|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
222-1546 |
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: 881.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 222 LLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHP---------------------- 279
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPvsavygkkdpskpkgssqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 280 -------------NRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTnnttgisetlsske 346
Cdd:TIGR00957 289 eevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPD-------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 347 flENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMW 426
Cdd:TIGR00957 355 --WQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 427 FLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK 506
Cdd:TIGR00957 431 LATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 507 LYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAE-AFASLSLFHILVTPL 585
Cdd:TIGR00957 511 LYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEkAFVSLALFNILRFPL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 586 FLLSTVVRFAVKAIISVQKLNEFLLSDEIgddswrtgesslpfesckkhtgvQPKTINRkqpgryhldsyeqstRRLRPA 665
Cdd:TIGR00957 591 NILPMVISSIVQASVSLKRLRIFLSHEEL-----------------------EPDSIER---------------RTIKPG 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 666 ETEDIAIKvtNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfeat 744
Cdd:TIGR00957 633 EGNSITVH--NATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 745 rsrnrySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVAR 824
Cdd:TIGR00957 700 ------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLAR 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 825 ALYQNTNIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpEGVLK-----NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 900 QTKDVELYEHWKTLMNRQDQElekDMEADQTTL------ERKTLRRAMY-----SREAKAQMEDEDEEEEEEEDEDDNMS 968
Cdd:TIGR00957 849 LQRDGAFAEFLRTYAPDEQQG---HLEDSWTALvsgegkEAKLIENGMLvtdvvGKQLQRQLSASSSDSGDQSRHHGSSA 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 969 TVMRLRTKMP-WKTC---------------WRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTgKADQ 1032
Cdd:TIGR00957 926 ELQKAEAKEEtWKLMeadkaqtgqvelsvyWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGT-QNNT 1004
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1033 TYYV---AGFSILCGAGIFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPP 1109
Cdd:TIGR00957 1005 SLRLsvyGALGILQGFAVFG---YSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPP 1081
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1110 TLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFR 1189
Cdd:TIGR00957 1082 VIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE 1161
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1190 HETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVR 1267
Cdd:TIGR00957 1162 EQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLfaALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVR 1241
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1268 NLADLEVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGR 1347
Cdd:TIGR00957 1242 MSSEMETNIVAVERLKEYSETEKEA-PWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGR 1320
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1348 TGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQL 1427
Cdd:TIGR00957 1321 TGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHL 1400
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1428 KNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRV 1507
Cdd:TIGR00957 1401 KTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1480
|
1370 1380 1390
....*....|....*....|....*....|....*....
gi 110832837 1508 HTILTADLVIVMKRGNILEYDTPESLLAQEnGVFASFVR 1546
Cdd:TIGR00957 1481 NTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
220-1547 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 765.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 220 VNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKvadhpnrtPSIWL--AMYRAFGRPI 297
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK--------PKPWLlrALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 298 LLSSTFRYLADLLGFAGPLCISGIVQRVnetQNGTNNTTGISETLSskeflenayvlavllflalilqrTFLQASYYVTI 377
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPLLLNLLLESM---QNGEPAWIGYIYAFS-----------------------IFVGVVLGVLC 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 378 E---------TGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILL 448
Cdd:PLN03130 358 EaqyfqnvmrVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 449 YNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSS 528
Cdd:PLN03130 436 YQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSW 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 529 LKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEF 608
Cdd:PLN03130 516 FRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGD-LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEEL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 609 LLSDEigddswRTGESSLPFESCkkhtgvqpktinrkQPgryhldsyeqstrrlrpaetediAIKVTNGYFSWGSGL--A 686
Cdd:PLN03130 595 LLAEE------RVLLPNPPLEPG--------------LP-----------------------AISIKNGYFSWDSKAerP 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqtlegkvhwsnvnesePSFEATRSRNRYSVAYAAQKPWLLNATV 766
Cdd:PLN03130 632 TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL----------------PPRSDASVVIRGTVAYVPQVSWIFNATV 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 846
Cdd:PLN03130 696 RDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 847 SDHLMQEGILKFLQddKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLMNR---------- 916
Cdd:PLN03130 776 GRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL-SNNGPLF---QKLMENagkmeeyvee 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 917 -----QDQELEKDMEADQTTLERKTLRRAMYSREAKAQMededeeeeeeededdnMSTVMRLRTKMPWKTCWRYLTS-GG 990
Cdd:PLN03130 850 ngeeeDDQTSSKPVANGNANNLKKDSSSKKKSKEGKSVL----------------IKQEERETGVVSWKVLERYKNAlGG 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 991 FFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKAdqtYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 1070
Cdd:PLN03130 914 AWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKTHGPL---FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHD 990
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1071 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 1150
Cdd:PLN03130 991 AMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAY 1070
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1151 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHetrfKQRMLELTDT---NNIAYLFLS-AANRWLEVRTDYL 1226
Cdd:PLN03130 1071 LYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKA----YDRMAEINGRsmdNNIRFTLVNmSSNRWLAIRLETL 1146
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1227 GACIV-LTASIA------SISGSSNSGLVGLGLLYALTITNYLNWVVRnLADL-EVQMGAVKKVNSFLTMESENyEGTMD 1298
Cdd:PLN03130 1147 GGLMIwLTASFAvmqngrAENQAAFASTMGLLLSYALNITSLLTAVLR-LASLaENSLNAVERVGTYIDLPSEA-PLVIE 1224
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1299 PSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS 1378
Cdd:PLN03130 1225 NNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS 1304
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1379 KLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFC 1458
Cdd:PLN03130 1305 KFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLS 1384
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1538
Cdd:PLN03130 1385 LARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
....*....
gi 110832837 1539 GVFASFVRA 1547
Cdd:PLN03130 1465 SAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
221-1547 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 734.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 221 NLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQkkkvadhpNRTPSIWL--AMYRAFGRPIL 298
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE--------SRRPKPWLlrALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 299 LSSTFRYLADLLGFAGPLCISGIVQRVNEtqngtNNTTGISETLSSKEFLENAYVlavllflalilqrTFLQASYYVTI- 377
Cdd:PLN03232 305 LGGIFKIGHDLSQFVGPVILSHLLQSMQE-----GDPAWVGYVYAFLIFFGVTFG-------------VLCESQYFQNVg 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 378 ETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSAL 457
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 458 VGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 537
Cdd:PLN03232 445 FGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 538 LSIFMNAAIPIAAVLATFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEigdd 617
Cdd:PLN03232 525 FNSFILNSIPVVVTLVSFGVFVLLGGD-LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEE---- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 618 swRTGESSLPFesckkhtgvqpktinrkQPGRyhldsyeqstrrlrPAetediaIKVTNGYFSWGSGLA--TLSNIDIRI 695
Cdd:PLN03232 600 --RILAQNPPL-----------------QPGA--------------PA------ISIKNGYFSWDSKTSkpTLSDINLEI 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 696 PTGQLTMIVGQVGCGKSSLLLAILGEMqtlegkvhwsnvnesePSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSP 775
Cdd:PLN03232 641 PVGSLVAIVGGTGEGKTSLISAMLGEL----------------SHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSD 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 776 FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGI 855
Cdd:PLN03232 705 FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCM 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 856 LKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVELYehwKTLM------------NRQDQELEK 923
Cdd:PLN03232 785 KDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLF---KKLMenagkmdatqevNTNDENILK 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 924 DMEADQTTLERKTLRRAMYSREAKAQMEDEDEeeeeeededdnmstvmRLRTKMPWKTCWRYLTS-GGFFLLILMIFSKL 1002
Cdd:PLN03232 859 LGPTVTIDVSERNLGSTKQGKRGRSVLVKQEE----------------RETGIISWNVLMRYNKAvGGLWVVMILLVCYL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1003 LKHSVIVAIDYWLATWTSEYSINNTGKAdqtYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIR 1082
Cdd:PLN03232 923 TTEVLRVSSSTWLSIWTDQSTPKSYSPG---FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPML 999
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1083 FFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQE 1162
Cdd:PLN03232 1000 FFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRR 1079
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1163 LDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDtNNIAY-LFLSAANRWLEVRTDYLGACIV-LTASIASIS 1240
Cdd:PLN03232 1080 LDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMD-NNIRFtLANTSSNRWLTIRLETLGGVMIwLTATFAVLR 1158
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1241 GSSNSGLVG----LGLL--YALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENyEGTMDPSQVPEHWPQEGEIKI 1314
Cdd:PLN03232 1159 NGNAENQAGfastMGLLlsYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEA-TAIIENNRPVSGWPSRGSIKF 1237
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1315 HDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQ 1394
Cdd:PLN03232 1238 EDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ 1317
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1395 DPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 1474
Cdd:PLN03232 1318 SPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1475 ATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRA 1547
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
365-1547 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 665.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 365 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 444
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 445 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 524
Cdd:PTZ00243 378 ILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRAR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 525 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQK 604
Cdd:PTZ00243 458 ELRYLRDVQLARVATSFVNNATPTLMIAVVFTVY-YLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 605 LNEFLLSDE-----IGD--DSWRTGESS----------------------LPF------------------ESCKKHTGV 637
Cdd:PTZ00243 537 ISTFLECDNatcstVQDmeEYWREQREHstacqlaavlenvdvtafvpvkLPRapkvktsllsralrmlccEQCRPTKRH 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 638 QPKTI---------------NRKQPGRYHLDSyEQSTrrlrPAETEDIAIKVTNGYFSWGSGLaTLSNIDIRIPTGQLTM 702
Cdd:PTZ00243 617 PSPSVvvedtdygspssasrHIVEGGTGGGHE-ATPT----SERSAKTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTV 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 703 IVGQVGCGKSSLLLAILGEMQTLEGKVhWsnvnesepsfeATRSrnrysVAYAAQKPWLLNATVEENITFGSPFNKQRYK 782
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRV-W-----------AERS-----IAYVPQQAWIMNATVRGNILFFDEEDAARLA 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 783 AVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDd 862
Cdd:PTZ00243 754 DAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAG- 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 863 kRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKD-IQTkdvELYEHWKT-LMNRQDQElEKDMEADQTTLER-KTLRR 939
Cdd:PTZ00243 833 -KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADfMRT---SLYATLAAeLKENKDSK-EGDADAEVAEVDAaPGGAV 907
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 940 AMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKM-PWKTCWRYLTS-GGFFLLILMIFSKLLKHSVIVAIDYWLAT 1017
Cdd:PTZ00243 908 DHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSvPWSTYVAYLRFcGGLHAAGFVLATFAVTELVTVSSGVWLSM 987
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1018 WTSeysiNNTGKADQTY-YV-AGFSILCGAGIFLCLVTSLTVEWMGltaAKNLHHNLLNKIILGPIRFFDTTPLGLILNR 1095
Cdd:PTZ00243 988 WST----RSFKLSAATYlYVyLGIVLLGTFSVPLRFFLSYEAMRRG---SRNMHRDLLRSVSRGTMSFFDTTPLGRILNR 1060
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1096 FSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHF 1175
Cdd:PTZ00243 1061 FSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLL 1140
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1176 SETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLT------ASIASISGSSNSGLVG 1249
Cdd:PTZ00243 1141 EEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVialigvIGTMLRATSQEIGLVS 1220
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1250 LGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF--------------LTMESENYEGT---------MDPSQVPEHW 1306
Cdd:PTZ00243 1221 LSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYtdevphedmpeldeEVDALERRTGMaadvtgtvvIEPASPTSAA 1300
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1307 P---QEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLH 1383
Cdd:PTZ00243 1301 PhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR 1380
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1384 TLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 1463
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1464 VRKSSILI-MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFA 1542
Cdd:PTZ00243 1461 LKKGSGFIlMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
....*
gi 110832837 1543 SFVRA 1547
Cdd:PTZ00243 1541 SMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1310-1549 |
2.46e-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: 516.77 E-value: 2.46e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1310 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1389
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1469
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1470 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM 1549
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
672-889 |
5.07e-157 |
|
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: 474.51 E-value: 5.07e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYS 751
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 831
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 832 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGS 889
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
221-1536 |
5.49e-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: 463.61 E-value: 5.49e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 221 NLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTnyvcLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLS 300
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADN----LSERLEREWDRELASAKKNPKLLNALRRCFFWRFVFY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 301 STFRYLADLLGFAGPLCISGIVQRVNEtqngtnnttgisetlSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETG 380
Cdd:TIGR01271 86 GILLYFGEATKAVQPLLLGRIIASYDP---------------FNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 381 INLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGA 460
Cdd:TIGR01271 151 MQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 461 AVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFAlytSLSI 540
Cdd:TIGR01271 229 GFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA---YLRY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 541 FMNAAIPIAAVLATF---VTHAYASGNNLKpaEAFASLSLFHIL-VTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEigd 616
