILQDPI-LFSGS-----IRFNLDPECKCTDDRLWEALEIAQLKNMvkslpggLDATVTEGGEnFSVGQRQLFCLARAFV 1460
Cdd:PRK13642 85 MVFQNPDnQFVGAtveddVAFGMENQGIPREEMIKRVDEALLAVNM-------LDFKTREPAR-LSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1461 RKSSILIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA-QEDGV 1536
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAtSEDMV 235
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
684-889 |
2.52e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNesePSFEATRSRSRYsVAYAAQKPwLL----N 759
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD---VTKLPEYKRAKY-IGRVFQDP-MMgtapS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 ATVEENI----------TFGSSFNRQRYKAVTDACSlqpDIDL-----LpfgdQTEIGergiNLSGGQRQRICVARALYQ 824
Cdd:COG1101 97 MTIEENLalayrrgkrrGLRRGLTKKRRELFRELLA---TLGLglenrL----DTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 825 NTNIVFLDDPFSALDIHLSDHLMQegiL--KFLQDDKRTVVLVTHKLQY-LTHADWIIAMKDGSVLRE 889
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRLIMMHEGRIILD 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
684-895 |
2.69e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 65.63 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvNESEPSFEATRSRS--------------RYSVA 749
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING-HKLEYGDYKYRCKHirmifqdpntslnpRLNIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 750 YAAQKPWLLNATVEEnitfgssfnRQRYKAVTDACSLqpdIDLLPfgDQTEIGergIN-LSGGQRQRICVARALYQNTNI 828
Cdd:COG4167 108 QILEEPLRLNTDLTA---------EEREERIFATLRL---VGLLP--EHANFY---PHmLSSGQKQRVALARALILQPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 829 VFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 895
Cdd:COG4167 171 IIADEALAALDMSVRSqiiNLMLE-----LQEKLGiSYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEV 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1308-1533 |
3.15e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 66.64 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFD----GKIVIDGIDISKLP---L 1378
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINLLErptsGSVLVDGVDLTALSereL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1379 HTLRSRLSIILQDpilfsgsirFNLdpeckctddrLWE---------ALEIA-----QLKNMVKSL-------------P 1431
Cdd:COG1135 78 RAARRKIGMIFQH---------FNL----------LSSrtvaenvalPLEIAgvpkaEIRKRVAELlelvglsdkadayP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1432 GGLdatvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENIL---QKVvmtafADR---TVVTIAHRVH 1504
Cdd:COG1135 139 SQL-----------SGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIVLITHEMD 202
|
250 260 270
....*....|....*....|....*....|....*..
gi 3273501 1505 TILT-ADLVIVMKRGNILEYDT-------PESLLAQE 1533
Cdd:COG1135 203 VVRRiCDRVAVLENGRIVEQGPvldvfanPQSELTRR 239
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
684-885 |
3.23e-11 |
|
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: 63.50 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILgemqtlegkvywnnvnesepsfeATRSRSRYsvayaaqkpwllnatve 763
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-----------------------YASGKARL----------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 enITFGSSFNRQRYKAVTdacSLQPDIDL----LPFGDQTEigergiNLSGGQRQRICVARALYQNT-NIVF-LDDPFSA 837
Cdd:cd03238 51 --ISFLPKFSRNKLIFID---QLQFLIDVglgyLTLGQKLS------TLSGGELQRVKLASELFSEPpGTLFiLDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3273501 838 LDIHLSDHLMQEgiLKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGS 885
Cdd:cd03238 120 LHQQDINQLLEV--IKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1308-1533 |
3.69e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHTL- 1381
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFGRNIYSPDVDPIe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 -RSRLSIILQDPILF---------SGSIRFN-LDPECKCTDDRLWEALEIAQL----KNMVKSLPGgldatvteggeNFS 1446
Cdd:PRK14267 83 vRREVGMVFQYPNPFphltiydnvAIGVKLNgLVKSKKELDERVEWALKKAALwdevKDRLNDYPS-----------NLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1447 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILTADLVIVMKRGNILE--- 1522
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgp 231
|
250
....*....|....*
gi 3273501 1523 ----YDTPESLLAQE 1533
Cdd:PRK14267 232 trkvFENPEHELTEK 246
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1308-1541 |
3.94e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 64.57 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1383
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFEtptsGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQDPILF-----SGSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFC 1454
Cdd:cd03300 73 PVNTVFQNYALFphltvFENIAFGLRlkklPK-AEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1455 LARAFVRKSSILIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESLL 1530
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
250
....*....|..
gi 3273501 1531 AQEDGVF-ASFV 1541
Cdd:cd03300 220 EEPANRFvADFI 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
679-900 |
4.23e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 679 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYSVayaAQKPWLL 758
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLV---PQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 -NATVEENITFGSSFNRQRYKAVTD-----ACSLQPDID--LLPFGDQteigerginlsggqrQRICVARALYQNTNIVF 830
Cdd:PRK15439 99 pNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDSSagSLEVADR---------------QIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 831 LDDPFSALDIHLSDHLMQEgiLKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 900
Cdd:PRK15439 164 LDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
687-890 |
4.27e-11 |
|
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: 64.31 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 687 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEAtrsRSRYSVAYAAQK--PWLlnaTVEE 764
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA---RRRLGFVSDSTGlyDRL---TARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 765 NITFGSSFNRQRYKAVTDAcsLQPDIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 844
Cdd:cd03266 98 NLEYFAGLYGLKGDELTAR--LEELADRLGMEELLD--RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3273501 845 HLMQegILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREG 890
Cdd:cd03266 174 ALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1307-1527 |
4.42e-11 |
|
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: 64.67 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1307 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhtlRSR-L 1385
Cdd:cd03296 2 SIEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIILQDPILF-----SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRvkprserPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPE 1527
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTTVFVTHdqeeALEVADRVVVMNKGRIEQVGTPD 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1308-1533 |
4.43e-11 |
|
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: 64.72 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL-SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1386
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1387 II---LQDPIL------------FSGSI-RF-NLDPECKCTDDRLWEALEIAQLKNM-VKSLpggldatvteggenfSVG 1448
Cdd:COG1119 82 LVspaLQLRFPrdetvldvvlsgFFDSIgLYrEPTDEQRERARELLELLGLAHLADRpFGTL---------------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1449 QRQLFCLARAFVRKSSILIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILTA-DLVIVMKRGNILEY 1523
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
250
....*....|
gi 3273501 1524 DTPESLLAQE 1533
Cdd:COG1119 225 GPKEEVLTSE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
680-918 |
4.76e-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: 67.13 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVYWNnVNESE-------PSF------------- 737
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYH-VALCEkcgyverPSKvgepcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 738 ----------EATRSRSRYSVAYAAQKPWLL--NATVEENITfgSSFNRQRYKAVTdacSLQPDIDLLpfgDQTEIGER- 804
Cdd:TIGR03269 91 peevdfwnlsDKLRRRIRKRIAIMLQRTFALygDDTVLDNVL--EALEEIGYEGKE---AVGRAVDLI---EMVQLSHRi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 805 ---GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIA 880
Cdd:TIGR03269 163 thiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIW 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 3273501 881 MKDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQELE 918
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVAVFMEGVS-----EVEKECEVE 274
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1334-1522 |
4.90e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1334 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirfNLDPEcKCT 1410
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-------SLDPR-QTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1411 DDRLWEALEI-------------AQLKNMVKSLPggldATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 1477
Cdd:PRK10261 421 GDSIMEPLRVhgllpgkaaaarvAWLLERVGLLP----EHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1478 ATE----NI---LQKVVMTAFA----DRTVVT-IAHRvhtiltadlVIVMKRGNILE 1522
Cdd:PRK10261 497 SIRgqiiNLlldLQRDFGIAYLfishDMAVVErISHR---------VAVMYLGQIVE 544
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1324-1533 |
5.13e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1324 VLKHVKAYIKPGQKVGICGRTGSGKSSlslAFFRMVDIF---DGKIVIDGIDISKLPLHTlRSRLSI--ILQDPILFSG- 1397
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVprdAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1398 ----------SIRFNLDPECKctDDRLWEALEIAQLKNMVKSLpggldatvtegGENFSVGQRQLFCLARAFVRKSSILI 1467
Cdd:PRK10895 94 svydnlmavlQIRDDLSAEQR--EDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1468 MDEATASIDMATENILQKVVmTAFADR--TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQE 1533
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
668-904 |
5.98e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.11 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWG--SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvnESEPSFEATRSRSR 745
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG--ELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 746 YSVAYAAQKPWLLNATVEENITFG---SSFNRQRYKAVTDACSLQpdIDLLPFgdQTEIGERginLSGGQRQRICVARAL 822
Cdd:PRK13642 83 IGMVFQNPDNQFVGATVEDDVAFGmenQGIPREEMIKRVDEALLA--VNMLDF--KTREPAR---LSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 823 YQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVE 901
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMR--VIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
...
gi 3273501 902 LYE 904
Cdd:PRK13642 234 MVE 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
684-906 |
6.36e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.24 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----YWNNVNESEPSFEATRSRsrysVAYAAQKP--WL 757
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagYHITPETGNKNLKKLRKK----VSLVFQFPeaQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 LNATVEENITFGS-SFNRQRYKAVTDACSLQPDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:PRK13641 99 FENTVLKDVEFGPkNFGFSEDEAKEKALKWLKKVGL----SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 837 ALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKDVELYEHW 906
Cdd:PRK13641 175 GLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHY 243
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1340-1534 |
8.66e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.26 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1340 ICGRTGSGKSSLSLAF----------FRMVDIFDG-KIVIDGIDISKLP-----LHTLRSRLSIILQDP--ILFSGSIRf 1401
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFnglikskygtIQVGDIYIGdKKNNHELITNPYSkkiknFKELRRRVSMVFQFPeyQLFKDTIE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1402 nldpeckctDDRLWEALEIAQLKNMVKSLPG------GLDATVTEGGE-NFSVGQRQLFCLARAFVRKSSILIMDEATAS 1474
Cdd:PRK13631 136 ---------KDIMFGPVALGVKKSEAKKLAKfylnkmGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1475 IDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQED 1534
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLeVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
684-895 |
9.96e-11 |
|
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: 63.33 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVN-ESEPSFEatrsRSRYSVAYAAQKPWLL-NAT 761
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDiTKLPMHK----RARLGIGYLPQEASIFrKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENI-----TFGSSFNRQRYKAVtdacSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:cd03218 92 VEENIlavleIRGLSKKEREEKLE----ELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 837 ALD-IHLSDhlMQEgILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:cd03218 163 GVDpIAVQD--IQK-IIKILKDRGIGVLITDHNVrETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1030-1201 |
1.09e-10 |
|
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: 64.37 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1030 FYVAGFSILCGAGIFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLES 1109
Cdd:cd18552 43 LAIIGLFLLRGLASYL---QTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1110 LTRSTLLCLSAIGMISYA----TPVFLIALAPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAF 1184
Cdd:cd18552 120 LVRDPLTVIGLLGVLFYLdwklTLIALVVLPLAALPIRRIGKRLRKISRRSQEsMGDLTS-----VLQETLSGIRVVKAF 194
|
170
....*....|....*..
gi 3273501 1185 RHETRFKQRMLELTDTN 1201
Cdd:cd18552 195 GAEDYEIKRFRKANERL 211
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1061-1189 |
1.63e-10 |
|
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: 64.07 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1061 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP----VFLIALA 1136
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkltlVMLLVVP 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1137 PLGVAFYFIQKYFRVASKDLQE-LDDSTQLpllchfsetAE----GLTTIRAFRHETR 1189
Cdd:cd18573 153 PIAVGAVFYGRYVRKLSKQVQDaLADATKV---------AEerlsNIRTVRAFAAERK 201
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
683-895 |
2.12e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.50 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 683 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVywnNVNESEPSfEATRSRSRYSVAYAAQKP--WLLNA 760
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI---TVGGMVLS-EETVWDVRRQVGMVFQNPdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITFGSSFN----RQRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:PRK13635 98 TVQDDVAFGLENIgvprEEMVERVDQALRQ---VGMEDFLNREPH-----RLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 837 ALDIHLSDHLMqeGILKFLQDDKR-TVVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK13635 170 MLDPRGRREVL--ETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1312-1531 |
2.70e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1312 DLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIIL 1389
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1390 QDP---ILFS---GSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKslpggldatvtEGGENFSVGQRQLFCLARAF 1459
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRnlgvPEAEITR-RVDEALTLVDAQHFRH-----------QPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1460 VRKSSILIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1531
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYeISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
667-891 |
2.73e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVYWNNVNESEPSFEATRSRS 744
Cdd:PRK11124 2 SIQLNGINCFYGAHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLrvLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 745 RYSVAYAAQK----PWLlnaTVEENIT------FGSSfnrqRYKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQ 814
Cdd:PRK11124 81 RRNVGMVFQQynlwPHL---TVQQNLIeapcrvLGLS----KDQALARAEKLLERLRLKPYADRFPL-----HLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 815 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGT 891
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
679-900 |
2.99e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 679 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNV--NESEPSFEATRSrsrYSVAYaaQKPW 756
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAAQLG---IGIIY--QELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 757 LLNA-TVEENITFGS--------------SFNRQRYKAVTDACSLQPDIDllpfgdqteigERGINLSGGQRQRICVARA 821
Cdd:PRK09700 91 VIDElTVLENLYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 822 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 900
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
682-899 |
3.15e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 682 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--------TLEGKVYWNnvneSEP--SFEATR-SRSRYSVAY 750
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN----GEPlaAIDAPRlARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 751 AAQKPWLLnaTVEENITFGSSFNRQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ------ 824
Cdd:PRK13547 91 AAQPAFAF--SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 825 ---NTNIVFLDDPFSALDI-HlsDHLMQEGILKFLQDDKRTVVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKD 899
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLaH--QHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVLTPA 246
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
684-903 |
3.31e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 61.92 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVN-ESEPSFEatrsRSRYSVAYAAQK----PWLl 758
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDiTGLPPHR----IARLGIGYVPEGrrifPSL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 naTVEENITFGSSFNRqrykavtDACSLQPDID----LLPfgdqtEIGER----GINLSGGQRQRICVARALYQNTNIVF 830
Cdd:COG0410 94 --TVEENLLLGAYARR-------DRAEVRADLErvyeLFP-----RLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 831 LDDPfSAldiHLSDHLMQE--GILKFLQDDKRTVVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDIQTKD--VELY 903
Cdd:COG0410 160 LDEP-SL---GLAPLIVEEifEIIRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLADPevREAY 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
684-892 |
3.44e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVYWNNVNESEPSFEATRSRSRYSVAYAAQKPWLL-NAT 761
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLL-HLLGGLDTpTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITF----GssfNRQRYKAVTDACSLqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 837
Cdd:PRK11629 104 ALENVAMplliG---KKKPAEINSRALEM-----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 838 LDIHLSDHLMQegILKFLQDDKRTVVL-VTHKLQYLTHADWIIAMKDGSVLREGTL 892
Cdd:PRK11629 176 LDARNADSIFQ--LLGELNRLQGTAFLvVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1274-1536 |
3.44e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1274 AVKKVNSFltmESENYEGTMDPSQVPEHWPQegeIKIHDLCVRYENN---LKPVlkhvKAYIKPGQKVGICGRTGSGKSS 1350
Cdd:PRK10522 295 AFNKLNKL---ALAPYKAEFPRPQAFPDWQT---LELRNVTFAYQDNgfsVGPI----NLTIKRGELLFLIGGNGSGKST 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1351 LSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSirfnLDPECKCTDDRLWEA-LEIAQLKNMVKS 1429
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLEL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1430 LPGGLDATvteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTIL 1507
Cdd:PRK10522 441 EDGRISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFI 514
|
250 260
....*....|....*....|....*....
gi 3273501 1508 TADLVIVMKRGNILEYDTPESLLAQEDGV 1536
Cdd:PRK10522 515 HADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1325-1531 |
3.90e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1325 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPI----------- 1393
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1394 LFSGSIRFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1472
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPHML-----------APGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1473 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT---ADLVIVMKRGNILEYDTPESLLA 1531
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMkhiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
679-886 |
4.12e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 60.52 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 679 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYwnnVNESEPSFEATRSRSRYSVAYAA----QK 754
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT---LDGKPVTRRSPRDAIRAGIAYVPedrkRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 755 PWLLNATVEENITFGSSfnrqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDP 834
Cdd:cd03215 88 GLVLDLSVAENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3273501 835 FSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSV 886
Cdd:cd03215 132 TRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
682-897 |
4.41e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.99 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 682 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLL------LAILGEMQTLEGKVYWnnVNESEPSFEATRSRSRYSVAYAAQKP 755
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnrlIEIYDSKIKVDGKVLY--FGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 756 WLlNATVEENITFGSSFN----RQRYKAVTDACslqpdidLLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTN 827
Cdd:PRK14246 102 FP-HLSIYDNIAYPLKSHgikeKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 828 IVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR--TVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 897
Cdd:PRK14246 174 VLLMDEPTSMIDI-----VNSQAIEKLITELKNeiAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1309-1479 |
6.52e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 6.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1309 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAF--------FRmvdiFDGKIVIDGIDISKLPlhT 1380
Cdd:COG4136 3 SLENLTITLGG--RPLLAPLSLTVAPGEILTLMGPSGSGKSTL-LAAiagtlspaFS----ASGEVLLNGRRLTALP--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 LRSRLSIILQDPILFS-----GSIRFNLDPECKCTD--DRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLF 1453
Cdd:COG4136 74 EQRRIGILFQDDLLFPhlsvgENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPATL-----------SGGQRARV 142
|
170 180
....*....|....*....|....*.
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDMAT 1479
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAAL 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
684-867 |
6.55e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.55 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWnnvnesepsfeatrsRSRYSVAYAAQKPWLL-NATV 762
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------------PKGLRIGYLPQEPPLDdDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITfgSSFNR-----QRYKAVTDACSlQPDIDLLPFGD-QTEIGER----------------GI----------NLSG 810
Cdd:COG0488 79 LDTVL--DGDAElraleAELEELEAKLA-EPDEDLERLAElQEEFEALggweaearaeeilsglGFpeedldrpvsELSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 811 GQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhlmqEGIL---KFLQDDKRTVVLVTH 867
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDL--------ESIEwleEFLKNYPGTVLVVSH 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
680-890 |
6.76e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYwnnVNESEPSFEATRSRSRYSVAYAAQKPWLL- 758
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---IDGQEMRFASTTAALAAGVAIIYQELHLVp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 NATVEENITFG---SSF---NRQRYKAVTDACSLQPDIDLLPfgdQTEIGErginLSGGQRQRICVARALYQNTNIVFLD 832
Cdd:PRK11288 93 EMTVAENLYLGqlpHKGgivNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 833 DPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLqylthaDWIIAMKDG-SVLREG 890
Cdd:PRK11288 166 EPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1308-1533 |
7.55e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:PRK09536 4 IDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPilfsgSIRFNLDPE----------------CKCTDDRLWE-ALEIAQLKNMVkslpgglDATVTEggenFSVGQR 1450
Cdd:PRK09536 82 VPQDT-----SLSFEFDVRqvvemgrtphrsrfdtWTETDRAAVErAMERTGVAQFA-------DRPVTS----LSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1451 QLFCLARAFVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLTA---DLVIVMKRGNILEYDTP 1526
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPP 223
|
....*..
gi 3273501 1527 ESLLAQE 1533
Cdd:PRK09536 224 ADVLTAD 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1320-1538 |
7.88e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1320 NLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPiLFS 1396
Cdd:PRK15079 33 TLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddEWRAVRSDIQMIFQDP-LAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1397 GSIRFNLdpeckctDDRLWEALEI-------AQLKNMVKSL---PGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSIL 1466
Cdd:PRK15079 111 LNPRMTI-------GEIIAEPLRTyhpklsrQEVKDRVKAMmlkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1467 IMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHR---VHTIltADLVIVMKRGNILEydtpeslLAQEDGVFA 1538
Cdd:PRK15079 184 ICDEPVSALDVSIQaqvvNLLQQ--LQREMGLSLIFIAHDlavVKHI--SDRVLVMYLGHAVE-------LGTYDEVYH 251
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
684-895 |
8.55e-10 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 61.99 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVYWNNVN---ESEPSFEATRSRSrysVAYAAQKPwl 757
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDllkLSEKELRKIRGRE---IQMIFQDP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 LNA-----TVEENIT------FGSSfNRQRYKAVtdacslqpdIDLLpfgdqteigER-GIN------------LSGGQR 813
Cdd:COG0444 96 MTSlnpvmTVGDQIAeplrihGGLS-KAEARERA---------IELL---------ERvGLPdperrldrypheLSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 814 QRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TVVLVTHKL---QYLthADWIIAMKDGSV 886
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITHDLgvvAEI--ADRVAVMYAGRI 229
|
....*....
gi 3273501 887 LREGTLKDI 895
Cdd:COG0444 230 VEEGPVEEL 238
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1307-1501 |
8.59e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1307 EIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI--SKLPLH 1379
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1380 TLRSRLSIILQDPILFSGSIRFNLDPECKCT------DDRLWEALEIAQLKNMVKSlpggldaTVTEGGENFSVGQRQLF 1453
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1501
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
680-901 |
1.19e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.53 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVYWNnvnESEPSFEATRSRSRYSVAYAAQKPWL 757
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWS---GSPLKASNIRDTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 L-NATVEENITFGSSF----NRQRYKAVTDAC-------SLQPDIDLLPFGDqteigerginLSGGQRQRICVARALYQN 825
Cdd:TIGR02633 90 VpELSVAENIFLGNEItlpgGRMAYNAMYLRAknllrelQLDADNVTRPVGD----------YGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 826 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKDVE 901
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLD--IIRDLKAHGVACVYISHKL------NEVKAVCDTiCVIRDG--QHVATKDMS 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1323-1520 |
1.33e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1323 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfdGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG-- 1397
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDS--GTLEIGGNPCARLtPAKAHQLGIYLVPQEPLLFPNls 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1398 ---SIRFNLdPEckctddrlwEALEIAQLKNMVKSLPGGLDATVTEGgeNFSVGQRQLFCLARAFVRKSSILIMDEATAS 1474
Cdd:PRK15439 103 vkeNILFGL-PK---------RQASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 3273501 1475 IDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1520
Cdd:PRK15439 171 LTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1308-1501 |
1.34e-09 |
|
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: 58.23 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmvdifdgkividgidisklplhtlrsrLSI 1387
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPILFSGSIRFNldpeckctddrlwEALEIAQLknmvkslpggldatvteggENFSVGQRQLFCLARAFVRKSSILI 1467
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 3273501 1468 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1501
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
684-895 |
1.35e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.63 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILgEMQTlEGKVYWNNVNESEPSFEATRsRSRYSVAYAAQKPWLLNA- 760
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLL-ERPT-SGSVLVDGVDLTALSERELR-AARRKIGMIFQHFNLLSSr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITF-----GSSfNRQRYKAVTDacslqpdidLLPFgdqTEIGERG----INLSGGQRQRICVARALYQNTNIVFL 831
Cdd:COG1135 98 TVAENVALpleiaGVP-KAEIRKRVAE---------LLEL---VGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 832 DDPFSALDIHLSDhlmqeGILKFLQDDKR----TVVLVTH------KLqylthADWIIAMKDGSVLREGTLKDI 895
Cdd:COG1135 165 DEATSALDPETTR-----SILDLLKDINRelglTIVLITHemdvvrRI-----CDRVAVLENGRIVEQGPVLDV 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
667-890 |
1.37e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 667 AIKVTNGYfswgSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRS--RS 744
Cdd:PRK14271 24 AVNLTLGF----AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDvlEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 745 RYSVAYAAQKPWLLNATVEENITFGSSFN----RQRYKAVTDACSLQPDI-DLLpfgdQTEIGERGINLSGGQRQRICVA 819
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVLAGVRAHklvpRKEFRGVAQARLTEVGLwDAV----KDRLSDSPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 820 RALYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFLQD--DKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREG 890
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTT-----EKIEEFIRSlaDRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
686-895 |
1.38e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.81 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN--VNESEPSFEATRSRSRysVAYAAQKPWLL-NATV 762
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvLFDAEKGICLPPEKRR--IGYVFQDARLFpHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFG-SSFNRQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 841
Cdd:PRK11144 94 RGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 842 LSDHLMQegilkFLQDDKRTV----VLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK11144 163 RKRELLP-----YLERLAREInipiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEEV 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
683-886 |
1.62e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.52 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 683 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWnnvnESEPSFEATRSRSRYSVAYAAQKP--WLLNA 760
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII----DGDLLTEENVWDIRHKIGMVFQNPdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITFG---SSFNRQRYKA-VTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:PRK13650 98 TVEDDVAFGlenKGIPHEEMKErVNEALEL---VGMQDFKEREPA-----RLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 3273501 837 ALDIHLSDHLMQEgILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSV 886
Cdd:PRK13650 170 MLDPEGRLELIKT-IKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
680-884 |
1.80e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.50 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESE-PSFEATRSRSRYSVAYAAQKpWLL 758
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQIGMIFQDHH-LLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 NATVEENITF-----GSSFN--RQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFL 831
Cdd:PRK10908 93 DRTVYDNVAIpliiaGASGDdiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 832 DDPFSALDIHLSdhlmqEGILKFLQDDKR---TVVLVTHKLQYLTHADW-IIAMKDG 884
Cdd:PRK10908 162 DEPTGNLDDALS-----EGILRLFEEFNRvgvTVLMATHDIGLISRRSYrMLTLSDG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1323-1530 |
1.84e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.11 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1323 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRLSIILQdpilfsgsiR 1400
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQ---------Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1401 FNLDPECKCTDDRLWEALEI-----AQLKNMVKSLPG--GLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1473
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVrgaskEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1474 SIDmatENILQKV--VMTAFADR----TVVT----IAHRVHTILtadlvIVMKRGNILEYDTPESLL 1530
Cdd:PRK09493 166 ALD---PELRHEVlkVMQDLAEEgmtmVIVTheigFAEKVASRL-----IFIDKGRIAEDGDPQVLI 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
659-867 |
1.97e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.00 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 659 RPAETEDVAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVywNNVNESEPSfE 738
Cdd:PRK13536 33 IPGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI--TVLGVPVPA-R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 739 ATRSRSRYSVAyaAQKPWL-LNATVEEN-ITFGSSF--NRQRYKAVTDAcslqpdidLLPFGD-QTEIGERGINLSGGQR 813
Cdd:PRK13536 109 ARLARARIGVV--PQFDNLdLEFTVRENlLVFGRYFgmSTREIEAVIPS--------LLEFARlESKADARVSDLSGGMK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 3273501 814 QRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKrTVVLVTH 867
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
679-901 |
2.05e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 679 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVYWnnvnESEP-SFEATRSRSRYSVAYAAQKP 755
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIF----EGEElQASNIRDTERAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 756 WLL-NATVEENITFGS---SFNRQRYKAVTDACS-----LQPDIDLlpfgdQTEIGergiNLSGGQRQRICVARALYQNT 826
Cdd:PRK13549 92 ALVkELSVLENIFLGNeitPGGIMDYDAMYLRAQkllaqLKLDINP-----ATPVG----NLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 827 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKDVE 901
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLD--IIRDLKAHGIACIYISHKL------NEVKAISDTiCVIRDG--RHIGTRPAA 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1307-1533 |
2.19e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1307 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1386
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1387 IILQDPILFSG-SIR----------FNLDPECKCTDDRLWE-ALEIAQLKNMVkslpgglDATVTEggenFSVGQRQLFC 1454
Cdd:PRK11231 80 LLPQHHLTPEGiTVRelvaygrspwLSLWGRLSAEDNARVNqAMEQTRINHLA-------DRRLTD----LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1455 LARAFVRKSSILIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTP 228
|
.