Cdd:TIGR01271 306 FYSSAFFFSGFFVVFlsvVPYALIKGIILR--RIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEE--- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 617 dsWRTGESSLpfesckkhTGVQPKTINRKQpgryhldSYEQSTRRL-RPAETEDIAIKVTNG----YFSWGSGLAT--LS 689
Cdd:TIGR01271 381 --YKTLEYNL--------TTTEVEMVNVTA-------SWDEGIGELfEKIKQNNKARKQPNGddglFFSNFSLYVTpvLK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfeatrsrnrySVAYAAQKPWLLNATVEEN 769
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPGTIKDN 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 770 ITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH 849
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 850 LMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD---------VELYEHWK--------- 911
Cdd:TIGR01271 587 IFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfsslllgLEAFDNFSaerrnsilt 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 912 -TLM-------------------------------------------NRQDQELEKDMEADQTT---------LERK--- 935
Cdd:TIGR01271 665 eTLRrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasARKFSFVQMGPQKAQATtiedavrepSERKfsl 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 936 ---------TLRRA-MYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRT---KM------------------------- 977
Cdd:TIGR01271 745 vpedeqgeeSLPRGnQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQLQTsfrKKssitqqnelaseldiysrrlskdsv 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 978 ---------------------------PWKTCWRYLTSGG--FFLLI--LMIFSKLLKHSVIVaidYWLATWTSEYSINN 1026
Cdd:TIGR01271 825 yeiseeineedlkecfaderenvfettTWNTYLRYITTNRnlVFVLIfcLVIFLAEVAASLLG---LWLITDNPSAPNYV 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1027 TGK-ADQTYYVAGFSILCGAG-----IFLCLVTSLTVEWMG-----------LTAAKNLHHNLLNKIILGPIRFFDTTPL 1089
Cdd:TIGR01271 902 DQQhANASSPDVQKPVIITPTsayyiFYIYVGTADSVLALGffrglplvhtlLTVSKRLHEQMLHSVLQAPMAVLNTMKA 981
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1090 GLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQL 1169
Cdd:TIGR01271 982 GRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARS 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1170 PLLCHFSETAEGLTTIRAFRHETRFK---QRMLELTDTNNIAYLflsAANRWLEVRTDYLGACIVLTASIASISGSSNSG 1246
Cdd:TIGR01271 1062 PIFSHLITSLKGLWTIRAFGRQSYFEtlfHKALNLHTANWFLYL---STLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGE 1138
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1247 -LVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGT-------------MDPSQVPEHWPQEGEI 1312
Cdd:TIGR01271 1139 gEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSggggkyqlstvlvIENPHAQKCWPSGGQM 1218
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1313 KIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRLSII 1392
Cdd:TIGR01271 1219 DVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVI 1297
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1393 LQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 1472
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLL 1377
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1473 DEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
299-605 |
9.19e-138 |
|
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: 426.65 E-value: 9.19e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 299 LSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISET--LSSKEFLENAYVLAVLLFLALILQRTFLQASYYVT 376
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVsyVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 377 IETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSA 456
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 457 LVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYT 536
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 537 SLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1310-1530 |
4.29e-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: 399.56 E-value: 4.29e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1310 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1389
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1469
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1470 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1530
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 ... |
995-1286 |
1.28e-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: 388.50 E-value: 1.28e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 995 ILMIFSKLLKHSVIVAIDYWLATWTSE----------YSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTA 1064
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEAnhdvasvvfnITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1065 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGV 1144
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1145 AFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTD 1224
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 1225 YLGACIVL----TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1286
Cdd:cd18602 242 YLGAVIVFlaalSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
672-889 |
2.38e-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: 330.97 E-value: 2.38e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLA----TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfeatrsr 747
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 748 nrySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 827
Cdd:cd03250 67 ---SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 828 QNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKrTLVLVTHKLQYLTHADWIIAMKDGS 889
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
971-1547 |
4.29e-102 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 339.45 E-value: 4.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 971 MRLRTKMPWKTCWRYLtSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSinNTGKADQTYYVAGFSILCGAGIFLC 1050
Cdd:COG1132 1 MSKSPRKLLRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL--AGGDLSALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1051 -LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMIS 1129
Cdd:COG1132 78 sYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1130 YATP----VFLVALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDT 1204
Cdd:COG1132 158 VIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEaLAELNG-----RLQESLSGIRVVKAFGREERELERFREANEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1205 NNIAYLFLSAANRWLEVRTDYLGACIVLTasiasisgssnsgLVGLG-----------------LLYALTITNYLNWVVR 1267
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELLGNLGLAL-------------VLLVGgllvlsgsltvgdlvafILYLLRLFGPLRQLAN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1268 NLADLEVQMGAVKKVNSFLTMESENYEGTmDPSQVPehwPQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGR 1347
Cdd:COG1132 300 VLNQLQRALASAERIFELLDEPPEIPDPP-GAVPLP---PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1348 TGSGKSSL-SLaFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALE 1423
Cdd:COG1132 375 SGSGKSTLvNL-LLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDA--TDEEVEEAAK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1424 IAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTI 1503
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 110832837 1504 AHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1547
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRL 574
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1306-1530 |
4.67e-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: 4.67e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1306 WPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL 1385
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 RSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEiaqlknmvkslpggldavVTEGGENFSVGQRQLFCLARAFVR 1465
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1466 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTP 1530
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
990-1285 |
6.70e-82 |
|
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: 271.30 E-value: 6.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 990 GFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTgkadqTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLH 1069
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG-----YYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1070 HNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFI 1149
Cdd:cd18580 76 DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1150 QKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGAC 1229
Cdd:cd18580 156 QRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 1230 IV--LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 1285
Cdd:cd18580 236 LAlvVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1036-1546 |
4.00e-81 |
|
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: 283.26 E-value: 4.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1036 VAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIP-PTLESL 1114
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1115 TRSTLLCLSAIGMISYATPVFLVALLPLGVAF---YFIQKYFRVASKDLQELDDSTQLpllcHFSETAEGLTTIRAFRHE 1191
Cdd:COG2274 278 LDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVllgLLFQPRLRRLSREESEASAKRQS----LLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1192 TRFKQRMLELTdtnnIAYLFLSAANRWLEVRTDYLGACIvltasiasisgssnSGLVGLGLLYA---------LTI---- 1258
Cdd:COG2274 354 SRFRRRWENLL----AKYLNARFKLRRLSNLLSTLSGLL--------------QQLATVALLWLgaylvidgqLTLgqli 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1259 -TNYLNWV----VRNLADL--EVQM--GAVKKVNSFLTMESENYEGTmDPSQVPEhwpQEGEIKIHDLCVRYENNLKPVL 1329
Cdd:COG2274 416 aFNILSGRflapVAQLIGLlqRFQDakIALERLDDILDLPPEREEGR-SKLSLPR---LKGDIELENVSFRYPGDSPPVL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1330 KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL-- 1407
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItl 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1408 -DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 1486
Cdd:COG2274 572 gDPDA--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1487 LQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFASFVR 1546
Cdd:COG2274 650 ILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQ 708
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
992-1273 |
1.33e-77 |
|
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: 258.95 E-value: 1.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 992 FLLILMIFskLLKHSVIVAIDYWLATWTSEYSINNTGKADQT-YYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 1070
Cdd:cd18603 1 SLLILLLY--LLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1071 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 1150
Cdd:cd18603 79 KLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1151 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 1230
Cdd:cd18603 159 RFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 110832837 1231 VLTASIASISGSSNSG--LVGLGLLYALTITNYLNWVVRNLADLE 1273
Cdd:cd18603 239 VLFAALFAVLSRDSLSpgLVGLSISYALQITQTLNWLVRMTSELE 283
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
995-1286 |
2.91e-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: 243.53 E-value: 2.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 995 ILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQ---TYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHN 1071
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEvsvLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1072 LLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQK 1151
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1152 YFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIV 1231
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 1232 L-TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1286
Cdd:cd18604 242 FaTAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1310-1536 |
5.20e-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: 5.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1310 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1389
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1466
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIrlgRPNA--TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1467 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1118-1537 |
1.42e-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: 245.05 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1118 TLLCLSAIGMISYATPVFLVALLPLGVAF-YFIQKYFRVASKD----LQELDDstqlpllcHFSETAEGLTTIRAFRHET 1192
Cdd:COG4988 146 PLLILVAVFPLDWLSGLILLVTAPLIPLFmILVGKGAAKASRRqwraLARLSG--------HFLDRLRGLTTLKLFGRAK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1193 RFKQRMLELTDTNNIAYL------FLSAANrwLEVRTdYLGACIVLtasiasisgssnsGLVGLGLLYA-LTITN----- 1260
Cdd:COG4988 218 AEAERIAEASEDFRKRTMkvlrvaFLSSAV--LEFFA-SLSIALVA-------------VYIGFRLLGGsLTLFAalfvl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1261 ------YLNwvVRNLAdleVQ-------MGAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKP 1327
Cdd:COG4988 282 llapefFLP--LRDLG---SFyharangIAAAEKIFALLDAPEP----AAPAGTAPLPAAGPPSIELEDVSFSYPGG-RP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1328 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 1407
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1408 ---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1484
Cdd:COG4988 432 rlgRPDA--SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1485 NILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1537
Cdd:COG4988 510 AEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
299-605 |
7.96e-69 |
|
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: 233.53 E-value: 7.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 299 LSSTFRYLADLLGFAGPLCISGIVQRVNETQNgtnnttgisetlsskEFLENAYVLAVLLFLALILQRTFLQASYYVTIE 378
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD---------------EPLSEGYLLALALFLVSLLQSLLLHQYFFLSFR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 379 TGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALV 458
Cdd:cd18579 66 LGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 459 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 538
Cdd:cd18579 144 GLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRAL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 539 SIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18579 224 NSFLFFSTPVLVSLATFATYVL-LGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
991-1286 |
2.02e-66 |
|
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: 227.03 E-value: 2.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 991 FFLLILMIFSKllkhsviVAIDYWLATWTSEYSIN--NTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 1068
Cdd:cd18605 5 LLSLILMQASR-------NLIDFWLSYWVSHSNNSffNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1069 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYF 1148
Cdd:cd18605 78 HNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1149 IQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGA 1228
Cdd:cd18605 158 IQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1229 CIV-----LTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1286
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 ... |
991-1279 |
6.09e-63 |
|
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: 216.57 E-value: 6.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 991 FFLLILMIFSKllkhsviVAIDYWLATWTSeysinNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHH 1070
Cdd:cd18606 5 LLLLILSQFAQ-------VFTNLWLSFWTE-----DFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1071 NLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQ 1150
Cdd:cd18606 73 KALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1151 KYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACI 1230
Cdd:cd18606 153 NYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1231 VL--TASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAV 1279
Cdd:cd18606 233 VLivALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSV 283
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1312-1522 |
6.20e-63 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 211.86 E-value: 6.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSILI 1471
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1472 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1522
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
365-605 |
4.04e-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: 4.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 365 QRTFLQASYYVTIETGINLRGALLAMIYNKILRLStsNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMG 444
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 445 VILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMK 524
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 525 ELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQ 603
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 110832837 604 KL 605
Cdd:cd18595 289 RL 290
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
990-1286 |
1.11e-60 |
|
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: 210.88 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 990 GFFLLILMIFSKLLKHSVIVAIDYWLATW--------------TSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSL 1055