gi 3273501 1533 E 1533
Cdd:PRK11231 229 G 229
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
987-1199 |
2.54e-09 |
|
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: 60.50 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 987 FFLLFLMIFSKLLkhsvIVAIDYWLATWTSEYSINDPGKADQTF-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAA---- 1061
Cdd:cd18547 2 ILVIILAIISTLL----SVLGPYLLGKAIDLIIEGLGGGGGVDFsGLLRILLLLLGLYLLSALFSYLQNRLMARVSqrtv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1062 KNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLIALAPLGV 1140
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLImMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1141 AFYFI-------QKYFRVASKDLQELDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTD 1199
Cdd:cd18547 158 SLLVTkfiakrsQKYFRKQQKALGELNGYIE--------EMISGQKVVKAFNREEEAIEEFDEINE 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1251-1532 |
3.28e-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: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1251 ALTITNYLNWVVRNLADLEVQM--GAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHV 1328
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLenGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKAV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1329 KAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI----DGIDISKlPLHTLRSR----LSIILQDPILFSG 1397
Cdd:TIGR03269 301 DNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTK-PGPDGRGRakryIGILHQEYDLYPH 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1398 SIRFnldpeckctdDRLWEAL------EIAQLKNMVKSLPGGLDATVTEG-----GENFSVGQRQLFCLARAFVRKSSIL 1466
Cdd:TIGR03269 380 RTVL----------DNLTEAIglelpdELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIV 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1467 IMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLdVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1322-1529 |
3.48e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1322 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILF-- 1395
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEqptaGQIMLDGVDLSHVPPY--QRPINMMFQSYALFph 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1396 ---SGSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIM 1468
Cdd:PRK11607 106 mtvEQNIAFGLKqdklPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1469 DEATASID------MATE--NILQKVVMTAfadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESL 1529
Cdd:PRK11607 174 DEPMGALDkklrdrMQLEvvDILERVGVTC------VMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1325-1532 |
3.76e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.79 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1325 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP----LHTLRSRLSIILQDP-------- 1392
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQFPesqlfedt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1393 ----ILFsGSIRFNLDPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIM 1468
Cdd:PRK13646 103 vereIIF-GPKNFKMNLD-EVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1469 DEATASIDMATenilQKVVMTAFA------DRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1532
Cdd:PRK13646 170 DEPTAGLDPQS----KRQVMRLLKslqtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
985-1201 |
3.88e-09 |
|
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: 59.87 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 985 GGFFLLFLMIFSKLLKHSVIVAIDYWLATWtseysindpgkadqtfYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 1064
Cdd:cd07346 11 ATALGLALPLLTKLLIDDVIPAGDLSLLLW----------------IALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1065 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLIALAPL---GV 1140
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALViLFYLNWKLTLVALLLLplyVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1141 AFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTN 1201
Cdd:cd07346 155 ILRYFRRRIRKASREVREsLAELSA-----FLQESLSGIRVVKAFAAEEREIERFREANRDL 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
684-905 |
3.90e-09 |
|
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: 58.31 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTL--EGKVYW--NNVNESEPSfeatrSRSRYSVAYAAQKPwlln 759
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFkgEDITDLPPE-----ERARLGIFLAFQYP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 atveenitfgssfnrQRYKAVTDAcslqpdiDLLpfgdqteigeRGIN--LSGGQRQRICVARALYQNTNIVFLDDPFSA 837
Cdd:cd03217 87 ---------------PEIPGVKNA-------DFL----------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 838 LDIhlsDHL-MQEGILKFLQDDKRTVVLVTHKLQYLTH--ADWIIAMKDGSVLREGtlkdiqtkDVELYEH 905
Cdd:cd03217 135 LDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSG--------DKELALE 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1308-1479 |
4.40e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 58.60 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKL---PLHTL 1381
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPTsGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1382 RSR-LSIILQD---------------PILFSGsirfnlDPECKctdDRLWEALEIAQLKNMVKSLPGGLdatvtEGGEnf 1445
Cdd:COG4181 88 RARhVGFVFQSfqllptltalenvmlPLELAG------RRDAR---ARARALLERVGLGHRLDHYPAQL-----SGGE-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 3273501 1446 svgqRQLFCLARAFVRKSSILIMDEATASIDMAT 1479
Cdd:COG4181 152 ----QQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
684-890 |
4.73e-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: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvnesEPSFEATRSRsrysVAYAAQKPWL-LNATV 762
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNR----IGYLPEERGLyPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFgssFNRQRYKAVTDAcslQPDID-LLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDI 840
Cdd:cd03269 88 IDQLVY---LAQLKGLKKEEA---RRRIDeWLERLELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3273501 841 HLSDHLMQEgiLKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREG 890
Cdd:cd03269 162 VNVELLKDV--IRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
653-886 |
5.35e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.46 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 653 EQARRL--RPAETEDVAikvtngyFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWN-N 729
Cdd:COG0488 306 PPPERLgkKVLELEGLS-------KSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeT 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 730 VNesepsfeatrsrsrysVAYAAQKPWLL--NATVEENITFGSSFNRQRYkaVTDACSlqpdiDLLpF-GDQ--TEIGer 804
Cdd:COG0488 378 VK----------------IGYFDQHQEELdpDKTVLDELRDGAPGGTEQE--VRGYLG-----RFL-FsGDDafKPVG-- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 805 giNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKRTVVLVTHKLQYL-THADWIIAMKD 883
Cdd:COG0488 432 --VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHDRYFLdRVATRILEFED 504
|
...
gi 3273501 884 GSV 886
Cdd:COG0488 505 GGV 507
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1308-1534 |
5.41e-09 |
|
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: 58.60 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYeNNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHtLRS 1383
Cdd:cd03219 1 LEVRGLTKRF-GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLISGFlrptSGSVLFDGEDITGLPPH-EIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSII--LQDPILFSG-SIRFNLD-----------------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvtegge 1443
Cdd:cd03219 74 RLGIGrtFQIPRLFPElTVLENVMvaaqartgsglllararREEREARERAEELLERVGLADLADRPAGEL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1444 nfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1521
Cdd:cd03219 145 --SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
250
....*....|...
gi 3273501 1522 EYDTPESLLAQED 1534
Cdd:cd03219 223 AEGTPDEVRNNPR 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
684-870 |
6.10e-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: 58.11 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVywnNVNESEPSFEATRSRSRYSVAYAaQKpwllnATVE 763
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV---RVAGLVPWKRRKKFLRRIGVVFG-QK-----TQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 764 ENITFGSSFN---------RQRYKAVTDACSlqpdiDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDP 834
Cdd:cd03267 108 WDLPVIDSFYllaaiydlpPARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 3273501 835 FSALDIHlsdhlMQEGILKFLQDDKR----TVVLVTHKLQ 870
Cdd:cd03267 181 TIGLDVV-----AQENIRNFLKEYNRergtTVLLTSHYMK 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
684-905 |
6.33e-09 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 58.56 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEM-----QTLE------GKVYWNNVnesepsfeatrsRSRYSVAYAA 752
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygNDVRlfgerrGGEDVWEL------------RKRIGLVSPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 753 -QKPWLLNATVEENIT---FGSSFnrqRYKAVTDAcslqpDI----DLLPFGDQTEIGERGIN-LSGGQRQRICVARALY 823
Cdd:COG1119 87 lQLRFPRDETVLDVVLsgfFDSIG---LYREPTDE-----QRerarELLELLGLAHLADRPFGtLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 824 QNTNIVFLDDPFSALDIHlsdhlMQEGILKFL----QDDKRTVVLVTHKLQYL----THAdwiIAMKDGSVLREGTLKDI 895
Cdd:COG1119 159 KDPELLILDEPTAGLDLG-----ARELLLALLdklaAEGAPTLVLVTHHVEEIppgiTHV---LLLKDGRVVAAGPKEEV 230
|
250
....*....|..
gi 3273501 896 QTKDV--ELYEH 905
Cdd:COG1119 231 LTSENlsEAFGL 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
699-943 |
6.55e-09 |
|
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: 60.33 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 699 IVGQVGCGKSSLLLAILGEMQTLEGkvywnnvnesepsfEATRSRSrYSVAYAAQKPWL-LNATVEENITFGSSFNRQ-- 775
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPG-IKVGYLPQEPQLdPTKTVRENVEEGVAEIKDal 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 776 -RYKAVTDACS---------------LQPDIDL------------------LPFGDQtEIGergiNLSGGQRQRICVARA 821
Cdd:TIGR03719 101 dRFNEISAKYAepdadfdklaaeqaeLQEIIDAadawdldsqleiamdalrCPPWDA-DVT----KLSGGERRRVALCRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 822 LYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDG-SVLREGTlkdiq 896
Cdd:TIGR03719 176 LLSKPDMLLLDEP--------TNHLDAESVAwleRHLQEYPGTVVAVTHDRYFLDNvAGWILELDRGrGIPWEGN----- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 3273501 897 tkdvelYEHW---KTlmNRQDQElEKDMEADQTTLERKT--LRRAMYSREAK 943
Cdd:TIGR03719 243 ------YSSWleqKQ--KRLEQE-EKEESARQKTLKRELewVRQSPKGRQAK 285
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1324-1536 |
9.84e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.17 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1324 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIILQDP--ILFSGSI 1399
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1400 R-------FNLDPECKCTDDRLWEALEIAQLKNMVKSLPggldatvteggENFSVGQRQLFCLARAFVRKSSILIMDEAT 1472
Cdd:PRK13639 97 EedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1473 ASID-MATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLLAQEDGV 1536
Cdd:PRK13639 166 SGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1323-1527 |
1.06e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1323 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LA-FFRMvDifDGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG- 1397
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMkiLSgVYQP-D--SGEILLDGEPVRFRsPRDAQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1398 SIRFNL------------DpeckctddrlWEALeIAQLKNMVKSLpgGLDATVTEGGENFSVGQRQLFCLARAFVRKSSI 1465
Cdd:COG1129 95 SVAENIflgreprrggliD----------WRAM-RRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1466 LIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG-NILEYDTPE 1527
Cdd:COG1129 162 LILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGrLVGTGPVAE 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
684-895 |
1.12e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.66 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTlEGKVYWNNVNESEPSFEATRsRSRYSVAYAAQKPWLLNA-T 761
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERPT-SGRVLVDGQDLTALSEKELR-KARRQIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITF-----------------------GSSFNRQRYKAvtdacslqpdidllpfgdqteigergiNLSGGQRQRICV 818
Cdd:PRK11153 99 VFDNVALplelagtpkaeikarvtellelvGLSDKADRYPA---------------------------QLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 819 ARALYQNTNIVFLDDPFSALDIHLSDhlmqeGILKFLQDDKR----TVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLK 893
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVS 226
|
..
gi 3273501 894 DI 895
Cdd:PRK11153 227 EV 228
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
684-891 |
1.39e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.62 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL---------------GEMQTLEG-----KVYwnNVNESEP-----SFE 738
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGlehidKVI--VIDQSPIgrtprSNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 739 ATRSR---------------SRY-----SVAYAAQK-PWLLNATVEENITFGSSFNRQRYKAVTdacsLQpDIDLlpfgD 797
Cdd:cd03271 89 ATYTGvfdeirelfcevckgKRYnretlEVRYKGKSiADVLDMTVEEALEFFENIPKIARKLQT----LC-DVGL----G 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 798 QTEIGERGINLSGGQRQRICVARALYQNTN---IVFLDDPFSALdiHLSD--HLMQegILKFLQDDKRTVVLVTHKLQYL 872
Cdd:cd03271 160 YIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL--HFHDvkKLLE--VLQRLVDKGNTVVVIEHNLDVI 235
|
250 260
....*....|....*....|....*
gi 3273501 873 THADWIIAM------KDGSVLREGT 891
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGT 260
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
649-895 |
1.93e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 649 LDNYEQARRLRPAETEDVAIKVTN---GYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK 724
Cdd:TIGR03269 261 MEGVSEVEKECEVEVGEPIIKVRNvskRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 725 VY------WnnVNESEPSFEAtRSRSRYSVAYAAQKPWLL-NATVEENITFGSS----FNRQRYKAVtdacslqpdIDLL 793
Cdd:TIGR03269 341 VNvrvgdeW--VDMTKPGPDG-RGRAKRYIGILHQEYDLYpHRTVLDNLTEAIGlelpDELARMKAV---------ITLK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 794 PFGDQTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTVVLVTHK 868
Cdd:TIGR03269 409 MVGFDEEKAEEILDkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMD-PITKVDVTHSILKAREEMEQTFIIVSHD 487
|
250 260
....*....|....*....|....*...
gi 3273501 869 LQY-LTHADWIIAMKDGSVLREGTLKDI 895
Cdd:TIGR03269 488 MDFvLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1308-1524 |
2.24e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHT-- 1380
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 LRSRLSIILQDPILFSGSI--------RFNLDPECKCTDDRLWEALEIAQLKNMVKSlpggldaTVTEGGENFSVGQRQL 1452
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 1453 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYD 1524
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYN 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1308-1533 |
2.40e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1387
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPIL-FSGS----IRFNLDP--ECKCTDDRLW-EALEIAQLKNMvkslpGGLDATVTEGGENfsvgQR-QlfcLARA 1458
Cdd:PRK13548 81 LPQHSSLsFPFTveevVAMGRAPhgLSRAEDDALVaAALAQVDLAHL-----AGRDYPQLSGGEQ----QRvQ---LARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1459 FVR------KSSILIMDEATASIDMATenilQKVVMTA---FADR---TVVTIAHRVH-TILTADLVIVMKRGNILEYDT 1525
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAH----QHHVLRLarqLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
....*...
gi 3273501 1526 PESLLAQE 1533
Cdd:PRK13548 225 PAEVLTPE 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
684-891 |
2.67e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGE--MQTLEGKVYWN--NVNESEPSfeatrSRSRYSVAYAAQKPwlln 759
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKgeSILDLEPE-----ERAHLGIFLAFQYP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 atVEENITFGSSFNRQRYKAVTDACSLqPDIDLLPF-----------GDQTEIGERGIN--LSGGQRQRICVARALYQNT 826
Cdd:CHL00131 94 --IEIPGVSNADFLRLAYNSKRKFQGL-PELDPLEFleiineklklvGMDPSFLSRNVNegFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 827 NIVFLDDPFSALDIhlsDHLMQ--EGILKFLQDDKrTVVLVTHK---LQYLThADWIIAMKDGSVLREGT 891
Cdd:CHL00131 171 ELAILDETDSGLDI---DALKIiaEGINKLMTSEN-SIILITHYqrlLDYIK-PDYVHVMQNGKIIKTGD 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
679-868 |
2.69e-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: 58.61 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 679 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMqtlegkvyWnnvnesePSFEATRSR-SRYSVAYAAQKPWL 757
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLF-RILGEL--------W-------PVYGGRLTKpAKGKLFYVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 LNATVEENITFGSSFNRQRYKAVTDAcSLQPDIDLLpfgDQTEIGERGIN----------LSGGQRQRICVARALYQNTN 827
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDK-DLEQILDNV---QLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 3273501 828 IVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTVVLVTHK 868
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYR-----LCREFGITLFSVSHR 638
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1308-1533 |
3.01e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRL 1385
Cdd:CHL00131 8 LEIKNLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLSkvIAGHPAYKILEGDILFKGESILDLE-PEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1386 SIIL--QDPILFSGS-----IRFNLDPECKCTDDRLWEALE----IAQLKNMVKSLPGGLDATVTEGgenFSVGQRQLFC 1454
Cdd:CHL00131 85 GIFLafQYPIEIPGVsnadfLRLAYNSKRKFQGLPELDPLEfleiINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1455 LARAFVRKSSILIMDEATASIDM-ATENILQKVVMTAFADRTVVTIAH--RVHTILTADLVIVMKRGNILEydTPESLLA 1531
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIdALKIIAEGINKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK--TGDAELA 239
|
..
gi 3273501 1532 QE 1533
Cdd:CHL00131 240 KE 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
681-889 |
3.34e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 681 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRYSVAYAAQKPWL--- 757
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLipt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 LNATveENITF-----GSSFNRQRYKAvtdacslqpdIDLLpfgDQTEIGER----GINLSGGQRQRICVARALYQNTNI 828
Cdd:PRK10584 103 LNAL--ENVELpallrGESSRQSRNGA----------KALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 829 VFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGSvLRE 889
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIA-DLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ-LQE 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1315-1515 |
3.79e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.88 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1315 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 1394
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1395 FSGSIRFNLD-PeckctddrlWEALEIA-QLKNMVKSLPG-GLDATVTEGGEN-FSVGQRQLFCLARAFVRKSSILIMDE 1470
Cdd:PRK10247 93 FGDTVYDNLIfP---------WQIRNQQpDPAIFLDDLERfALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3273501 1471 ATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVM 1515
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1308-1531 |
3.84e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.89 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD---GKIV----------------- 1367
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1368 ----------------IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFnLDPECKCTDDRLWEALE----IAQLKNMV 1427
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTV-LDNVLEALEEIGYEGKEavgrAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1428 KslpggLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHT 1505
Cdd:TIGR03269 157 Q-----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|....*..
gi 3273501 1506 IL-TADLVIVMKRGNILEYDTPESLLA 1531
Cdd:TIGR03269 232 IEdLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1312-1524 |
4.10e-08 |
|
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: 55.38 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1312 DLCVRYENNLKPVlkHVK-AYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDG---IDISK---LPLHt 1380
Cdd:cd03297 1 MLCVDIEKRLPDF--TLKiDFDLNEEVTGIFGASGAGKSTL----LRCIagleKPDGGTIVLNGtvlFDSRKkinLPPQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 lRSRLSIILQDPILFSG-SIRFNLD---PECKCTDDRLW--EALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFC 1454
Cdd:cd03297 74 -QRKIGLVFQQYALFPHlNVRENLAfglKRKRNREDRISvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 1455 LARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1524
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQLLPELkqIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
675-899 |
4.29e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 56.35 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 675 FSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVywnnVNESEPSFEATRSRSRYSVAYAAQK 754
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV----LIRGEPITKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 755 P--WLLNATVEENITFG-------SSFNRQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQN 825
Cdd:PRK13652 87 PddQIFSPTVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 826 TNIVFLDDPFSALDIHLSDHLmqegiLKFLQDDKR----TVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKD 899
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKEL-----IDFLNDLPEtygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
661-899 |
5.17e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 661 AETEDVAIKVTNGYFSWGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNnvNESEPSFeat 740
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD--GENIPAM--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 741 rSRSRYsvaYAAQKPWLL---------NATVEENITFGSSFNRQRYKAVT--------DACSLQPDIDLLPfgdqteige 803
Cdd:PRK11831 75 -SRSRL---YTVRKRMSMlfqsgalftDMNVFDNVAYPLREHTQLPAPLLhstvmmklEAVGLRGAAKLMP--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 804 rgINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-IHLsdhlmqeGILKFLQDDKR-----TVVLVTHKL-QYLTHAD 876
Cdd:PRK11831 142 --SELSGGMARRAALARAIALEPDLIMFDEPFVGQDpITM-------GVLVKLISELNsalgvTCVVVSHDVpEVLSIAD 212
|
250 260
....*....|....*....|....*
gi 3273501 877 --WIIAmkDGSVLREGTLKDIQTKD 899
Cdd:PRK11831 213 haYIVA--DKKIVAHGSAQALQANP 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
668-891 |
5.57e-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: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 668 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQTLEGKVYWNNVNEsepsfEATRSRSR 745
Cdd:cd03265 1 IEVENLVKKYGDFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTikMLTTLLKPTSGRATVAGHDVVR-----EPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 746 ysVAYAAQKPWLLNA-TVEENI-TFGSSFNRQRYKAVTDACSLQPDIDLLPFGDqteigERGINLSGGQRQRICVARALY 823
Cdd:cd03265 75 --IGIVFQDLSVDDElTGWENLyIHARLYGVPGAERRERIDELLDFVGLLEAAD-----RLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 824 QNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTVVLVTHklqYLTHA----DWIIAMKDGSVLREGT 891
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVW-EYIEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGT 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
662-884 |
6.15e-08 |
|
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: 55.13 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 662 ETEDVAIKVTNGyfswGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILgEMQTlEGKVYWNNVNESEPSFEA 739
Cdd:COG4181 10 ELRGLTKTVGTG----AGELTILKGISLEVEAGESVAIVGASGSGKSTLLglLAGL-DRPT-SGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 740 -TRSRSRySVAYAAQKPWLLNA-TVEENIT-----FGSSFNRQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQ 812
Cdd:COG4181 84 rARLRAR-HVGFVFQSFQLLPTlTALENVMlplelAGRRDARARARALLERVGLGHRLDHYP--AQ---------LSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 813 RQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegiLKF-LQDDKR-TVVLVTHKLQYLTHADWIIAMKDG 884
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIID---LLFeLNRERGtTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1324-1527 |
6.49e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1324 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLplHTLRSRLSIILQDPILF---- 1395
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAGLEhqtsGHIRFHGTDVSRL--HARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1396 -SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILI 1467
Cdd:PRK10851 91 vFDNIAFGLTvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 1468 MDEATASIDMATENILQKVVMTAFADR--TVVTIAH-RVHTILTADLVIVMKRGNILEYDTPE 1527
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
679-884 |
9.19e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 679 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI---LGEMQTLEGKVYWNNVNESEpsfeaTRSRSRYSVAYAAQK- 754
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKE-----FAEKYPGEIIYVSEEd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 755 ---PWLlnaTVEENITFgssfnrqrykavtdACSLQpdidllpfGDQTEigeRGInlSGGQRQRICVARALYQNTNIVFL 831
Cdd:cd03233 93 vhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 832 DDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVThklqyLTHA--------DWIIAMKDG 884
Cdd:cd03233 143 DNSTRGLDSSTALEILK--CIRTMADVLKTTTFVS-----LYQAsdeiydlfDKVLVLYEG 196
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
684-890 |
1.04e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.01 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNN--VNESEPSFEATRSRsrysVAYAAQKP--WLLN 759
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQ----VATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 ATVEENITFGssfnrQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSAL 838
Cdd:PRK13638 93 TDIDSDIAFS-----LRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3273501 839 DIHLSDHLMqeGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREG 890
Cdd:PRK13638 168 DPAGRTQMI--AIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1310-1501 |
1.15e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.23 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1310 IHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVID-GIDISKLPlhtlrsr 1384
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILagelEPDSGEVSIPkGLRIGYLP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 lsiilQDPILFSG-SIRFNL----------------------DPECKCTD-DRLWEALEIA---QLKNMVKSLPGGL--- 1434
Cdd:COG0488 68 -----QEPPLDDDlTVLDTVldgdaelraleaeleeleaklaEPDEDLERlAELQEEFEALggwEAEARAEEILSGLgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1435 ----DATVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT----ENILQK----VVMT----AFADRTVVT 1498
Cdd:COG0488 143 eedlDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNypgtVLVVshdrYFLDRVATR 218
|
...