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgnttnnvdnSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1056 TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVF 1135
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1136 LVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAA 1215
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1216 NRWLEVRTDYLGACIVLTASIASISGSSNS--GLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFL 1286
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSIspAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1312-1543 |
3.47e-58 |
|
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: 200.92 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1468
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDA--TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1469 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqENGVFAS 1543
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1312-1542 |
1.20e-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: 199.38 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 1468
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1469 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFA 1542
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYA 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1036-1543 |
1.28e-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: 210.34 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1036 VAGFSILCGAGIFlclVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 1115
Cdd:TIGR02203 60 VIGLAVLRGICSF---VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1116 RSTLLCLSAIGMI---SYATPVFLVALLPL-GVAFYFIQKYFRVASKDLQELD-DSTQLpllchFSETAEGLTTIRAFRH 1190
Cdd:TIGR02203 137 RETLTVIGLFIVLlyySWQLTLIVVVMLPVlSILMRRVSKRLRRISKEIQNSMgQVTTV-----AEETLQGYRVVKLFGG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1191 ETRFKQRmleltdtnniaYLFLSAANRWLEVRTDYLGACI-----VLTASIASISGSSNSGLVGLGLLYALTITNYLNWV 1265
Cdd:TIGR02203 212 QAYETRR-----------FDAVSNRNRRLAMKMTSAGSISspitqLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1266 ------VRNLADLEVQM----GAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAY 1335
Cdd:TIGR02203 281 ialirpLKSLTNVNAPMqrglAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1336 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPEcK 1412
Cdd:TIGR02203 355 IEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTE-Q 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1413 CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1492
Cdd:TIGR02203 434 ADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALE 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1493 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFAS 1543
Cdd:TIGR02203 514 RLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
371-895 |
5.27e-56 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 205.78 E-value: 5.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 371 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFL-FLCPNLWAMPVQIIMGVILLY 449
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 450 NLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVEETRMKE 525
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREerelERFREANEELRRAN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 526 LSSLKTFALYTSLSIFMNAAIpIAAVLAtFVTHAYASGNnLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLG-LALVLL-VGGLLVLSGS-LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 606 NEFL-LSDEIGDdswrtGESSLPFesckkhtgvqpktinrkqpgryhldsyeqstrrlrPAETEDIAIK-VTngyFSWGS 683
Cdd:COG1132 315 FELLdEPPEIPD-----PPGAVPL-----------------------------------PPVRGEIEFEnVS---FSYPG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLN 763
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ----IGVVPQDTFLFS 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 ATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 842
Cdd:COG1132 428 GTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 110832837 843 DIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:COG1132 508 DTE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
368-605 |
2.22e-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: 194.98 E-value: 2.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 368 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 528 SLKTFALYTSLSIFMNAAIPIAAVLATFVThAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18597 217 YVRKLQILRSILTAVAFSLPVLASMLSFIT-YYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1327-1547 |
5.47e-55 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 191.60 E-value: 5.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1327 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 1406
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1407 L---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 1483
Cdd:cd03249 97 IrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1484 ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEnGVFASFVRA 1547
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
367-911 |
1.36e-53 |
|
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: 201.22 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 367 TFLQASYYVTIETGINLRgaLLAMIYNKILRLSTSNL---SMGEMtLGQINNLVAIE---TNQLMWFLFLCPNLWampvq 440
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDL-ASRFRDVESIReflTGSLLTALLDLLFVL----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 441 IIMGVILLYNllGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYA--------WEH 512
Cdd:COG2274 285 IFLIVLFFYS--PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWEN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 513 IFCKSVEetrmKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVTHayasgNNLKPAEAFASLSLFHILVTPLF-LLS 589
Cdd:COG2274 363 LLAKYLN----ARFKLRRLSNLLSTLSGLLQQLATVALLWlgAYLVID-----GQLTLGQLIAFNILSGRFLAPVAqLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 590 TVVRFAvKAIISVQKLNEFLlsdeigddswrtgesSLPFEsckkhtgvqpktinrkqpgryhldsyEQSTRRLRPAETED 669
Cdd:COG2274 434 LLQRFQ-DAKIALERLDDIL---------------DLPPE--------------------------REEGRSKLSLPRLK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 670 IAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSrn 748
Cdd:COG2274 472 GDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR-- 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 749 rySVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 827
Cdd:COG2274 550 --QIGVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 828 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELY 907
Cdd:COG2274 628 RNPRILILDEATSALDAE-TEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
....
gi 110832837 908 EHWK 911
Cdd:COG2274 705 ELVQ 708
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
367-603 |
4.08e-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: 186.16 E-value: 4.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 367 TFLQASYYVTIETGINLRGALLAMIYNKILRL-----------------STSNLSMGEMTLGQINNLVAIETN---QLMW 426
Cdd:cd18596 54 LLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANrisEFAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 427 FLFLcpnLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK 506
Cdd:cd18596 134 FLHL---LVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 507 LYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLF 586
Cdd:cd18596 211 FFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLN 290
|
250
....*....|....*..
gi 110832837 587 LLSTVVRFAVKAIISVQ 603
Cdd:cd18596 291 VLPELITQLLQAKVSLD 307
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
990-1282 |
6.02e-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: 185.99 E-value: 6.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 990 GFFLLILMIFSKLLKHSVIVAIDYWLATWTSEY---------------SINNTGKADQTYYVAGFSILCGAGIFLCLVTS 1054
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEeklndttdrvqgensTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1055 LTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPV 1134
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1135 FLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAY-LFLs 1213
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWfLFL- 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1214 AANRWLEVRTDYLGA--CIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKV 1282
Cdd:cd18601 240 ATSRWLAVRLDALCAlfVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
983-1545 |
8.97e-52 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 196.10 E-value: 8.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 983 WRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLvtsltvewMGL 1062
Cdd:TIGR00958 160 WPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYT--------MAR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1063 TAAKnLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRS--TLLCLSAIgMIS---YATPVFLV 1137
Cdd:TIGR00958 232 INLR-IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNlvMLLGLLGF-MLWlspRLTMVTLI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1138 ALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQLPLlchfsETAEGLTTIRAFRHE----TRFKQ---RMLELTDTNNIAY 1209
Cdd:TIGR00958 310 NLPLVFLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFAAEegeaSRFKEaleETLQLNKRKALAY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1210 LFLSAANRWLE----VRTDYLGACIVLTASIASISgssnsgLVGLgLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSF 1285
Cdd:TIGR00958 385 AGYLWTTSVLGmliqVLVLYYGGQLVLTGKVSSGN------LVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1286 L--TMESENyEGTMDPSQVpehwpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRM 1362
Cdd:TIGR00958 458 LdrKPNIPL-TGTLAPLNL------EGLIEFQDVSFSYPNRPdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1363 VDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAV 1441
Cdd:TIGR00958 531 YQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLtDTPDEEIMAAAKAANAHDFIMEFPNGYDTE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1442 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKR 1521
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKK 688
|
570 580
....*....|....*....|....
gi 110832837 1522 GNILEYDTPESLLAQEnGVFASFV 1545
Cdd:TIGR00958 689 GSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1310-1538 |
1.33e-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: 183.52 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1310 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 1389
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 1469
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1470 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1538
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
667-903 |
2.00e-51 |
|
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: 191.90 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 667 TEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRS 746
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 RnrysVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 825
Cdd:COG4988 412 Q----IAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 826 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 903
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1049-1537 |
2.30e-51 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 192.24 E-value: 2.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1049 LCLVTSLTVEWMGLTA-AKNLHHN---LLNKIILG----------------PIRFFDTTPLGLILNRFSADTNIIDQHIP 1108
Cdd:PRK10790 61 LGLVAGLAAAYVGLQLlAAGLHYAqslLFNRAAVGvvqqlrtdvmdaalrqPLSAFDTQPVGQLISRVTNDTEVIRDLYV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1109 PTLESLTRSTLLcLSA--IGMISYATPVFLVALL--PLGVAFYFIQKYF------RVASKdLQELDDStqlpllchFSET 1178
Cdd:PRK10790 141 TVVATVLRSAAL-IGAmlVAMFSLDWRMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1179 AEGLTTIRAFRHETRFKQRMLELTDTNNIAylflsaanRWLEVRTD--------YLGACIVLTASIASISGSSNSGlVGL 1250
Cdd:PRK10790 211 INGMSVIQQFRQQARFGERMGEASRSHYMA--------RMQTLRLDgfllrpllSLFSALILCGLLMLFGFSASGT-IEV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1251 GLLYALTitNYLNWVVRNLADLE-----VQMGAVKKVNSFLTMESENYEGTMDPSQVpehwpQEGEIKIHDLCVRYENNl 1325
Cdd:PRK10790 282 GVLYAFI--SYLGRLNEPLIELTtqqsmLQQAVVAGERVFELMDGPRQQYGNDDRPL-----QSGRIDIDNVSFAYRDD- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1326 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 1405
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1406 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 1485
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1486 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1537
Cdd:PRK10790 514 AIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1310-1524 |
2.51e-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: 174.70 E-value: 2.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1310 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1389
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1466
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 1467 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1524
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1260-1543 |
1.03e-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: 184.64 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1260 NYLNWVVR----NLADLEvQMGAVkkvnsfLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAY 1335
Cdd:COG5265 313 NFLGFVYReirqALADME-RMFDL------LDQPPE----VADAPDAPPLVVGGGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1336 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECk 1412
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDA- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1413 cTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM 1492
Cdd:COG5265 460 -SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1493 TAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQeNGVFAS 1543
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQ 588
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1286-1549 |
2.16e-48 |
|
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: 185.16 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1286 LTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDI 1365
Cdd:TIGR03797 432 LEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRLLLG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1366 FD----GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAV 1441
Cdd:TIGR03797 502 FEtpesGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1442 VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFA--DRTVVTIAHRVHTILTADLVIVM 1519
Cdd:TIGR03797 582 ISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRTQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVL 657
|
250 260 270
....*....|....*....|....*....|
gi 110832837 1520 KRGNILEYDTPESLLAQEnGVFASFVRADM 1549
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 ... |
303-605 |
2.31e-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: 171.58 E-value: 2.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 303 FRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLenayvlavllflalilqRTFLQASY-YVTIETGI 381
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLL-----------------GALLSSHYnFQMNKVSL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 382 NLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQLMWFlflCPNL---WAMPVQIIMGVILLYNLLGSSALV 458
Cdd:cd18598 68 KVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGVAFLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 459 GAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSL 538
Cdd:cd18598 143 GLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 539 SIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18598 223 CVYFWATTPVLISILTFATYVL-MGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1320-1545 |
5.75e-47 |
|
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: 168.82 E-value: 5.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1320 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILF 1399
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1400 SGSIRFNL---DPECKCtdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1476
Cdd:cd03252 89 NRSIRDNIalaDPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1477 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAqENGVFASFV 1545
Cdd:cd03252 167 SALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLY 234
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1294-1546 |
1.74e-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: 179.75 E-value: 1.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1294 EGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMV----DIFDGK 1369
Cdd:TIGR03796 460 EPEGSAATSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVaglyQPWSGE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1370 IVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG 1446
Cdd:TIGR03796 536 ILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGG 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1447 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilqKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNI 1524
Cdd:TIGR03796 614 ANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKV 689
|
250 260
....*....|....*....|..
gi 110832837 1525 LEYDTPESLLAQEnGVFASFVR 1546
Cdd:TIGR03796 690 VQRGTHEELWAVG-GAYARLIR 710
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
368-605 |
1.07e-44 |
|
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: 163.89 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 368 FLQASYYVTIETGINLRGALLAMIYNKILRLStsnlSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 528 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHaYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAH-VALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1276-1542 |
1.88e-44 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 171.36 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1276 MGAVKKVNSFLTMESENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1355
Cdd:PRK11176 312 MAACQTLFAILDLEQEKDEGKRVIERA------KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1356 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPEC--KCTDDRLWEALEIAQLKNMVKS 1433
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINK 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1434 LPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTA 1513
Cdd:PRK11176 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKA 545
|
250 260
....*....|....*....|....*....
gi 110832837 1514 DLVIVMKRGNILEYDTPESLLAQeNGVFA 1542
Cdd:PRK11176 546 DEILVVEDGEIVERGTHAELLAQ-NGVYA 573
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
672-888 |
4.28e-44 |
|
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: 157.93 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnry 750
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 sVAYAAQKPWLLNATVEENItfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNT 830
Cdd:cd03228 78 -IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 831 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDG 888
Cdd:cd03228 116 PILILDEATSALDPE-TEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1281-1547 |
9.41e-44 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 169.37 E-value: 9.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1281 KVNSFLTME-----SENYEGTMDPSQVpehwpqEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL 1355
Cdd:PRK13657 305 KLEEFFEVEdavpdVRDPPGAIDLGRV------KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1356 SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVK 1432
Cdd:PRK13657 378 INLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRPDA--TDEEMRAAAERAQAHDFIE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1433 SLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT 1512
Cdd:PRK13657 456 RKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN 535
|
250 260 270
....*....|....*....|....*....|....*
gi 110832837 1513 ADLVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1547
Cdd:PRK13657 536 ADRILVFDNGRVVESGSFDELVAR-GGRFAALLRA 569
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
651-895 |
4.28e-43 |
|
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: 166.87 E-value: 4.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 651 HLDSYEQSTRRL------RPAETE---------DIAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL 714
Cdd:COG4987 298 HLGRVRAAARRLnelldaPPAVTEpaepapapgGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 715 LLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPD 793
Cdd:COG4987 378 LALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR----IAVVPQRPHLFDTTLRENLRLARPdATDEELWAALERVGLGDW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 794 IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKL 873
Cdd:COG4987 454 LAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRL 530
|
250 260
....*....|....*....|..
gi 110832837 874 QYLTHADWIIAMKDGSVLREGT 895
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGT 552
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
688-939 |
1.35e-42 |
|
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: 157.71 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesepsfeatrsrnrySVAYAAQKPWLLNATVE 767
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 847
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 848 DHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHwktLMNRQdqelekdmEA 927
Cdd:cd03291 196 KEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSK---LMGYD--------TF 262
|
250
....*....|....*...
gi 110832837 928 DQTTLERK------TLRR 939
Cdd:cd03291 263 DQFSAERRnsilteTLRR 280
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1118-1519 |
8.16e-42 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 162.46 E-value: 8.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1118 TLLCLSAIGMISYATPVFLVALLPLgVAFYFIQKYFRVASKDLQELDDSTQLPllCHFSETAEGLTTIRAFRHETRFKQR 1197
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPL-IPIFMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1198 MLELTD--------TNNIAylFLSAANrwLEVRTDyLGACIVLTAsiasisgssnsglVGLGLLY-------ALTI---- 1258
Cdd:TIGR02857 209 IRRSSEeyrertmrVLRIA--FLSSAV--LELFAT-LSVALVAVY-------------IGFRLLAgdldlatGLFVllla 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1259 -TNYLNwvVRNL-ADLEVQMGAVKKVNSFLTMESENyeGTMDPSQVPEHWPQEGEIKIHDLCVRYENNlKPVLKHVKAYI 1336
Cdd:TIGR02857 271 pEFYLP--LRQLgAQYHARADGVAAAEALFAVLDAA--PRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTV 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1337 KPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkc 1413
Cdd:TIGR02857 346 PPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA-- 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1414 TDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT 1493
Cdd:TIGR02857 424 SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
|
410 420
....*....|....*....|....*.
gi 110832837 1494 AFADRTVVTIAHRVHTILTADLVIVM 1519
Cdd:TIGR02857 504 LAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
368-606 |
1.72e-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: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 368 FLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVIL 447
Cdd:cd18594 55 LHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 448 LYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELS 527
Cdd:cd18594 133 LWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 528 SLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYaSGNNLKPAEAFASLSLFHILVTPL-FLLSTVVRFAVKAIISVQKLN 606
Cdd:cd18594 213 LIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVL-TGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
672-911 |
6.80e-40 |
|
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: 148.15 E-value: 6.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSrnryS 751
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWLLNATVEENITFGSP--FNKQRYKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 829
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYGRPdaTDEEVIEAAKAAQ-IHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 830 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEH 909
Cdd:cd03253 156 PPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
..
gi 110832837 910 WK 911
Cdd:cd03253 233 WK 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
672-895 |
4.21e-39 |
|
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: 145.83 E-value: 4.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrys 751
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWLLNATVEENITFGSPFNKQ-RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 830
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 831 NIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:cd03254 159 KILILDEATSNIDTE-TEKLIQEALEKLMKG--RTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1068-1547 |
6.33e-39 |
|
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: 156.44 E-value: 6.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1068 LHHNLLNKIILG--------PIRFFDTTPLGLILNRFSADTNIIDqhippTLESLTRSTLLCLSAIGMISYA-----TPV 1134
Cdd:TIGR01193 223 LGQRLSIDIILSyikhlfelPMSFFSTRRTGEIVSRFTDASSIID-----ALASTILSLFLDMWILVIVGLFlvrqnMLL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1135 FLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLpLLCHFSETAEGLTTIRAFRHE-TRFKQ----------RMLELTD 1203
Cdd:TIGR01193 298 FLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAV-LNSSIIEDLNGIETIKSLTSEaERYSKidsefgdylnKSFKYQK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1204 TNNIAYLFLSAANRWLEVRTDYLGACIVLTASIAsisgssnsglVGLGLLYALTITNYLNwVVRNLADLEVQMGAVK--- 1280
Cdd:TIGR01193 377 ADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLT----------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvan 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1281 -KVNSFLTMESE-NYEGTMDPSQVPEhwpqeGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLA 1358
Cdd:TIGR01193 446 nRLNEVYLVDSEfINKKKRTELNNLN-----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1359 FFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLWEALEIAQLKNMVKSLPG 1436
Cdd:TIGR01193 520 LVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1437 GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILTAD 1514
Cdd:TIGR01193 600 GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSD 676
|
490 500 510
....*....|....*....|....*....|...
gi 110832837 1515 LVIVMKRGNILEYDTPESLLAQeNGVFASFVRA 1547
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELLDR-NGFYASLIHN 708
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1307-1506 |
2.51e-38 |
|
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: 152.13 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1307 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1386
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1387 SRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 1463
Cdd:TIGR02868 409 RRVSVCAQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110832837 1464 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1506
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
686-894 |
2.52e-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: 140.42 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 686 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESE--PsfeATRSRNrysVAYAAQKPWLLN 763
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldP---ADLRRN---IGYVPQDVTLFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 ATVEENITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 842
Cdd:cd03245 92 GTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110832837 843 DIHLSDHLMQEgiLKFLQDDKrTLVLVTHKLQYLTHADWIIAMKDGSVLREG 894
Cdd:cd03245 172 DMNSEERLKER--LRQLLGDK-TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1277-1547 |
9.07e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.07 E-value: 9.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1277 GAVKKVNSFLTMESEnyegTMDPSQVPEHWPQEGEIKIHDLCVrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS 1356
Cdd:PRK11174 319 GAAESLVTFLETPLA----HPQQGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1357 ---LAFFRmvdiFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPECkcTDDRLWEALEIAQLKNM 1430
Cdd:PRK11174 394 nalLGFLP----YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1431 VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI 1510
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 110832837 1511 LTADLVIVMKRGNILE---YDTpeslLAQENGVFASFVRA 1547
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
682-895 |
1.84e-36 |
|
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: 138.52 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSrnrySVAYAAQKPWL 761
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR----QIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 840
Cdd:cd03251 88 FNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 841 ALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:cd03251 168 ALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
652-885 |
1.00e-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: 143.97 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 652 LDSYEQSTRRLRPA-ETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVh 730
Cdd:TIGR02857 301 LDAAPRPLAGKAPVtAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 731 wsNVNeSEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQ-RYKAVTDACSLQPDIDLLPFGDQTEIGERG 809
Cdd:TIGR02857 380 --AVN-GVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGG 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 810 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAM 885
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE-TEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1307-1542 |
1.38e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 144.58 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1307 PQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 1386
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1387 SRLSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSlPGGLDAVVTEGGENFSVGQRQLFCLARAF 1463
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1464 VRKSSILIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFA 1542
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
688-895 |
6.39e-35 |
|
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: 134.20 E-value: 6.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 767
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ----IGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSPFNKQryKAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 844
Cdd:cd03249 95 ENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 845 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:cd03249 173 E-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1300-1524 |
5.08e-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: 131.05 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1300 SQVPEHWpqEGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS 1378
Cdd:cd03248 2 SLAPDHL--KGIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1379 KLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLF 1457
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQsCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1524
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
667-909 |
5.40e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 667 TEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNesepsfeATRS 746
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPV-LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-------PRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 RNRysVAYAAQK---PWLLNATVEE--------NITFGSPFNKQRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGG 815
Cdd:COG1121 74 RRR--IGYVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADRP-IGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 816 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGsVLREG 894
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVrEYFDRVLLLNRG-LVAHG 220
|
250
....*....|....*..
gi 110832837 895 TLKDIQTKDV--ELYEH 909
Cdd:COG1121 221 PPEEVLTPENlsRAYGG 237
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1312-1524 |
1.03e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 128.10 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIF---DGKIVIDGIDISKLPLHTLRSR 1388
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLrptSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 LSIILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSS 1468
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1469 ILIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNI 1524
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
372-579 |
1.05e-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: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 372 SYYVTIETGINLRGALLAMIYNKILRLSTSnlSMGEMTLGQINNLVAIETNQL-MWFLFLcPNLWAMPVQIIMGVILLYN 450
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 451 LLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLK 530
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110832837 531 TFALYTSlsifMNAAIPIAA----VLATFVTHAYaSGNNLKPAEAFASLSLFH 579
Cdd:cd18593 217 RTSFLRA----LNMGLFFVSskliLFLTFLAYIL-LGNILTAERVFVTMALYN 264
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1312-1536 |
3.09e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 137.15 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCvrYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:PRK10789 316 VNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1470
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1471 IMDEATASIDMATE-NILQKVVMTAfADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1536
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 ... |
673-888 |
5.89e-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: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 673 KVTNGYFSWGSGL-ATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrys 751
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRIC 821
Cdd:cd03225 77 VGLVFQNPddQFFGPTVEEEVAFG-LENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 822 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDG 888
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
688-907 |
6.53e-32 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 125.93 E-value: 6.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAtRSRNrysVAYAAQK---PWLLna 764
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE-LARR---IAYVPQEppaPFGL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFG--------SPFNKQRYKAVTDACslqpdidllpfgDQTEIG---ERGIN-LSGGQRQRICVARALYQNTNI 832
Cdd:COG1120 91 TVRELVALGryphlglfGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeLSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 833 VFLDDPFSALDIHlsdHlmQEGILKFLQD----DKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQTKDV--E 905
Cdd:COG1120 159 LLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTPELleE 233
|
..