gi 3273501 1499 IAH 1501
Cdd:COG0488 219 ILE 221
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1030-1278 |
1.29e-07 |
|
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: 54.86 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1030 FYVAGFSILCG------AGIFLcLVTSLTVEWMGLTaaknLHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHI 1103
Cdd:cd18572 40 LLLLLLSVLSGlfsglrGGCFS-YAGTRLVRRLRRD----LFRSLLRQ----DIAFFDATKTGELTSRLTSDCQKVSDPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1104 PPTLESLTRSTLLCLSAIGMISYATP----VFLIALAPLGVAFYFIQKYFRVASKDLQElddstqlpLLCHFSETAE--- 1176
Cdd:cd18572 111 STNLNVFLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQD--------ALAEANQVAEeal 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1177 -GLTTIRAFRHET----RFKQRMLELTDTN---NIAYLFLSAANRWLevrtDYLGACIVLtasiasisgssnsgLVGLGL 1248
Cdd:cd18572 183 sNIRTVRSFATEErearRYERALDKALKLSvrqALAYAGYVAVNTLL----QNGTQVLVL--------------FYGGHL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 3273501 1249 ---------------LYALTITNYLNWVVRNLADLEVQMGAVKKV 1278
Cdd:cd18572 245 vlsgrmsagqlvtfmLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
364-602 |
1.32e-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: 54.86 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 364 TFLQASYYVTIETGI--NLRGALlamiYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLF-LCPNLWAMPVQIIM 440
Cdd:cd07346 56 SYLRRYLAARLGQRVvfDLRRDL----FRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 441 GVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVE 516
Cdd:cd07346 130 ALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 517 ETRMKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVthayaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVK 594
Cdd:cd07346 210 DLRDANLRAARLSALFSPLIGLLTALGTALVLLygGYLV-----LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQ 284
|
....*...
gi 3273501 595 AIISVQKL 602
Cdd:cd07346 285 ALASLERI 292
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1332-1540 |
1.61e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1332 IKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKlplHTLRSR-LSIILQDPILFSG-SIRFNL-- 1403
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmSLGENVgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1404 --------DPECKctdDRLWEALEIAQLKnmvkslpGGLDATVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1475
Cdd:PRK11432 102 glkmlgvpKEERK---QRVKEALELVDLA-------GFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1476 D------MaTENI--LQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNILEYDTPESLLAQEDGVF-ASF 1540
Cdd:PRK11432 168 DanlrrsM-REKIreLQQQF-----NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFmASF 236
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
690-878 |
1.83e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 690 RIPT---GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----YWNNV------NESEPSFEATRS---RSRYSVAYAAQ 753
Cdd:cd03236 19 RLPVpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDEIldefrgSELQNYFTKLLEgdvKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 754 KPWLLNATVEENITfgSSFNRQRYKAVTDACSLQPdidllpfgdqteIGERGI-NLSGGQRQRICVARALYQNTNIVFLD 832
Cdd:cd03236 99 IPKAVKGKVGELLK--KKDERGKLDELVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 3273501 833 DPFSALDIHlsDHLMQEGILKFLQDDKRTVVLVTHKLQYLTH-ADWI 878
Cdd:cd03236 165 EPSSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1064-1278 |
2.19e-07 |
|
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: 54.49 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1064 LHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGM---ISYA-TPVFLIALAPLG 1139
Cdd:cd18557 75 LFSSLLRQ----EIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIIlfiLSWKlTLVLLLVIPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1140 VAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAF----RHETRFKQRMLELTDTNN---IAYLFLSAA 1211
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDaLAKAGQ-----VAEESLSNIRTVRSFsaeeKEIRRYSEALDRSYRLARkkaLANALFQGI 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 1212 NRWLEvrtdYLGACIVLtasiasisgSSNSGLVGLG----------LLYALTITNYLNWVVRNLADLEVQMGAVKKV 1278
Cdd:cd18557 226 TSLLI----YLSLLLVL---------WYGGYLVLSGqltvgeltsfILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
693-867 |
2.27e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 693 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesEPSFEATRSRSRysvayaaqkpwllnatveenitfgssf 772
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG---EDILEEVLDQLL--------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 773 nrqrykavtdacslqpdidllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQE--- 849
Cdd:smart00382 51 -------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
|
170
....*....|....*....
gi 3273501 850 -GILKFLQDDKRTVVLVTH 867
Cdd:smart00382 106 rLLLLLKSEKNLTVILTTN 124
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1310-1529 |
2.38e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1310 IHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI-------------VIDGIDIS 1374
Cdd:PRK10261 15 VENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1375 KLPLHTLR-SRLSIILQDPIL-----------FSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvt 1439
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGasrEEAMVEAKRMLDQVRIPEAQTILSRYPHQL----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1440 eggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVHTIL-TADLVIVMK 1516
Cdd:PRK10261 170 ------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQLIkVLQKEMSMGVIFITHDMGVVAeIADRVLVMY 243
|
250
....*....|...
gi 3273501 1517 RGNILEYDTPESL 1529
Cdd:PRK10261 244 QGEAVETGSVEQI 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1325-1508 |
2.64e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1325 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQD---------- 1391
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDhhllmdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1392 -----PILFSGSirfnldpeckCTDD---RLWEALEIAQLKNMVKSLPGGLdatvtEGGENFSVGqrqlfcLARAFVRKS 1463
Cdd:PRK10908 98 dnvaiPLIIAGA----------SGDDirrRVSAALDKVGLLDKAKNFPIQL-----SGGEQQRVG------IARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 3273501 1464 SILIMDEATASIDMA-TENILQ------KVVMTAF-ADRTVVTIAHRVHTILT 1508
Cdd:PRK10908 157 AVLLADEPTGNLDDAlSEGILRlfeefnRVGVTVLmATHDIGLISRRSYRMLT 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1308-1392 |
2.98e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.08 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKLPLHTL 1381
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSEREL 86
|
90
....*....|....*
gi 3273501 1382 R----SRLSIILQDP 1392
Cdd:COG4172 87 RrirgNRIAMIFQEP 101
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
807-890 |
3.68e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 807 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQ-YLTHADWIiamkdgS 885
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKLReVMAIADRV------T 212
|
....*
gi 3273501 886 VLREG 890
Cdd:COG3845 213 VLRRG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
684-891 |
4.05e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEpsfEATRSRSRYSVAYAAQKPWLLN-ATV 762
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD---WQTAKIMREAVAIVPEGRRVFSrMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 763 EENITFGSSF-NRQRYKAvtdacSLQPDIDLLPFGDQTEIgERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-- 839
Cdd:PRK11614 98 EENLAMGGFFaERDQFQE-----RIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLApi 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 840 --IHLSDHLMQegilkfLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGT 891
Cdd:PRK11614 172 iiQQIFDTIEQ------LREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
684-894 |
6.00e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVYWNNVNESEPSFEATRSRSRYSVAYaaqkPWLlnaT 761
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKQILKRTGFVTQDDILY----PHL---T 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENITFGS------SFNRQRYKAVTDacSLQPDIDLLPFGDqTEIGE---RGInlSGGQRQRICVARALYQNTNIVFLD 832
Cdd:PLN03211 157 VRETLVFCSllrlpkSLTKQEKILVAE--SVISELGLTKCEN-TIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 833 DPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTHA--DWIIAMKDGSVLREGTLKD 894
Cdd:PLN03211 232 EPTSGLDATAAYRLVL--TLGSLAQKGKTIVTSMHQPSSRVYQmfDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
686-867 |
6.04e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.27 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWnnVNESEPSfEATRSRSRYSVAyaaqkPWLLNA----T 761
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL--CGEPVPS-RARHARQRVGVV-----PQFDNLdpdfT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 762 VEENI-TFGssfnrqRYKAVTDACSLQPDIDLLPFGD-----QTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPF 835
Cdd:PRK13537 97 VRENLlVFG------RYFGLSAAAARALVPPLLEFAKlenkaDAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190
....*....|....*....|....*....|..
gi 3273501 836 SALDIHlSDHLMQEGiLKFLQDDKRTVVLVTH 867
Cdd:PRK13537 167 TGLDPQ-ARHLMWER-LRSLLARGKTILLTTH 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
686-895 |
6.84e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.21 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVY-----WNNVNESEPSFEATRSRSRYSVAYAAQKPWL-LN 759
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMaekleFNGQDLQRISEKERRNLVGAEVAMIFQDPMTsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 A--TVEENITF------GSSFNRQRYKAVtDACSLQ--PD----IDLLPFgdqteigergiNLSGGQRQRICVARALYQN 825
Cdd:PRK11022 104 PcyTVGFQIMEaikvhqGGNKKTRRQRAI-DLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 826 TNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQII-ELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
680-907 |
7.34e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.20 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYwnnVNESEPSFEATRSRSRYSVAYAAQKPWLLN 759
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---IDDEDISLLPLHARARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 A-TVEENIT----FGSSFNRQRYKavTDACSLQPDIDLLPFGDQTeigerGINLSGGQRQRICVARALYQNTNIVFLDDP 834
Cdd:PRK10895 92 RlSVYDNLMavlqIRDDLSAEQRE--DRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 835 FSALD-IHLSDhlmQEGILKFLQDDKRTVVLVTHKL-QYLTHADWIIAMKDGSVLREGT----LKDIQTKDVELYEHWK 907
Cdd:PRK10895 165 FAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTpteiLQDEHVKRVYLGEDFR 240
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
699-869 |
7.93e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 52.81 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 699 IVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSR---------YSVayaaqkpwlLNA--TVEENIT 767
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRrmqmvfqdpYAS---------LNPrmTVGDIIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 768 FGSSFN--------RQRYKAVTDACSLQPD-IDLLPFgdqteigErginLSGGQRQRICVARALYQNTNIVFLDDPFSAL 838
Cdd:COG4608 120 EPLRIHglaskaerRERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190
....*....|....*....|....*....|....*
gi 3273501 839 DihLSdhlMQEGILKFLQDDKR----TVVLVTHKL 869
Cdd:COG4608 189 D--VS---IQAQVLNLLEDLQDelglTYLFISHDL 218
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
684-881 |
8.36e-07 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.87 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLL-AILGEMQtlegKVYwnnvNESEPSFEATR----SRSRY------SVAYA- 751
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFdTIYAEGQ----RRY----VESLSAYARQFlgqmDKPDVdsieglSPAIAi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 752 -----AQKPwllNATVEeNITFGSSFNRQRYKAVtdacSLQPDIDLLpfgdqTEIG------ERGIN-LSGGQRQRICVA 819
Cdd:cd03270 83 dqkttSRNP---RSTVG-TVTEIYDYLRLLFARV----GIRERLGFL-----VDVGlgyltlSRSAPtLSGGEAQRIRLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 820 RALYQN-TNIVF-LDDPFSALdiHLSDHLMQEGILKFLQDDKRTVVLVTHKLQYLTHADWIIAM 881
Cdd:cd03270 150 TQIGSGlTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
681-895 |
8.48e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.71 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 681 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL-------GEMQTleGKVYWNNVNE-----SEPSFEATRSRSRYSV 748
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqagGLVQC--DKMLLRRRSRqvielSEQSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 749 AYAAQKPWL-LNAT------VEENITFGSSFNRQRykAVTDACSLqpdIDLLPFGDQTEIGERGIN-LSGGQRQRICVAR 820
Cdd:PRK10261 107 AMIFQEPMTsLNPVftvgeqIAESIRLHQGASREE--AMVEAKRM---LDQVRIPEAQTILSRYPHqLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 821 ALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRT-VVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 895
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMSMgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1322-1531 |
9.64e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1322 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI-SKLPLHTLRSRLSIILQDPILF 1395
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1396 SGSIRFNLDPECKCtdDRLWEALE---IAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1472
Cdd:PRK14271 114 PMSIMDNVLAGVRA--HKLVPRKEfrgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1473 ASIDMATENILQKVVMTaFADR-TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLA 1531
Cdd:PRK14271 192 SALDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1308-1523 |
1.28e-06 |
|
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: 50.74 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV-DIF---DGKIVIDGIDISKLPLHT--- 1380
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTT----IRMIlGIIlpdSGEVLFDGKPLDIAARNRigy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1381 ------LRSRLSIilQDPILFSGSIRfNLDP-ECKCTDDRLWEALEIAQLKNmvKSLpggldatvteggENFSVGQRQLF 1453
Cdd:cd03269 75 lpeergLYPKMKV--IDQLVYLAQLK-GLKKeEARRRIDEWLERLELSEYAN--KRV------------EELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1454 CLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEY 1523
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLY 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1315-1524 |
1.31e-06 |
|
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: 51.18 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1315 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKLPL------HTLRSRLSII 1388
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-------LKILSGLLQPTSGEVRVAGLvpwkrrKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1389 L------------QDPILFSGSIrFNLDP-ECKCTDDRLWEALEIAQLknmvkslpggLDATVteggENFSVGQRQLFCL 1455
Cdd:cd03267 100 FgqktqlwwdlpvIDSFYLLAAI-YDLPPaRFKKRLDELSELLDLEEL----------LDTPV----RQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1456 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNILeYD 1524
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLL-YD 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1334-1534 |
1.63e-06 |
|
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: 52.03 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1334 PGQKV-GICGRTGSGKSSLslafFRMV------DifDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SI 1399
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTL----LRAIaglerpD--SGRIRLGGevlQDSARgifLPPH--RRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1400 RFNLD--------PECKCTDDRLWEALEIAQLknmVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 1471
Cdd:COG4148 95 RGNLLygrkraprAERRISFDEVVELLGIGHL---LDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1472 TASIDMATEN----ILQKVvmtafADRT---VVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQED 1534
Cdd:COG4148 161 LAALDLARKAeilpYLERL-----RDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
809-890 |
1.85e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 809 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TVVLVTHKLQY---LTHAdwIIAMKDG 884
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQKHQlAYLFISHDLHVvraLCHQ--VIVLRQG 502
|
....*.