gi 110832837 906 LY 907
Cdd:COG1120 234 VY 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1312-1526 |
1.69e-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: 122.04 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRLSI 1391
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPILFSGSIRFNLdpeckctddrlwealeiaqlknmvkslpggldavvtegGENFSVGQRQLFCLARAFVRKSSILI 1471
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1472 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILE 1526
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
672-899 |
1.88e-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: 123.60 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrys 751
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPW--LLNATVEENITFGsPFN--------KQRYKAVTDACSLQpdiDLL---PFgdqteigergiNLSGGQRQ 818
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEEDVAFG-PENlglpreeiRERVEEALELVGLE---HLAdrpPH-----------ELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 819 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLK 897
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPR 219
|
..
gi 110832837 898 DI 899
Cdd:COG1122 220 EV 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
688-895 |
3.59e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 130.99 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 767
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR----LAVVSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 846
Cdd:PRK10789 407 NNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR- 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 847 SDHlmqeGILKFLQD--DKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:PRK10789 486 TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
672-895 |
5.27e-31 |
|
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: 122.22 E-value: 5.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnry 750
Cdd:cd03244 3 IEFKNVSLRYRPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 sVAYAAQKPWLLNATVEENItfgSPFNK----QRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 826
Cdd:cd03244 80 -ISIIPQDPVLFSGTIRSNL---DPFGEysdeELWQAL-ERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 827 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:cd03244 155 LRKSKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1312-1537 |
1.42e-30 |
|
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: 121.29 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPI--LFSGSIR---------FNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1460
Cdd:COG1122 80 VFQNPDdqLFAPTVEedvafgpenLGLPREE--IRERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1461 RAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQE 1537
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
682-903 |
1.90e-30 |
|
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: 128.68 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWL 761
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ----VALVSQDVVL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNATVEENITFGSP--FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:TIGR02203 418 FNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 840 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKD 903
Cdd:TIGR02203 498 SALDNE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1313-1522 |
2.07e-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: 118.12 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1313 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1392
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1393 LQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSILIM 1472
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1473 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTA-DLVIVMKRG 1522
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
994-1232 |
2.07e-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: 122.37 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 994 LILMIFSKLLKHSVIVAIDYWLATWTSEYS-INNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNL 1072
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1073 LNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKY 1152
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1153 FRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVL 1232
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
688-920 |
3.97e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 128.04 E-value: 3.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMqTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 767
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH----LSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 846
Cdd:PRK11174 441 DNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH- 519
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 847 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQE 920
Cdd:PRK11174 520 SEQLVMQALNAASRR--QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT-----LLAHRQE 586
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1312-1522 |
4.14e-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: 119.11 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENN---LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgidisklplhTLRSR 1388
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 LSIILQDPILFSGSIRFN------LDPEckctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 1462
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpFDEE------RYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1463 FVRKSSILIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRG 1522
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
672-908 |
6.22e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 120.19 E-value: 6.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQtlEGKVHWSNVNESE-PSFE-ATRsr 747
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrLLPPD--SGEVLVDGLDVATtPSRElAKR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 748 nrysVAYAAQKPWL-LNATVEENITFGS-PFNKQR-----YKAVTDAcslqpdIDLLpfgDQTEIGERGIN-LSGGQRQR 819
Cdd:COG4604 77 ----LAILRQENHInSRLTVRELVAFGRfPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 820 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLK 897
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPE 221
|
250
....*....|...
gi 110832837 898 DIQTKDV--ELYE 908
Cdd:COG4604 222 EIITPEVlsDIYD 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
667-899 |
6.88e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 6.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 667 TEDIAIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEa 743
Cdd:COG1116 3 AAAPALELRGvskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 744 trsrnrysVAYAAQK----PWLlnaTVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGD----Qteigergin 811
Cdd:COG1116 82 --------RGVVFQEpallPWL---TVLDNVALGLELRgvpkAERRERARELLEL---VGLAGFEDayphQ--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 812 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ---YLthADWIIAMKDg 888
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDE-LLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSA- 214
|
250
....*....|.
gi 110832837 889 svlREGTLKDI 899
Cdd:COG1116 215 ---RPGRIVEE 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
481-1546 |
8.95e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 129.38 E-value: 8.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 481 QKSTLDYSTERLKKTNEILKGIKLLKLYAWEHifcksveeTRMKELS-SLKTFALYTSLSIFMNAaIPIAaVLATFVTHA 559
Cdd:PTZ00265 225 KKTSLLYNNNTMSIIEEALVGIRTVVSYCGEK--------TILKKFNlSEKLYSKYILKANFMES-LHIG-MINGFILAS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 560 YASG------------NNLKPAEAFASLSLFHILV---TPLFLLSTV---VRFAVKAIISVQKLNEFLLSDEIGDDSwRT 621
Cdd:PTZ00265 295 YAFGfwygtriiisdlSNQQPNNDFHGGSVISILLgvlISMFMLTIIlpnITEYMKSLEATNSLYEIINRKPLVENN-DD 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 622 GESslpFESCKKhtgVQPKTInrkqpgRYHLDsyeqsTRRlrpaeteDIAIkvtngyfswgsglatLSNIDIRIPTGQLT 701
Cdd:PTZ00265 374 GKK---LKDIKK---IQFKNV------RFHYD-----TRK-------DVEI---------------YKDLNFTLTEGKTY 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 702 MIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFG-------- 773
Cdd:PTZ00265 415 AFVGESGCGKSTILKLIERLYDPTEGDII---INDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdle 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 774 --------SPFNKQRYKAVTDACSLQPDIDL------------------------------------------LPFGDQT 803
Cdd:PTZ00265 492 alsnyyneDGNDSQENKNKRNSCRAKCAGDLndmsnttdsneliemrknyqtikdsevvdvskkvlihdfvsaLPDKYET 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 804 EIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWII 883
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIF 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 884 AMK--------DGSVLREGTLKDIQTKD--------------------------VELYEH----------WKTLMNRQ-- 917
Cdd:PTZ00265 651 VLSnrergstvDVDIIGEDPTKDNKENNnknnkddnnnnnnnnnnkinnagsyiIEQGTHdalmknkngiYYTMINNQkv 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 918 --------DQELEKDM------------EADQTTLERKTLRRAMySREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKM 977
Cdd:PTZ00265 731 sskkssnnDNDKDSDMkssaykdsergyDPDEMNGNSKHENESA-SNKKSCKMSDENASENNAGGKLPFLRNLFKRKPKA 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 978 P------WKTCWRY-----------LTSGGFFLLILMIFSKLlkhsVIVAIDYW-LATWTSEYSInntgkadqtyyvagF 1039
Cdd:PTZ00265 810 PnnlrivYREIFSYkkdvtiialsiLVAGGLYPVFALLYAKY----VSTLFDFAnLEANSNKYSL--------------Y 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1040 SILCGAGIFLC-LVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDT---TPlGLILNRFSADTNIIDQHIPPTLESLT 1115
Cdd:PTZ00265 872 ILVIAIAMFISeTLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFT 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1116 RSTLLCLSAIGMISYATPVflVALLPLGVAFYFIqKYFRV-----ASKDLQELDDSTQLPLLCHFS-------------E 1177
Cdd:PTZ00265 951 HFIVLFLVSMVMSFYFCPI--VAAVLTGTYFIFM-RVFAIrarltANKDVEKKEINQPGTVFAYNSddeifkdpsfliqE 1027
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1178 TAEGLTTIRAFRHETRFKQRMLELTDTNN------------------IAYLFLSAANRW----------LEVrTDYLGAc 1229
Cdd:PTZ00265 1028 AFYNMNTVIIYGLEDYFCNLIEKAIDYSNkgqkrktlvnsmlwgfsqSAQLFINSFAYWfgsflirrgtILV-DDFMKS- 1105
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1230 iVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNlADLEVQ-MGAVKKVNSFLTmesenyegtmdpsqvpehwpq 1308
Cdd:PTZ00265 1106 -LFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRK-SNIDVRdNGGIRIKNKNDI--------------------- 1162
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1309 EGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD-------------------- 1367
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdy 1242
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1368 ----------------------------------GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD-PECK 1412
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKED 1322
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1413 CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV- 1491
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIv 1402
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1492 -MTAFADRTVVTIAHRVHTILTADLVIVM----KRGNILE-YDTPESLLAQENGVFASFVR 1546
Cdd:PTZ00265 1403 dIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKKYVK 1463
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
672-899 |
9.40e-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: 119.13 E-value: 9.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGS-GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnry 750
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 sVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 829
Cdd:cd03252 78 -VGVVLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 830 TNIVFLDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03252 157 PRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
385-873 |
2.50e-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: 124.78 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 385 GALLAMIYNKILRLS---TSNLSMGEMtlgqINNLVA-IETNQLMWFLFLCPNLWAMPVQII--MGVILLYNLLGSSALV 458
Cdd:TIGR02868 86 GALRVRVYERLARQAlagRRRLRRGDL----LGRLGAdVDALQDLYVRVIVPAGVALVVGAAavAAIAVLSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 459 GAAVIVLLAPiqyFIATKLAEAQKSTLDYS-TERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTS 537
Cdd:TIGR02868 162 GLLLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 538 LSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVT-PLFLLSTVVRFAVKAIISVQKLNEFLlsdeigD 616
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeAFAALPAAAQQLTRVRAAAERIVEVL------D 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 617 DSWRTGESSLPfesckkhtgvQPKTINRKQPGRyhldsyeqstrrlrpaETEDIAikvtngyFSWGSGLATLSNIDIRIP 696
Cdd:TIGR02868 313 AAGPVAEGSAP----------AAGAVGLGKPTL----------------ELRDLS-------AGYPGAPPVLDGVSLDLP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 697 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVEENITFGSP- 775
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFDTTVRENLRLARPd 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 776 FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGI 855
Cdd:TIGR02868 436 ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDL 514
|
490
....*....|....*...
gi 110832837 856 LKflQDDKRTLVLVTHKL 873
Cdd:TIGR02868 515 LA--ALSGRTVVLITHHL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
682-890 |
4.11e-29 |
|
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: 124.48 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 682 GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSnvnesepsfeatRSRNRYSVA 753
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsQWD------------REELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 754 YAAQKPWLLNATVEENIT-FGSPfNKQrykAVTDACSLQpD----IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 828
Cdd:COG4618 410 YLPQDVELFDGTIAENIArFGDA-DPE---KVVAAAKLA-GvhemILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 829 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 890
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAA--AIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
679-886 |
5.57e-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: 116.09 E-value: 5.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 679 FSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNesepSFEATRSRNRysVAYAAQK 758
Cdd:cd03235 7 VSYGGHPV-LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR---VF----GKPLEKERKR--IGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 759 ---PWLLNATVEE--------NITFGSPFNKQRYKAVTDAcslqpdidlLPFGDQTEIGERGI-NLSGGQRQRICVARAL 826
Cdd:cd03235 77 rsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEA---------LERVGLSELADRQIgELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 827 YQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMK 886
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIY--ELLRELRREGMTILVVTHDLGLVLeYFDRVLLLN 206
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
687-902 |
7.07e-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: 123.61 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW--SNVNESEPSFEATrsrnrySVAYAAQKPWLLNA 764
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgADLKQWDRETFGK------HIGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENIT-FGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 843
Cdd:TIGR01842 407 TVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 844 IHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTK 902
Cdd:TIGR01842 487 EEGEQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
303-605 |
8.07e-29 |
|
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: 118.09 E-value: 8.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 303 FRYLADLLGFAGPLCISGIVQRVNETQngtnnttgisetlsskEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGIN 382
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVN----------------GPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 383 LRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAV 462
Cdd:cd18559 69 ASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 463 IVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFM 542
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 543 NAAIPIAAVLATFVTHAYASGNN-LKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKL 605
Cdd:cd18559 227 WCVGPCIVLFASFFAYVSRHSLAgLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
674-893 |
7.38e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 112.95 E-value: 7.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 674 VTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEatrsrnrysVA 753
Cdd:cd03293 6 VSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---------RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 754 YAAQK----PWLlnaTVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQTeIGErginLSGGQRQRICVARA 825
Cdd:cd03293 77 YVFQQdallPWL---TVLDNVALGLELQgvpkAEARERAEELLEL---VGLSGFENAY-PHQ----LSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 826 LYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQ---YLthADWIIAM--KDGSVLRE 893
Cdd:cd03293 146 LAVDPDVLLLDEPFSALD-ALTREQLQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
688-840 |
9.31e-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: 110.43 E-value: 9.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNA-TV 766
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE----IGYVFQDPQLFPRlTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 767 EENITFGSPFnkQRYKAVTDACSLQPDIDLLPFGDQ--TEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 840
Cdd:pfam00005 77 RENLRLGLLL--KGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
673-894 |
1.11e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.99 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 673 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAtRSRNrysV 752
Cdd:cd03214 1 EVENLSVGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE-LARK---I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 753 AYAAQkpwLLNATveenitfgspfnkqrykavtdacslqpdiDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTN 831
Cdd:cd03214 76 AYVPQ---ALELL-----------------------------GLAHLAD------RPFNeLSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 832 IVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKL-QYLTHADWIIAMKDGSVLREG 894
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLE--LLRRLARERgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
673-888 |
1.31e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.03 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 673 KVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysV 752
Cdd:cd00267 1 EIENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR----I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 753 AYAAQkpwllnatveenitfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNI 832
Cdd:cd00267 76 GYVPQ------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 833 VFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA-DWIIAMKDG 888
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1312-1536 |
1.37e-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: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI---FDGKIVIDGIDISKLPLHTLRSR 1388
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 LSIILQDPI--LFSGSIRFNLD--PECKCTD-----DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 1459
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAeaLENLGLSraearARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1460 ARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1532
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
....
gi 110832837 1533 LLAQ 1536
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 ... |
1313-1522 |
1.66e-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: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1313 KIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1392
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1393 LQDP--ILFSGSIR----FNLDPECKCTDD---RLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAF 1463
Cdd:cd03225 81 FQNPddQFFGPTVEeevaFGLENLGLPEEEieeRVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1464 VRKSSILIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG 1522
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1312-1527 |
1.97e-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: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---R 1386
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1387 SRLSIILQDPILfsgsirfNLDP------------ECKCTDDRLWEALEIAQLKNMVKSLPGG-LDAVVTEggenFSVGQ 1453
Cdd:cd03257 82 KEIQMVFQDPMS-------SLNPrmtigeqiaeplRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHE----LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1454 RQLFCLARAFVRKSSILIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTIL-TADLVIVMKRGNILEY 1527
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAkIADRVAVMYAGKIVEE 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
688-913 |
2.37e-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: 119.03 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 767
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR----MALVPQDPVLFAASVM 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhL 846
Cdd:TIGR02204 432 ENIRYGRPdATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA-E 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 847 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDvELYEHWKTL 913
Cdd:TIGR02204 511 SEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG-GLYARLARL 574
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
672-888 |
5.05e-27 |
|
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: 110.66 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHWSNVNESEPSfEATRS- 746
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVRVDGTDISKLS-EKELAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 -RNRySVAYAAQKPWLLNA-TVEENITFGSPFNKQRYKAVTDACslqpdIDLLpfgDQTEIGERgIN-----LSGGQRQR 819
Cdd:cd03255 79 fRRR-HIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERA-----EELL---ERVGLGDR-LNhypseLSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 820 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDG 888
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
666-888 |
7.20e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.91 E-value: 7.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 666 ETEDIAIKVTNGYFswgsglatLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATR 745
Cdd:COG4619 2 ELEGLSFRVGGKPI--------LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SRnrysVAYAAQKPWLLNATVEENITFGSPFNKQRYkavtdacSLQPDIDLLP-FGDQTEIGERGI-NLSGGQRQRICVA 823
Cdd:COG4619 74 RQ----VAYVPQEPALWGGTVRDNLPFPFQLRERKF-------DRERALELLErLGLPPDILDKPVeRLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 824 RALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 888
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRV-EELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1309-1536 |
9.02e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 117.16 E-value: 9.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1309 EGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAffrMVDIFD---GKIVIDGIDISKLPlhtl 1385
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVWPptaGSVRLDGADLSQWD---- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 RSRLSIIL----QDPILFSGSI-----RFNlDPeckcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQL 1456
Cdd:COG4618 401 REELGRHIgylpQDVELFDGTIaeniaRFG-DA----DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1457 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1535
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
.
gi 110832837 1536 Q 1536
Cdd:COG4618 556 R 556
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
680-894 |
1.44e-26 |
|
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: 109.15 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 680 SWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPsfeATRSRNrysVAYAAQK- 758
Cdd:cd03259 9 TYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV---PPERRN---IGMVFQDy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 759 ---PWLlnaTVEENITFGSPFNKQRYKAVTDACSLqpdidLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVF 834
Cdd:cd03259 82 alfPHL---TVAENIAFGLKLRGVPKAEIRARVRE-----LLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 835 LDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREG 894
Cdd:cd03259 154 LDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
688-890 |
1.48e-26 |
|
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: 107.69 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVnesePSFEATRSRNRYSVAYAAQKPWLLNATVE 767
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA----DISQWDPNELGDHVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENItfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 847
Cdd:cd03246 94 ENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110832837 848 DHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 890
Cdd:cd03246 133 RALNQ--AIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1312-1533 |
2.48e-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: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLH--T 1384
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 LRSRLSIILQDPILFSGSIRFNLD--------PECKCTDDRLWEALEIAQLKNMVKSLPGGLDavvteggenFSVGQRQL 1456
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1457 FCLARAFVRKSSILIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESL 1533
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
371-585 |
3.31e-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: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 371 ASYYVTIETGINLRGALLAMIYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYN 450
Cdd:pfam00664 60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 451 LLG-SSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSL 529
Cdd:pfam00664 138 YYGwKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAG 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 530 KTFALYTSLSI-FMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPL 585
Cdd:pfam00664 218 IKKAVANGLSFgITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1013-1280 |
4.09e-26 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 110.00 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1013 YWLATWTSEysiNNTGKADQTY-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGL 1091
Cdd:cd18559 20 LWLLLWFDD---PVNGPQEHGQvYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1092 ILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVAlLPLGVAFYFIQKYFRVASKDLQELDDSTQLPL 1171
Cdd:cd18559 97 LVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLESVSKDPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1172 LCHFSETAEGLTTIRAFRHETRFKQRMLELTDtNNIAYLFLSAANRWLEVRTDYLGACIV-LTASIASISGSSNSGLVGL 1250
Cdd:cd18559 176 YKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVlFASFFAYVSRHSLAGLVAL 254
|
250 260 270
....*....|....*....|....*....|
gi 110832837 1251 GLLYALTITNYLNWVVRNLADLEVQMGAVK 1280
Cdd:cd18559 255 KVFYSLALTTYLNWPLNMSPEVITNIVAAE 284
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
669-893 |
5.21e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 107.82 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 669 DIAIKVTNGYFSWGSGLAT---LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVHW-----SNVNESEp 739
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVLIdgqdiSSLSERE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 740 sfeATRSRNRYsVAYAAQKPWLL-NATVEENITF-----GSPFNKQRYKAvtdacslqpdIDLLpfgDQTEIGERgIN-- 811
Cdd:COG1136 80 ---LARLRRRH-IGFVFQFFNLLpELTALENVALplllaGVSRKERRERA----------RELL---ERVGLGDR-LDhr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 812 ---LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFL-QDDKRTLVLVTHKLQYLTHADWIIAMKD 887
Cdd:COG1136 142 psqLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE--LLRELnRELGTTIVMVTHDPELAARADRVIRLRD 219
|
....*.
gi 110832837 888 GSVLRE 893
Cdd:COG1136 220 GRIVSD 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
668-890 |
1.41e-25 |
|
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: 105.96 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 668 EDIAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRS 746
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 rnrySVAYAAQKPWLLNATVEENItfgSPFNKQRYKAVTDACSlqpdidllpfgdqteIGERGINLSGGQRQRICVARAL 826
Cdd:cd03369 83 ----SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 827 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDkrTLVLVTHKLQYLTHADWIIAMKDGSV 890
Cdd:cd03369 141 LKRPRVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
979-1286 |
4.50e-25 |
|
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: 107.97 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 979 WKTCWRYLTSGGFFLLILmIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKAD---QTY---------------YVAGFS 1040
Cdd:cd18600 3 WNTYLRYITSHKSLIFVL-ILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPEsssNTYavivtftssyyvfyiYVGVAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1041 ILCGAGIF--LCLVTSLtvewmgLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRST 1118
Cdd:cd18600 82 SLLAMGFFrgLPLVHTL------ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1119 LLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRM 1198
Cdd:cd18600 156 LIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1199 LELTDTNNIAYLFLSAANRWLEVRTDYLGAC-IVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMG 1277
Cdd:cd18600 236 HKALNLHTANWFLYLSTLRWFQMRIEMIFVIfFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMR 315
|
....*....
gi 110832837 1278 AVKKVNSFL 1286
Cdd:cd18600 316 SVSRIFKFI 324
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1329-1477 |
5.49e-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: 102.34 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1329 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG-SIRFNL 1407
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1408 DPECKCT-------DDRLWEALEiaQLknmvkSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1477
Cdd:pfam00005 81 RLGLLLKglskrekDARAEEALE--KL-----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
650-899 |
1.03e-24 |
|
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: 111.76 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 650 YHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV 729
Cdd:TIGR01193 452 YLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 730 HWSNVNESEPSfeatRSRNRYSVAYAAQKPWLLNATVEENITFGSPFN--KQRYKAVTDACSLQPDIDLLPFGDQTEIGE 807
Cdd:TIGR01193 532 LLNGFSLKDID----RHTLRQFINYLPQEPYIFSGSILENLLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTELSE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 808 RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILkFLQDdkRTLVLVTHKLQYLTHADWIIAMKD 887
Cdd:TIGR01193 608 EGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT-ITEKKIVNNLL-NLQD--KTIIFVAHRLSVAKQSDKIIVLDH 683
|
250
....*....|..
gi 110832837 888 GSVLREGTLKDI 899
Cdd:TIGR01193 684 GKIIEQGSHDEL 695
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1312-1538 |
1.07e-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: 104.55 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVIDGIDISKLPLHtLRS 1387
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMlaglLKPDSGSILIDGEDVRKEPRE-ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQDPILFSG-SIRFNLDPECKCTDDRLWEALEIAQlkNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1466
Cdd:COG4555 75 QIGVLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIE--ELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1467 SSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQEN 1538
Cdd:COG4555 151 PKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
688-899 |
1.07e-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: 111.76 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQTLEGKVHWSNVNESEPsfeATRSRNrysVAYAAQKPWLLNAT 765
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQHGQVLVDGVDLAIADP---AWLRRQ---MGVVLQENVLFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 844
Cdd:TIGR01846 547 IRDNIALCNPgAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDY 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 845 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:TIGR01846 627 E-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
672-906 |
1.08e-24 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 104.51 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSF-EATRSRNRY 750
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 SVAYaaQKPWLLNA-TVEENITFG----SPFNKQRYKAVT----DACSLQPDIDLLPfgdqteigergINLSGGQRQRIC 821
Cdd:cd03261 80 GMLF--QSGALFDSlTVFENVAFPlrehTRLSEEEIREIVleklEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 822 VARALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKfLQDDKR-TLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASG-VIDDLIRS-LKKELGlTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEEL 224
|
....*..
gi 110832837 900 QTKDVEL 906
Cdd:cd03261 225 RASDDPL 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
671-899 |
1.52e-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: 104.50 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 671 AIKVTN---GYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnvNESEPSFEATRSR 747
Cdd:COG1124 1 MLEVRNlsvSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF---DGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 748 NRySVAYAAQKPWL-LNA--TVEENIT-----FGSPFNKQRYKAVTDACSLQPDI-DLLPfgDQteigerginLSGGQRQ 818
Cdd:COG1124 78 RR-RVQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYP--HQ---------LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 819 RICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLRE 893
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEE 220
|
....*.