gi 3273501 885 SVLREG 890
Cdd:PRK15134 503 EVVEQG 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
686-840 |
2.08e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 686 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEPSFEATRSRSRySVAYAAQKPWllnATVEEN 765
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDPY---ASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 766 ITFGSSFNR--------QRYKAVTDACSLQPDIDLLPfgdqtEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFS 836
Cdd:PRK10261 418 QTVGDSIMEplrvhgllPGKAAAARVAWLLERVGLLP-----EHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVS 492
|
....
gi 3273501 837 ALDI 840
Cdd:PRK10261 493 ALDV 496
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1322-1526 |
2.25e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1322 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLP-----LHTlrsrlsiILQDPIL 1394
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVlrLIAGFETPD--SGRIMLDGQDITHVPaenrhVNT-------VFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1395 FSG-SIRFNLDPECKC-------TDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSIL 1466
Cdd:PRK09452 98 FPHmTVFENVAFGLRMqktpaaeITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1467 IMDEATASID------MATE-NILQKVVMTAFadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTP 1526
Cdd:PRK09452 167 LLDESLSALDyklrkqMQNElKALQRKLGITF-----VFVTHDQEEALTmSDRIVVMRDGRIEQDGTP 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
684-895 |
2.77e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.41 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQltmIVGQVG---CGKSSLLLAILGEMQTLEGKVYWNNVNESE-PSFEatrsRSRYSVAYAAQKP---W 756
Cdd:COG1137 19 VKDVSLEVNQGE---IVGLLGpngAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPMHK----RARLGIGYLPQEAsifR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 757 LLnaTVEENI-----TFGSSFNRQRYKAVtdacSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFL 831
Cdd:COG1137 92 KL--TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 832 DDPFSALD-IHLSDhlMQEgILKFLQDdkRTV-VLVT-HK----LQ-----YLthadwiiaMKDGSVLREGTLKDI 895
Cdd:COG1137 161 DEPFAGVDpIAVAD--IQK-IIRHLKE--RGIgVLITdHNvretLGicdraYI--------ISEGKVLAEGTPEEI 223
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
684-1518 |
2.96e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ----TLEGKVYWNNVNESEpsfeaTRSRSRYSVAYAAQK----P 755
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEE-----IKKHYRGDVVYNAETdvhfP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 756 WLlnaTVEENITFGSSFN--RQRYKAVT--DACSLQPDIDLLPFG----DQTEIGE---RGInlSGGQRQRICVARALYQ 824
Cdd:TIGR00956 152 HL---TVGETLDFAARCKtpQNRPDGVSreEYAKHIADVYMATYGlshtRNTKVGNdfvRGV--SGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 825 NTNIVFLDDPFSALD--------------IHLSDHLMQEGILKFLQD-----DKRTVV---------LVTHKLQYL---- 872
Cdd:TIGR00956 227 GAKIQCWDNATRGLDsatalefiralktsANILDTTPLVAIYQCSQDayelfDKVIVLyegyqiyfgPADKAKQYFekmg 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 873 -------THADWIIAMKDGS--VLREGTLKDIQTKDVELYEHWKTLMNRqdQELEKDMEA----DQTTLERKTLRRAMYS 939
Cdd:TIGR00956 307 fkcpdrqTTADFLTSLTSPAerQIKPGYEKKVPRTPQEFETYWRNSPEY--AQLMKEIDEyldrCSESDTKEAYRESHVA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 940 REAKAqmededeeeeEEEDEDDNMSTVMRLrtKMPWKTCWWYLTSGGFFLLFlMIFSKLLKHSVIVAIDYWLATWTSeys 1019
Cdd:TIGR00956 385 KQSKR----------TRPSSPYTVSFSMQV--KYCLARNFLRMKGNPSFTLF-MVFGNIIMALILSSVFYNLPKNTS--- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1020 indpgkadqTFYVAG----FSILCGAgiFLCLVT-SLTVEWMGLTA---AKNLHH---NLLNKIILG-PIRFFDTTPLGL 1087
Cdd:TIGR00956 449 ---------DFYSRGgalfFAILFNA--FSSLLEiASMYEARPIVEkhrKYALYHpsaDAIASIISEiPFKIIESVVFNI 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1088 IL----------NRF------SADTNIIDQHIPPTLESLTRSTLLC--LSAIGMIS------YATPVFLIA--------L 1135
Cdd:TIGR00956 518 ILyfmvnfrrtaGRFffylliLFICTLAMSHLFRSIGAVTKTLSEAmtPAAILLLAlsiytgFAIPRPSMLgwskwiyyV 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1136 APLGVAF-YFIQKYFRVASKDLQEL----DDSTQLPL---LCH------FSETAEGLTTIR-AFRHETRFKQR----MLE 1196
Cdd:TIGR00956 598 NPLAYAFeSLMVNEFHGRRFECSQYvpsgGGYDNLGVtnkVCTvvgaepGQDYVDGDDYLKlSFQYYNSHKWRnfgiIIG 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1197 LTDTNNIAYLFLSAANRWLEVRTDYLgacivltasiasisgssnsglvglgllyaLTITNYLNWVVRNLADLEVQMGAVK 1276
Cdd:TIGR00956 678 FTVFFFFVYILLTEFNKGAKQKGEIL-----------------------------VFRRGSLKRAKKAGETSASNKNDIE 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1277 KVNSF----LTMESENYEGTMDpsqvpEHWPQEGEIKI-HDLC--VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKS 1349
Cdd:TIGR00956 729 AGEVLgstdLTDESDDVNDEKD-----MEKESGEDIFHwRNLTyeVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKT 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1350 SLSLAFFRMVD---IFDGKIVIDGIDISK---------------LPLHTLRSRLSiilqdpilFSGSIRFNLDPECKCTD 1411
Cdd:TIGR00956 804 TLLNVLAERVTtgvITGGDRLVNGRPLDSsfqrsigyvqqqdlhLPTSTVRESLR--------FSAYLRQPKSVSKSEKM 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1412 DRLWEALEIAQLKNMVkslpgglDATVTEGGENFSVGQRQLFCLARAFVRK-SSILIMDEATASIDMATE-NILQKVVMT 1489
Cdd:TIGR00956 876 EYVEEVIKLLEMESYA-------DAVVGVPGEGLNVEQRKRLTIGVELVAKpKLLLFLDEPTSGLDSQTAwSICKLMRKL 948
|
970 980 990
....*....|....*....|....*....|.
gi 3273501 1490 AFADRTVVTIAHRVHTILTA--DLVIVMKRG 1518
Cdd:TIGR00956 949 ADHGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
684-867 |
3.32e-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: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI----LGEMQ-----TLEGKVywnnVNESEpsfeaTRSRSrysvAYAAQK 754
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKgsgsvLLNGMP----IDAKE-----MRAIS----AYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 755 PWLLNA-TVEENITFGSSF----------NRQRYKAVTDACSLQPDIDllpfgdqTEIGERGI--NLSGGQRQRICVARA 821
Cdd:TIGR00955 108 DLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCAN-------TRIGVPGRvkGLSGGERKRLAFASE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3273501 822 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTH 867
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
694-900 |
3.41e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 694 GQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVYWNNVNESEPSfEATRSRSRysvAYAAQK-PWLLNATVEENITF---G 769
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWS-AAELARHR---AYLSQQqTPPFAMPVFQYLTLhqpD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 770 SSFNRQRYKAVTDACSLQPDIDLLPfgdqteigeRGIN-LSGGQRQRICVARALYQ-------NTNIVFLDDPFSALDI- 840
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLG---------RSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVa 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 841 ------HLSDHLMQEGIlkflqddkrTVVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDIQTKDV 900
Cdd:PRK03695 168 qqaaldRLLSELCQQGI---------AVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
808-895 |
5.64e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.84 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 808 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRT----VVLVTHKLQYLTH-ADWIIAMK 882
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLGVVRRfADRVAVMR 231
|
90
....*....|...
gi 3273501 883 DGSVLREGTLKDI 895
Cdd:COG4172 232 QGEIVEQGPTAEL 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
680-884 |
6.41e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesEPSFEATRSRSRYSVAYAAQKPWL-L 758
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFKSSKEALENGISMVHQELNLvL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 NATVEENITFGssfnrqRY--KAV----------TDACSLQPDIDLLPfgdqteiGERGINLSGGQRQRICVARALYQNT 826
Cdd:PRK10982 87 QRSVMDNMWLG------RYptKGMfvdqdkmyrdTKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 827 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTH-ADWIIAMKDG 884
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1318-1526 |
7.24e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1318 ENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIV---IDG-IDISKLP-LHTLRSRLS------ 1386
Cdd:PLN03140 890 EDRLQ-LLREVTGAFRPGVLTALMGVSGAGKTTL-------MDVLAGRKTggyIEGdIRISGFPkKQETFARISgyceqn 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1387 ------IILQDPILFSGSIRfnLDPECKCTD-----DRLWEALEIAQLKNMVKSLPGgldatVTeggeNFSVGQRQLFCL 1455
Cdd:PLN03140 962 dihspqVTVRESLIYSAFLR--LPKEVSKEEkmmfvDEVMELVELDNLKDAIVGLPG-----VT----GLSTEQRKRLTI 1030
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 1456 ARAFVRKSSILIMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVHT-ILTA-DLVIVMKRGNILEYDTP 1526
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSIdIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1332-1487 |
7.53e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.59 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1332 IKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLH-TLRSRLSIILQDPILFSG-SIRFN--LDP 1405
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSVAENifLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1406 ECKCTDDRLWEALEIAQLKNMVKSLPggLDAT-VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 1484
Cdd:TIGR02633 104 EITLPGGRMAYNAMYLRAKNLLRELQ--LDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILL 181
|
...
gi 3273501 1485 KVV 1487
Cdd:TIGR02633 182 DII 184
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
684-891 |
8.96e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.40 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL---------------GEMQTLEG-----KVYwnNVNESEP-----SFE 738
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanrlngaktvpGRYTSIEGlehldKVI--HIDQSPIgrtprSNP 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 739 AT------------------RSR----SRYSV-----AYAA---------QKPWLLNATVEENITFGSSFNRQ----RYK 778
Cdd:TIGR00630 702 ATytgvfdeirelfaetpeaKVRgytpGRFSFnvkggRCEAcqgdgvikiEMHFLPDVYVPCEVCKGKRYNREtlevKYK 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 779 AVTDACSLQ-------------PDID-----LLPFGDQ-TEIGERGINLSGGQRQRICVARALYQNTN---IVFLDDPFS 836
Cdd:TIGR00630 782 GKNIADVLDmtveeayeffeavPSISrklqtLCDVGLGyIRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTT 861
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 837 ALdiHLSD--HLMQegILKFLQDDKRTVVLVTHKLQYLTHADWII------AMKDGSVLREGT 891
Cdd:TIGR00630 862 GL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTVVASGT 920
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
806-879 |
9.22e-06 |
|
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: 47.95 E-value: 9.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 806 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQeGILKFLQDDKRTVVLVTHKLQYLTH-ADWII 879
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR-AIRRLSEEGKKTALVVEHDLAVLDYlSDRIH 143
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1306-1521 |
1.29e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.88 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1306 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRs 1383
Cdd:PLN03211 67 HKPKISDETRQIQE--RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1384 RLSIILQDPILFSG-SIRFNLdpeCKCTDDRLWEALEIAQLKNMVKSLPGGLDATVTEG---GENF----SVGQRQLFCL 1455
Cdd:PLN03211 141 RTGFVTQDDILYPHlTVRETL---VFCSLLRLPKSLTKQEKILVAESVISELGLTKCENtiiGNSFirgiSGGERKRVSI 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 1456 ARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILtaDLVIVMKRGNIL 1521
Cdd:PLN03211 218 AHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCL 286
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
605-869 |
2.05e-05 |
|
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: 49.63 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 605 FLLSdeigEDSWRTGEGTlpfeSCKKHTGVQ-SKPINRKQPGRYHLDNYEQA--RRLRPAETEDVAIKVTNGYFSwGSGL 681
Cdd:TIGR01257 873 FLLQ----ESYWLGGEGC----STREERALEkTEPLTEEMEDPEHPEGINDSffERELPGLVPGVCVKNLVKIFE-PSGR 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 682 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvNESEPSFEATRSrsrySVAYAAQKPWLLN-A 760
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-KDIETNLDAVRQ----SLGMCPQHNILFHhL 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 761 TVEENITFGSSFNRQRYkavtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 840
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
250 260
....*....|....*....|....*....
gi 3273501 841 HlSDHLMQEGILKFlqDDKRTVVLVTHKL 869
Cdd:TIGR01257 1095 Y-SRRSIWDLLLKY--RSGRTIIMSTHHM 1120
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
803-895 |
2.20e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.24 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 803 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPfsALDIHLSDHLMQEGILKFLQDDKRTVVLVTHKLQYLTHADWII 879
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEP--SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|..
gi 3273501 880 AM------KDGSVLREGTLKDI 895
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEI 582
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1035-1218 |
2.29e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 47.86 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1035 FSILCGAGIFLCLVTSL---TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 1111
Cdd:cd18575 39 FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1112 RSTLLCLSAIGMISYATP---VFLIALAPLGVA-FYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRH 1186
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQDrLADLSA-----FAEETLSAIKTVQAFTR 193
|
170 180 190
....*....|....*....|....*....|..
gi 3273501 1187 ETRFKQRMLELTDTNniaylfLSAANRWLEVR 1218
Cdd:cd18575 194 EDAERQRFATAVEAA------FAAALRRIRAR 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
699-878 |
2.56e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 699 IVGQVGCGKSSLLLAILGEMQTLEGkvywnnvnesepsfEATRSRSrYSVAYAAQKPWL-LNATVEENIT--FGSSFN-R 774
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG--------------EARPAPG-IKVGYLPQEPQLdPEKTVRENVEegVAEVKAaL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 775 QRYKAVTDACS---------------LQPDIDL------------------LPFGDqTEIGergiNLSGGQRQRICVARA 821
Cdd:PRK11819 103 DRFNEIYAAYAepdadfdalaaeqgeLQEIIDAadawdldsqleiamdalrCPPWD-AKVT----KLSGGERRRVALCRL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3273501 822 LYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTVVLVTHKLQYLTH-ADWI 878
Cdd:PRK11819 178 LLEKPDMLLLDEP--------TNHLDAESVAwleQFLHDYPGTVVAVTHDRYFLDNvAGWI 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1332-1527 |
2.98e-05 |
|
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: 47.34 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1332 IKPGQKVGICGRTGSGKSSLslafFRMV------DifDGKIVIDGIDISKLPLHtLRSRLSII--LQDPILFSG------ 1397
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTL----FNLItgfyrpT--SGRILFDGRDITGLPPH-RIARLGIArtFQNPRLFPEltvlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1398 --------------SIRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFV 1460
Cdd:COG0411 100 vlvaaharlgrgllAALLRLPRarrEEREARERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1461 RKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPE 1527
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEeTEELAELIRrLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1284-1502 |
3.48e-05 |
|
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: 48.59 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1284 MESENYEGTMDP--------SQVPEHWPQEGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKS 1349
Cdd:TIGR00954 413 VKSGNFKRPRVEeiesgregGRNSNLVPGRGIVEYQDNGIKFENiplvtpNGDVLIESLSFEVPSGNNLLICGPNGCGKS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1350 SLslafFRMVD----IFDGKIVIDG----IDISKLPLHTLRSrlsiiLQDPILFSGSIrfnLDPECK-CTDDRLWEALEI 1420
Cdd:TIGR00954 493 SL----FRILGelwpVYGGRLTKPAkgklFYVPQRPYMTLGT-----LRDQIIYPDSS---EDMKRRgLSDKDLEQILDN 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1421 AQLKNMVKSlPGGLDAtVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA--SIDM--ATENILQKVVMTAFadrtv 1496
Cdd:TIGR00954 561 VQLTHILER-EGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSavSVDVegYMYRLCREFGITLF----- 633
|
....*.
gi 3273501 1497 vTIAHR 1502
Cdd:TIGR00954 634 -SVSHR 638
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
796-943 |
3.61e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 796 GDQ-TEIGERginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQ-----EGILKFLQDDKRTVVLVTHKL 869
Cdd:PRK10636 421 GDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEalidfEGALVVVSHDRHLLRSTTDDL 497
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 870 qYLTHadwiiamkDGSVlregtlkDIQTKDVELYEHWktLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAK 943
Cdd:PRK10636 498 -YLVH--------DGKV-------EPFDGDLEDYQQW--LSDVQKQENQTDEAPKENNANSAQARKDQKRREAE 553
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1308-1524 |
4.83e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.75 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVI-DGIDISKLPlhtlr 1382
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLlageLEPDSGTVKLgETVKIGYFD----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1383 srlsiilQDpilfsgsiRFNLDPeckctDDRLWEalEIAQLKnmvkslPGGLDATVTE-------GGE-------NFSVG 1448
Cdd:COG0488 385 -------QH--------QEELDP-----DKTVLD--ELRDGA------PGGTEQEVRGylgrflfSGDdafkpvgVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1449 QRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTaFaDRTVVTIAH------RVhtiltADLVIVMKRGNILE 1522
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-F-PGTVLLVSHdryfldRV-----ATRILEFEDGGVRE 509
|
..
gi 3273501 1523 YD 1524
Cdd:COG0488 510 YP 511
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1308-1524 |
4.94e-05 |
|
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: 46.37 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLKP--------------------VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 1367
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1368 IDGIDISKLPLHT-LRSRLSIIlqDPILFSGSIrFNLDPecKCTDDRLWEALEIAQLKNMvkslpggLDATVteggENFS 1446
Cdd:cd03220 81 VRGRVSSLLGLGGgFNPELTGR--ENIYLNGRL-LGLSR--KEIDEKIDEIIEFSELGDF-------IDLPV----KTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1447 VGQ--RQLFCLARAFvrKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILE 1522
Cdd:cd03220 145 SGMkaRLAFAIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKrLCDRALVLEKGKIRF 222
|
..
gi 3273501 1523 YD 1524
Cdd:cd03220 223 DG 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1313-1478 |
5.19e-05 |
|
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: 45.81 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1313 LCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP 1392
Cdd:TIGR01189 7 ACSRGE---RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1393 ILFSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIMD 1469
Cdd:TIGR01189 84 LKPELSALENLHfwaAIHGGAQRTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 3273501 1470 EATASIDMA 1478
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
986-1206 |
6.25e-05 |
|
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: 46.61 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 986 GFFLLFLMIFSKLLKHSVI-VAIDywlatwtsEYSINDPGKADQTFYVAGFSILCGAGIFLCL-VTSLTVEWMGLTAAKN 1063
Cdd:cd18544 4 ALLLLLLATALELLGPLLIkRAID--------DYIVPGQGDLQGLLLLALLYLGLLLLSFLLQyLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1064 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISY----ATPVFLIALAPLG 1139
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLlnwrLALISLLVLPLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1140 VAFYFIQKYFRVASKDLQEL--DDSTQLpllchfSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYL 1206
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKlsRLNAFL------QESISGMSVIQLFNREKREFEEFDEINQEYRKANL 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
809-890 |
6.54e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 809 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRT----VVLVTHKL---QYLTHAdwIIAM 881
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225
|
....*....
gi 3273501 882 KDGSVLREG 890
Cdd:PRK11701 226 KQGRVVESG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1332-1533 |
7.63e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1332 IKPGQKVGICGRTGSGKSSLSLAFFRMVD-IFDGKIVIDG--IDIsKLPLHTLRSRLSIILQD-------PIL------- 1394
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDI-RNPAQAIRAGIAMVPEDrkrhgivPILgvgknit 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1395 ------FSGSIRFNLDPECKCTDdrlwEALEIAQLKNMVKSLP-GGLdatvteggenfSVGQRQLFCLARAFVRKSSILI 1467
Cdd:TIGR02633 362 lsvlksFCFKMRIDAAAELQIIG----SAIQRLKVKTASPFLPiGRL-----------SGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3273501 1468 MDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNiLEYDTPESLLAQE 1533
Cdd:TIGR02633 427 LDEPTRGVDVgAKYEIYKLINQLAQEGVAIIVVSSELAEVLgLSDRVLVIGEGK-LKGDFVNHALTQE 493
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1334-1513 |
8.17e-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: 44.29 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1334 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIdgIDISKLPLHTLRSRLSIILQDPILFSGSIRfnldpeckctddr 1413
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGEL------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1414 lwealeiaqlknmvkslpggldatvteggenfsvGQRQLFclARAFVRKSSILIMDEATASIDMATENILQKVVMTAF-- 1491
Cdd:smart00382 66 ----------------------------------RLRLAL--ALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180
....*....|....*....|....*..
gi 3273501 1492 -----ADRTVVTIAHRVHTILTADLVI 1513
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1064-1193 |
8.32e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 46.47 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1064 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG---MISYA-TPVFLIALAPLG 1139
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVfmfTTSWKlTLVMLSVVPPLS 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1140 VAFYFIQKYFRVASKDLQ-ELDDStqlpllchfSETAE----GLTTIRAFRHETRFKQR 1193
Cdd:cd18780 157 IGAVIYGKYVRKLSKKFQdALAAA---------STVAEesisNIRTVRSFAKETKEVSR 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1322-1476 |
8.57e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 46.75 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1322 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIILQdpilFSgsirf 1401
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FD----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1402 NLDPECKCTDD------------RLWEA-----LEIAQLKNMVkslpgglDATVTEggenFSVGQRQLFCLARAFVRKSS 1464
Cdd:PRK13536 124 NLDLEFTVRENllvfgryfgmstREIEAvipslLEFARLESKA-------DARVSD----LSGGMKRRLTLARALINDPQ 192
|
170
....*....|..