gi 110832837 894 GTLKDI 899
Cdd:COG1124 221 LTVADL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
657-907 |
3.74e-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: 108.45 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 657 QSTRRLRPAETEDIAIKVTN---GYFSWGSGLAT-LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS 732
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRNlskRYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 733 NVNESEPSFEATRSRNRySVAYAAQKPWL-LNA--TVEENITFG-------SPfnKQRYKAVT---DACSLQPD-IDLLP 798
Cdd:COG1123 326 GKDLTKLSRRSLRELRR-RVQMVFQDPYSsLNPrmTVGDIIAEPlrlhgllSR--AERRERVAellERVGLPPDlADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 799 FGdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKL- 873
Cdd:COG1123 403 HE-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLa 466
|
250 260 270
....*....|....*....|....*....|....*.
gi 110832837 874 --QYLthADWIIAMKDGSVLREGTLKDIQTKDVELY 907
Cdd:COG1123 467 vvRYI--ADRVAVMYDGRIVEDGPTEEVFANPQHPY 500
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1312-1535 |
3.81e-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: 103.34 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1389
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPIlfsGSI--RFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDAVvteG-GENF--------SVGQRQLFC 1458
Cdd:COG1124 82 QMVFQDPY---ASLhpRHTVD-------RILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESL 1533
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
..
gi 110832837 1534 LA 1535
Cdd:COG1124 227 LA 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
688-890 |
3.95e-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: 102.55 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnVNESEPsfeATRSRNRY---SVAYAAQKPWLLNA 764
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV----LLDGKP---ISQYEHKYlhsKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFG---SPFnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:cd03248 103 SLQDNIAYGlqsCSF--ECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110832837 842 LDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSV 890
Cdd:cd03248 181 LDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1312-1536 |
4.02e-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: 108.45 E-value: 4.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLK---PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTL 1385
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 RSRLSIILQDPilfSGSirfnLDPECKCTDDrLWEALEI------AQLKNMVKSLpggLDAVvteG----------GEnF 1449
Cdd:COG1123 341 RRRVQMVFQDP---YSS----LNPRMTVGDI-IAEPLRLhgllsrAERRERVAEL---LERV---GlppdladrypHE-L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1450 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRG 1522
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|....
gi 110832837 1523 NILEYDTPESLLAQ 1536
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
672-899 |
4.09e-24 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 102.76 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS--NVNESEPSfeatrsRNR 749
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgeDIREQDPV------ELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 750 YSVAYAAQKPWLL-NATVEENITFGSPFNK-QRYKAVTDACSLQPDIDLLPfgdqTEIGER-GINLSGGQRQRICVARAL 826
Cdd:cd03295 75 RKIGYVIQQIGLFpHMTVEENIALVPKLLKwPKEKIRERADELLALVGLDP----AEFADRyPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 827 YQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
672-905 |
4.51e-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: 103.01 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAtrsrnRYS 751
Cdd:COG4555 2 IEVENLSKKYGKVPA-LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-----RRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWL-LNATVEENITFGSPFN---KQRYKAVTDacSLQPDIDLLPFGDQTeIGErginLSGGQRQRICVARALY 827
Cdd:COG4555 76 IGVLPDERGLyDRLTVRENIRYFAELYglfDEELKKRIE--ELIELLGLEEFLDRR-VGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 828 QNTNIVFLDDPFSALDIhLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVE 905
Cdd:COG4555 149 HDPKVLLLDEPTNGLDV-MARRLLRE-ILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
672-903 |
5.81e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 108.57 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNVNESEPSFEATRSRn 748
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDID--EGEILLDGHDLRDYTLASLRNQ- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 749 rysVAYAAQKPWLLNATVEENITFGSpfnKQRY------KAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICV 822
Cdd:PRK11176 419 ---VALVSQNVHLFNDTIANNIAYAR---TEQYsreqieEAARMAYAMD-FINKMDNGLDTVIGENGVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 823 ARALYQNTNIVFLDDPFSALDIHlSDHLMQEGiLKFLQDDKRTLVlVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTK 902
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTE-SERAIQAA-LDELQKNRTSLV-IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
.
gi 110832837 903 D 903
Cdd:PRK11176 569 N 569
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
672-907 |
6.35e-24 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 102.26 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnRYS 751
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL-RRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWLLN-ATVEENITFG------------SPFNKQRYKAvtdACSLQPDIDLLPFGDQteigeRGINLSGGQRQ 818
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGrlgrrstwrslfGLFPKEEKQR---ALAALERVGLLDKAYQ-----RADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 819 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLK 897
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVM-DLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPA 230
|
250
....*....|.
gi 110832837 898 DIQTKDV-ELY 907
Cdd:cd03256 231 ELTDEVLdEIY 241
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
688-894 |
7.52e-24 |
|
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: 100.08 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPS-FEATRSRnrySVAYAAQKPWLLNATV 766
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT---LDGVPVSdLEKALSS---LISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENItfgspfnkqrykavtdacslqpdidllpfgdqteigerGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 846
Cdd:cd03247 92 RNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110832837 847 SDHLMqEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREG 894
Cdd:cd03247 134 ERQLL-SLIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1312-1538 |
1.29e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.38 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPI-LFSGS-----IRFNLdpECKCTD-----DRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLA 1460
Cdd:PRK13632 88 IFQNPDnQFIGAtveddIAFGL--ENKKVPpkkmkDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1461 RAFVRKSSILIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQEN 1538
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
377-917 |
1.54e-23 |
|
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: 107.73 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 377 IETGINlrGALLAMIYNKILRL--------STSNLSMGEMTLGQINNLVAIET-NQLMWFLFLCPNLWAMpvqiimgviL 447
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLGLM---------F 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 448 LYNLlgSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLK--------LYAWEHIFCKSVE 519
Cdd:TIGR03797 272 YYSW--KLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 520 ---ETRMKE--LSSLKT-FALYTSLSIFMNAAIPIAAV---LATFVTHAYASGNNLKPAEAFASlSLFHIL-VTPLFlls 589
Cdd:TIGR03797 350 lelSAQRIEnlLTVFNAvLPVLTSAALFAAAISLLGGAglsLGSFLAFNTAFGSFSGAVTQLSN-TLISILaVIPLW--- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 590 tvvrfavkaiisvqklnefllsdeigddswrtgESSLP-FESckkhtgvQPKT-INRKQPGRYHLdsyeqstrrlrpaet 667
Cdd:TIGR03797 426 ---------------------------------ERAKPiLEA-------LPEVdEAKTDPGKLSG--------------- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 668 ediAIKVTNGYFSWG-SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRS 746
Cdd:TIGR03797 451 ---AIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 RnrysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARAL 826
Cdd:TIGR03797 528 Q----LGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 827 YQNTNIVFLDDPFSALdihlsDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVEL 906
Cdd:TIGR03797 604 VRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLF 678
|
570
....*....|.
gi 110832837 907 YEhwktLMNRQ 917
Cdd:TIGR03797 679 AQ----LARRQ 685
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
688-899 |
2.11e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.52 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRysVAYAAQKPWL-LNATV 766
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVR---VLGEDVARDPAEVRRR--IGYVPQEPALyPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITF-------GSPFNKQRYKAVTDACSLQPDIDllpfgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:COG1131 91 RENLRFfarlyglPRKEARERIDELLELFGLTDAAD-----------RKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 840 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHklqYLTHA----DWIIAMKDGSVLREGTLKDI 899
Cdd:COG1131 160 SGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
672-888 |
3.20e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 98.41 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRys 751
Cdd:cd03229 1 LELKNVSKRYGQKTV-LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWLL-NATVEENITFGspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNT 830
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 831 NIVFLDDPFSALDIhlsdhLMQEGILKFLQD----DKRTLVLVTHKLQYLTH-ADWIIAMKDG 888
Cdd:cd03229 120 DVLLLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
672-899 |
3.29e-23 |
|
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: 99.95 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHWSNVNESEPSFEATRS 746
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 RNRysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAC---SLQpDIDLLP-FGDQTEIGErginLSGGQRQRICV 822
Cdd:cd03260 80 RRR--VGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERveeALR-KAALWDeVKDRLHALG----LSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 823 ARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFlqDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1312-1538 |
5.38e-23 |
|
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: 100.12 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffRMVDIFDGKIVIDGIDISKLPLHTLRSRL 1389
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLlrALA--GLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPIL-FSGSIR--------------FNLDPEckctDDRL-WEALE---IAQLKN-MVKSLPGGldavvteggenf 1449
Cdd:COG1120 78 AYVPQEPPApFGLTVRelvalgryphlglfGRPSAE----DREAvEEALErtgLEHLADrPVDELSGG------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1450 svgQRQLFCLARAFVRKSSILIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNI 1524
Cdd:COG1120 142 ---ERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRI 216
|
250
....*....|....
gi 110832837 1525 LEYDTPESLLAQEN 1538
Cdd:COG1120 217 VAQGPPEEVLTPEL 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
684-880 |
5.67e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnvnesepsfeatRSRNRySVAYAAQK---PW 760
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------------RAGGA-RVAYVPQRsevPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 761 LLNATVEENITFG--------SPFNKQRYKAVTDACSlqpDIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNI 832
Cdd:NF040873 69 SLPLTVRDLVAMGrwarrglwRRLTRDDRAAVDDALE---RVGLADLAGR-QLGE----LSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110832837 833 VFLDDPFSALDIHLSDHLmqEGILKFLQDDKRTLVLVTHKLQYLTHAD 880
Cdd:NF040873 141 LLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDLELVRRAD 186
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
688-909 |
1.75e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.42 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 767
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ----VALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSPF-NKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 846
Cdd:TIGR00958 573 ENIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE- 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 847 SDHLMQEgiLKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTkDVELYEH 909
Cdd:TIGR00958 652 CEQLLQE--SRSRAS--RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME-DQGCYKH 709
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
688-894 |
3.46e-22 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 96.81 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfEATRSRNRYSVAYAAQKPWL-LNA-- 764
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRKIRRKEIQMVFQDPMSsLNPrm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENIT-----FGSPFNKQRYKAVT--DACSLQPDIDLL---PFGdqteigerginLSGGQRQRICVARALYQNTNIVF 834
Cdd:cd03257 100 TIGEQIAeplriHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 835 LDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKL---QYLthADWIIAMKDGSVLREG 894
Cdd:cd03257 169 ADEPTSALDVSVQAQILD--LLKKLQEELgLTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
671-909 |
4.42e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.76 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 671 AIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHW--SNVNESEPsfeatRSR 747
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT-SGEILIggRDVTDLPP-----KDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 748 NrysVAYAAQKPWLL-NATVEENITFG------SPfnKQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRI 820
Cdd:COG3839 76 N---IAMVFQSYALYpHMTVYENIAFPlklrkvPK--AEIDRRVREAAEL---LGLEDLLDR-----KPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 821 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdi 899
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAE-IKRLHRRLGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPE-- 219
|
250
....*....|
gi 110832837 900 qtkdvELYEH 909
Cdd:COG3839 220 -----ELYDR 224
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
688-895 |
6.69e-22 |
|
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: 102.71 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVnesePSFEATRSRNRYSVAYAAQKPWLLNATVE 767
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGI----PREEIPREVLANSVAMVDQDIFLFEGTVR 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSPF--NKQRYKAVTDACsLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-- 843
Cdd:TIGR03796 571 DNLTLWDPTipDADLVRACKDAA-IHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDpe 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110832837 844 --IHLSDHLMQEGIlkflqddkrTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:TIGR03796 650 teKIIDDNLRRRGC---------TCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
688-899 |
7.48e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.07 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtLE----GKVHW------SNVnesepsfeATRSRNrysVAYAAQ 757
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLngrdlfTNL--------PPRERR---VGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 758 KPWLL-NATVEENITFG---SPFNKQRYKA-VTDACSLqpdIDLLPFGD----QteigerginLSGGQRQRICVARALYQ 828
Cdd:COG1118 83 HYALFpHMTVAENIAFGlrvRPPSKAEIRArVEELLEL---VQLEGLADrypsQ---------LSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 829 NTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRW-LRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
690-899 |
2.75e-21 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 95.40 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLL-NATVEE 768
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 769 NITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVARALYQNTNIVFLDDPFSALD- 843
Cdd:cd03294 122 NVAFGLEVQgvprAEREERAAEALEL---VGLEGWEHK-YPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDp 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 844 -IHLSdhlMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03294 194 lIRRE---MQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
667-906 |
3.87e-21 |
|
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: 94.28 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 667 TEDIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRS 746
Cdd:COG1127 1 MSEPMIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 -RNRYSVAYaaQKPWLLNA-TVEENITFG-------SPfnKQRYKAVT---DACSLQPDIDLLPfgdqteiGErginLSG 814
Cdd:COG1127 80 lRRRIGMLF--QGGALFDSlTVFENVAFPlrehtdlSE--AEIRELVLeklELVGLPGAADKMP-------SE----LSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 815 GQRQRICVARALYQNTNIVFLDDPFSALDIHLS---DHLMQEgilkfLQDD-KRTLVLVTHKLQYL-THADWIIAMKDGS 889
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSaviDELIRE-----LRDElGLTSVVVTHDLDSAfAIADRVAVLADGK 219
|
250
....*....|....*..