gi 3273501 1465 ILIMDEATASID 1476
Cdd:PRK13536 193 LLILDEPTTGLD 204
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1056-1199 |
1.14e-04 |
|
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: 45.89 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1056 MGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADT----NIIDQHIPptlESLTRSTLLCLSAIGMISYATPVF 1131
Cdd:cd18551 63 TGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELITSGLP---QLVTGVLTVVGAVVLMFLLDWVLT 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1132 LIALAPLGVAF---YFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTD 1199
Cdd:cd18551 140 LVTLAVVPLAFliiLPLGRRIRKASKRAQDaLGELSA-----ALERALSAIRTVKASNAEERETKRGGEAAE 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
684-890 |
1.75e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.56 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK----VYWNNVNESEPSFEATrsrsrYSVAYAAQKPWLLN 759
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAgcvdVPDNQFGREASLIDAI-----GRKGDFKDAVELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 760 AT-VEENITFgssfnRQRYKavtdacslqpdidllpfgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 838
Cdd:COG2401 121 AVgLSDAVLW-----LRRFK----------------------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 3273501 839 DIHLSdHLMQEGILKFLQDDKRTVVLVTHklqyltHADWIIAMKDGSVLREG 890
Cdd:COG2401 168 DRQTA-KRVARNLQKLARRAGITLVVATH------HYDVIDDLQPDLLIFVG 212
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1055-1197 |
1.82e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 45.17 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1055 WMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VF 1131
Cdd:cd18576 62 RVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3273501 1132 LIALAP-LGVAFYFIQKYFRVASKDLQ-ELDDSTQlpllcHFSETAEGLTTIRAFRHE----TRFKQRMLEL 1197
Cdd:cd18576 142 MLATVPvVVLVAVLFGRRIRKLSKKVQdELAEANT-----IVEETLQGIRVVKAFTREdyeiERYRKALERV 208
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1332-1522 |
1.98e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1332 IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIV-----IDGIDISKLPLHTLR----SRLSIILQDPILfsgsirfN 1402
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISEKERRnlvgAEVAMIFQDPMT-------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1403 LDPeCKCTDDRLWEALEIAQlknmvkslpGGLDAT--------VTEGG------------ENFSVGQRQLFCLARAFVRK 1462
Cdd:PRK11022 102 LNP-CYTVGFQIMEAIKVHQ---------GGNKKTrrqraidlLNQVGipdpasrldvypHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1463 SSILIMDEATASIDMATE--------NILQKVVMtafadrTVVTIAHRVHTIL-TADLVIVMKRGNILE 1522
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQaqiielllELQQKENM------ALVLITHDLALVAeAAHKIIVMYAGQVVE 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
684-839 |
1.99e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 684 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVNESEpsfeatrsrsrysvayaAQKPWL------ 757
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-----------------IAKPYCtyighn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 758 ----LNATVEENITFGSSFnrqrYKAVTdacSLQPDIDLLPFGDQteIGERGINLSGGQRQRICVARALYQNTNIVFLDD 833
Cdd:PRK13541 79 lglkLEMTVFENLKFWSEI----YNSAE---TLYAAIHYFKLHDL--LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
....*.
gi 3273501 834 PFSALD 839
Cdd:PRK13541 150 VETNLS 155
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1434-1518 |
2.82e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1434 LDATVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI-DMATENILQkvVMTAFAD--RTVVTIAHRVHTILT-A 1509
Cdd:COG3845 135 PDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE--ILRRLAAegKSIIFITHKLREVMAiA 208
|
....*....
gi 3273501 1510 DLVIVMKRG 1518
Cdd:COG3845 209 DRVTVLRRG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1313-1526 |
3.52e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.39 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1313 LCVR-----YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSI 1387
Cdd:TIGR01257 929 VCVKnlvkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQDPILF-----SGSIRFNLDpeckcTDDRLWEALEIaQLKNMVKSLpgGLDATVTEGGENFSVGQRQLFCLARAFVRK 1462
Cdd:TIGR01257 1008 CPQHNILFhhltvAEHILFYAQ-----LKGRSWEEAQL-EMEAMLEDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3273501 1463 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTP 1526
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1308-1476 |
5.97e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.64 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1387
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1388 ILQdpilFSgsirfNLDPECKCTDDRL----WEALEIAQLKNMVKSL------PGGLDATVTEggenFSVGQRQLFCLAR 1457
Cdd:PRK13537 85 VPQ----FD-----NLDPDFTVRENLLvfgrYFGLSAAAARALVPPLlefaklENKADAKVGE----LSGGMKRRLTLAR 151
|
170
....*....|....*....
gi 3273501 1458 AFVRKSSILIMDEATASID 1476
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLD 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
807-869 |
6.00e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 6.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 807 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlSDHLMQEGILKFLQDDKRTVVLVTHKL 869
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
808-884 |
6.17e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 808 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TVVLVTHKLQYLTH-ADWIIAMK 882
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 3273501 883 DG 884
Cdd:PRK15134 232 NG 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
694-867 |
6.93e-04 |
|
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: 43.17 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 694 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNVnesepsfeatrsrsrySVAYaaqKPWLLNA----TVEEnitfg 769
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD----------------TVSY---KPQYIKAdyegTVRD----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 770 ssFNRQRYKAVTDACSLQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsDHLMQE 849
Cdd:cd03237 81 --LLSSITKDFYTHPYFKTEI-AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRLMAS 155
|
170
....*....|....*....
gi 3273501 850 GILK-FLQDDKRTVVLVTH 867
Cdd:cd03237 156 KVIRrFAENNEKTAFVVEH 174
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1334-1477 |
7.60e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.71 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1334 PGQKV-GICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SIRFNLDP 1405
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPE--KRRIGYVFQDARLFPHyKVRGNLRY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1406 ECKCTD----DRLWEALEIAQLknmVKSLPGGLdatvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDM 1477
Cdd:PRK11144 100 GMAKSMvaqfDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
809-895 |
8.68e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.17 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 809 SGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TVVLVTHKLQYLTH-ADWIIAMKD 883
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDLGVVAGiCDKVLVMYA 237
|
90
....*....|..
gi 3273501 884 GSVLREGTLKDI 895
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
680-896 |
9.79e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 680 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVYWNNvneSEPSFEATRSRSRYSVAYAAQKPWLL- 758
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSQEAGIGIIHQELNLIp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 759 NATVEENITFG----SSFNRQRYKAVTDacslQPDIDL----LPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVF 830
Cdd:PRK10762 93 QLTIAENIFLGrefvNRFGRIDWKKMYA----EADKLLarlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3273501 831 LDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYL-THADWIIAMKDGSVLREGTLKDIQ 896
Cdd:PRK10762 165 MDEPTDALTDTETESLFR--VIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADLT 229
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
801-904 |
1.28e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 801 IGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTVVLVTHK--LQYLTHADW 877
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT--VRNTVDTGRTVVCTIHQpsIDIFEAFDE 1089
|
90 100
....*....|....*....|....*...
gi 3273501 878 IIAMK-DGSVLREGTLKDIQTKDVELYE 904
Cdd:PLN03140 1090 LLLMKrGGQVIYSGPLGRNSHKIIEYFE 1117
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
803-936 |
1.29e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 803 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPFSALDIHLSDHLMQegILKFLQDDKRTVVLVTHKLQYLTHADWII 879
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLgAELIGITYiLDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3273501 880 ------AMKDGSVLREGTLKDIQTKDVELYEHWKtlmnRQDQELEKDmEADQTTLERKTLRRA 936
Cdd:PRK00635 549 digpgaGIFGGEVLFNGSPREFLAKSDSLTAKYL----RQELTIPIP-EKRTNSLGTLTLSKA 606
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
808-895 |
1.83e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.08 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 808 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TVVLVTHKLQYLTH-ADWIIAMK 882
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqliNLMLE-----LQEKQGiSYIYVTQHLGMMKHiSDQVLVMH 224
|
90
....*....|...
gi 3273501 883 DGSVLREGTLKDI 895
Cdd:PRK15112 225 QGEVVERGSTADV 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1335-1492 |
1.85e-03 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 41.32 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1335 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDR 1413
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHAdHSDEQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 1414 LWEALEIAQLkNMVKSLPGGldatvteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILqkvvMTAFA 1492
Cdd:cd03231 106 VEEALARVGL-NGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF----AEAMA 169
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
801-912 |
1.89e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 801 IGERGINLSGGQRQRICVARALY---QNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTVVLVTHKLQYLTHADW 877
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQ--LRTLVSLGHSVIYIDHDPALLKQADY 1770
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 3273501 878 IIAM------KDGSVLREGTLKDIQ-TKDVELyehwKTLMNR 912
Cdd:PRK00635 1771 LIEMgpgsgkTGGKILFSGPPKDISaSKDSLL----KTYMCN 1808
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
649-854 |
2.20e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.61 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 649 LDNYEQARRLRPAETE--------DVAIKVTNGYFSWGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT 720
Cdd:TIGR03719 296 LLSQEFQKRNETAEIYippgprlgDKVIEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 721 LEGKVywnNVNESepsfeatrsrsrYSVAYAAQKPWLL--NATVEENITFG-----------------SSFNrqrYKAvt 781
Cdd:TIGR03719 375 DSGTI---EIGET------------VKLAYVDQSRDALdpNKTVWEEISGGldiiklgkreipsrayvGRFN---FKG-- 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 782 dacslqpdidllpfGDQTE-IGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKF 854
Cdd:TIGR03719 435 --------------SDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL-EEALLNF 489
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
808-882 |
3.02e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 3.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3273501 808 LSGGQRQRICVARAL----YQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLqDDKRTVVLVTHKLQYLTHADWIIAMK 882
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAILEHL-VKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1067-1229 |
3.27e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 41.14 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1067 NLLNK-IILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTllcLSAIGMI------SYATPVFLIALAPL- 1138
Cdd:cd18784 73 NLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSL---VKAIGVIvfmfklSWQLSLVTLIGLPLi 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1139 -GVAFYFiQKYFRVASKDLQeldDStqlplLCHFSETAE----GLTTIRAFRHET----RFK---QRMLELTDTNNIAYL 1206
Cdd:cd18784 150 aIVSKVY-GDYYKKLSKAVQ---DS-----LAKANEVAEetisSIRTVRSFANEDgeanRYSeklKDTYKLKIKEALAYG 220
|
170 180
....*....|....*....|....*..
gi 3273501 1207 FLSAANRWLE----VRTDYLGACIVLT 1229
Cdd:cd18784 221 GYVWSNELTElaltVSTLYYGGHLVIT 247
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
809-872 |
4.07e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 4.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3273501 809 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFlqddKRTVVLVTHKLQYL 872
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKW----PKTFIVVSHAREFL 404
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1069-1193 |
4.37e-03 |
|
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: 40.89 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1069 LNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIPPTLESLTRSTLLCL-SAIGMISYATPVFLIALAPL---GVAFYF 1144
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIiSGIILFFYNWKLFLITLLIIplyILIILL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 3273501 1145 IQKYFRVASKDLQELDDSTQlpllCHFSETAEGLTTIRAFRHETRFKQR 1193
Cdd:cd18570 161 FNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKK 205
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
806-900 |
5.02e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 806 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTVVLVTHKLQYLTHADWIIAMKDGs 885
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNG- 525
|
90
....*....|....*..
gi 3273501 886 VLRE--GTLKDIQTKDV 900
Cdd:PRK10522 526 QLSEltGEERDAASRDA 542
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1308-1522 |
5.59e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1308 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSR 1384
Cdd:PRK09580 2 LSIKDLHVSVEDK--AILRGLNLEVRPGEVHAIMGPNGSGKSTLSatLAGREDYEVTGGTVEFKGKDLLELsPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1385 LSIILQDPILFSG-SIRFNLDPECKCTDD-RLWEAL----------EIAQLKNMVKSLpggLDATVTEGgenFSVGQRQL 1452
Cdd:PRK09580 80 IFMAFQYPVEIPGvSNQFFLQTALNAVRSyRGQEPLdrfdfqdlmeEKIALLKMPEDL---LTRSVNVG---FSGGEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3273501 1453 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMT------AFadrTVVTIAHRVHTILTADLVIVMKRGNILE 1522
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSlrdgkrSF---IIVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
799-840 |
6.68e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 6.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 3273501 799 TEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 840
Cdd:PRK13409 203 ENILDRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1033-1198 |
7.46e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 40.14 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1033 AGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSAdTNIIDQHIPPTL-ESLT 1111
Cdd:cd18567 46 IGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFvEALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1112 RSTLLCLSAIGMISYATPVFLIALAplGVAFYFI-----QKYFRVASKDLQELD---DStqlpllcHFSETAEGLTTIRA 1183
Cdd:cd18567 125 DGLMAILTLVMMFLYSPKLALIVLA--AVALYALlrlalYPPLRRATEEQIVASakeQS-------HFLETIRGIQTIKL 195
|
170
....*....|....*
gi 3273501 1184 FRHETRFKQRMLELT 1198
Cdd:cd18567 196 FGREAEREARWLNLL 210
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1340-1501 |
8.87e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1340 ICGRTGSGKSSLslaffrmvdifdgkivIDGIDISKLPLHTLRSRLSIILQDPIlFSGSIRFNLDPECKCTDDRLWEAL- 1418
Cdd:cd03240 27 IVGQNGAGKTTI----------------IEALKYALTGELPPNSKGGAHDPKLI-REGEVRAQVKLAFENANGKKYTITr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3273501 1419 EIAQLKNMVKSLPGGLDATVTEGGENFSVGQRQLFC------LARAFVRKSSILIMDEATASIDmaTENILQKVV----- 1487
Cdd:cd03240 90 SLAILENVIFCHQGESNWPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLD--EENIEESLAeiiee 167
|
170
....*....|....
gi 3273501 1488 MTAFADRTVVTIAH 1501
Cdd:cd03240 168 RKSQKNFQLIVITH 181
|
|
| |