gi 110832837 890 VLREGTLKDIQTKDVEL 906
Cdd:COG1127 220 IIAEGTPEELLASDDPW 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
666-908 |
4.15e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.82 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 666 ETEDIAIKVTNGYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAT 744
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 745 RSRnrysVAYAAQKP--WLLNATVEENITFG-----SPFNKQRYKaVTDACSlqpDIDLLPFGDQTEigergINLSGGQR 817
Cdd:PRK13648 82 RKH----IGIVFQNPdnQFVGSIVKYDVAFGlenhaVPYDEMHRR-VSEALK---QVDMLERADYEP-----NALSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 818 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLTHADWIIAMKDGSVLREGTL 896
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD--LVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
250
....*....|..
gi 110832837 897 KDIQTKDVELYE 908
Cdd:PRK13648 227 TEIFDHAEELTR 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
672-890 |
4.19e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 92.08 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRys 751
Cdd:cd03230 1 IEVRNLSKRYGKKTA-LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK---VLGKDIKKEPEEVKRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWLL-NATVEENItfgspfnkqrykavtdacslqpdidllpfgdqteigergiNLSGGQRQRICVARALYQNT 830
Cdd:cd03230 75 IGYLPEEPSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 831 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSV 890
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1312-1528 |
1.19e-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: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1387
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLErpdsGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCL 1459
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKLRGVPKAEiraRVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1460 ARAFVRKSSILIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1528
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
671-877 |
1.63e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.18 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 671 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQT---LEGKVHWSNVNESEPSFEATR 745
Cdd:PRK14258 7 AIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELESevrVEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SRNRYSVAYAaqKPWLLNATVEENITFGSPFNKQRYKAVTDAC--SLQPDIDLLpfgDQTE--IGERGINLSGGQRQRIC 821
Cdd:PRK14258 86 LRRQVSMVHP--KPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIveSALKDADLW---DEIKhkIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 822 VARALYQNTNIVFLDDPFSALDIHLS---DHLMQEGILKflqdDKRTLVLVTHKLQYLT 877
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVS 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
688-901 |
1.78e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRYsVAYAAQKPWLLNA-TV 766
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF---LGDKPISMLSSRQLARR-LALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFG-SPFNK------QRYKAVTDACSLQPDIDllpfgdqtEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDP 838
Cdd:PRK11231 94 RELVAYGrSPWLSlwgrlsAEDNARVNQAMEQTRIN--------HLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 839 FSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDIQT 901
Cdd:PRK11231 166 TTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1313-1525 |
1.87e-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: 90.57 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1313 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSII 1392
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1393 LQdpILfsgsirfnldpeckctddrlwEALEIAQLKN-MVKSLPGGldavvteggenfsvgQRQLFCLARAFVRKSSILI 1471
Cdd:cd03214 79 PQ--AL---------------------ELLGLAHLADrPFNELSGG---------------ERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1472 MDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILTADLVIVMKRGNIL 1525
Cdd:cd03214 121 LDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
703-913 |
1.92e-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: 94.48 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 703 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEaTRSRNRYSVAYAAqkpwLLNATVEENITFGSPFNK---- 778
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-LRHINMVFQSYAL----FPHMTVEENVAFGLKMRKvpra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 779 QRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKF 858
Cdd:TIGR01187 76 EIKPRVLEALRL---VQLEEFADR-----KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE--LKT 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 859 LQDD-KRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEHWKTL 913
Cdd:TIGR01187 146 IQEQlGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPE-------EIYEEPANL 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
664-895 |
5.45e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.05 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 664 PAETEDIAIKVTNGYFSW-GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFE 742
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 743 ATRSrnrySVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQpdiDLLPfGDQ---TEIGERGINLSGGQRQ 818
Cdd:PRK11160 411 ALRQ----AISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLE---KLLE-DDKglnAWLGEGGRQLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 819 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILEL-LAEHAQN--KTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1249-1536 |
7.31e-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: 95.14 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1249 GLGLLYaltITNYLNwVVRNLAD----LE----VQMGAVKKVnsFLTM---------ESEnyegtmdPSQVPEHWPQEGE 1311
Cdd:COG4172 207 GMALLL---ITHDLG-VVRRFADrvavMRqgeiVEQGPTAEL--FAAPqhpytrkllAAE-------PRGDPRPVPPDAP 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 --IKIHDLCVRYENN---LKPVLKHVKAY------IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDGIDISKL 1380
Cdd:COG4172 274 plLEARDLKVWFPIKrglFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1381 P---LHTLRSRLSIILQDPilFsGSirfnLDPeckctddRL------WEALEI-------AQLKNMVKSLPG--GLDAVV 1442
Cdd:COG4172 353 SrraLRPLRRRMQVVFQDP--F-GS----LSP-------RMtvgqiiAEGLRVhgpglsaAERRARVAEALEevGLDPAA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1443 -----TEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATenilQKVVMTAFA---------------DRTVV- 1501
Cdd:COG4172 419 rhrypHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehglaylfishDLAVVr 490
|
330 340 350
....*....|....*....|....*....|....*
gi 110832837 1502 TIAHRvhtiltadlVIVMKRGNILEYDTPESLLAQ 1536
Cdd:COG4172 491 ALAHR---------VMVMKDGKVVEQGPTEQVFDA 516
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
688-871 |
7.64e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 89.46 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPsfeatRSRNRYSVAYAAQKPWLLNA-TV 766
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-----REDYRRRLAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITF-----GSPFNKQRYKAVTDACSLQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:COG4133 93 RENLRFwaalyGLRADREAIDEALEAVGLAGLADL-PVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 110832837 842 LDI--------HLSDHLMQEGIlkflqddkrtLVLVTH 871
Cdd:COG4133 162 LDAagvallaeLIAAHLARGGA----------VLLTTH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
671-899 |
7.94e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 94.97 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 671 AIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNVNESEPSfEATRS 746
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELS-EALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 RnrySVAYAAQKPW--LLNATVEENITFGSpfnkqRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVA 823
Cdd:COG1123 83 R---RIGMVFQDPMtqLNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPHqLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 824 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDK-RTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 899
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILD--LLRELQRERgTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
664-874 |
1.24e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 664 PAETEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHWSNVNESE 738
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLA-VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 739 PSFEATRSRNRYSVAYaaQKPWLLNATVEENITFGSPFNKqrYKavtdacslqpdidllpfGDQTEIGER---------- 808
Cdd:PRK14243 82 PDVDPVEVRRRIGMVF--QKPNPFPKSIYDNIAYGARING--YK-----------------GDMDELVERslrqaalwde 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 809 --------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDhLMQEGILKFLQDDkRTLVLVTHKLQ 874
Cdd:PRK14243 141 vkdklkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD-PIST-LRIEELMHELKEQ-YTIIIVTHNMQ 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
690-894 |
1.37e-19 |
|
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: 88.89 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPtGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNV--NESEPSFEATRSRNRysVAYAAQKPWLL-NATV 766
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLPPQQRK--IGLVFQQYALFpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFGSPFN-----KQRYKAVTDACSLQPdidllpfgdqteIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFS 840
Cdd:cd03297 93 RENLAFGLKRKrnredRISVDELLDLLGLDH------------LLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 841 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKL---QYLthADWIIAMKDGSVLREG 894
Cdd:cd03297 161 ALDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
678-871 |
1.66e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.92 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 678 YFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfeATRsrnrysvAYAAQ 757
Cdd:COG4525 13 YPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--ADR-------GVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 758 K----PWLlnaTVEENITFGSPFNK----QRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVARALYQN 829
Cdd:COG4525 84 KdallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VGLADFARR-RIWQ----LSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110832837 830 TNIVFLDDPFSALDIhLSDHLMQEGILKFLQDDKRTLVLVTH 871
Cdd:COG4525 153 PRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
663-895 |
2.26e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.01 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 663 RPAETEDIAIKvtNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFE 742
Cdd:PRK10790 334 RPLQSGRIDID--NVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 743 ATRSrnrySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICV 822
Cdd:PRK10790 412 VLRQ----GVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 823 ARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQ--DDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSG-----TEQAIQQALAavREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1312-1536 |
4.23e-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: 88.02 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLK--PVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---L 1382
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsGSVLVDGTDLTLLSgkeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1383 HTLRSRLSIILQDPILFS-----GSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQR 1454
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1455 QLFCLARAFVRKSSILIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTP 1530
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 110832837 1531 ESLLAQ 1536
Cdd:cd03258 226 EEVFAN 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
672-890 |
4.34e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 87.31 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS--NVNESEPSfeatrSRNr 749
Cdd:cd03301 1 VELENVTKRFGNVTA-LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrDVTDLPPK-----DRD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 750 ysVAYAAQKPWLL-NATVEENITFGSPFNKQRY----KAVTDACSLQpDIDLLpfgdqteIGERGINLSGGQRQRICVAR 824
Cdd:cd03301 74 --IAMVFQNYALYpHMTVYDNIAFGLKLRKVPKdeidERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 825 ALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSV 890
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAE-LKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1312-1524 |
4.38e-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: 87.55 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYEN--NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHTL 1385
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL----LNILGGLDrptsGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 ----RSRLSIILQD---------------PILFSGSIRfnldPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvtegg 1446
Cdd:cd03255 77 aafrRRHIGFVFQSfnllpdltalenvelPLLLAGVPK----KERR---ERAEELLERVGLGDRLNHYPSEL-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1447 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILTADLVIVMKRG 1522
Cdd:cd03255 142 ---SGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
..
gi 110832837 1523 NI 1524
Cdd:cd03255 217 KI 218
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
690-927 |
4.88e-19 |
|
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: 93.03 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEpsfeATRSRNRYSVAYAAQKPWLLNATVEEN 769
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINT----VTRESLRKSIATVFQDAGLFNRSIREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 770 ITFG--SPFNKQRYKAvTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 847
Cdd:TIGR01192 429 IRLGreGATDEEVYEA-AKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVE-T 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 848 DHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEA 927
Cdd:TIGR01192 507 EARVKNAIDALRKN--RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPATKPLRK 584
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
688-895 |
5.95e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 5.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHWS--NVNESEPsfeatrsrNRYSVAYAAQK----PW 760
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLDgrDVTGLPP--------EKRNVGMVFQDyalfPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 761 LlnaTVEENITFG------SPfnKQRYKAVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIV 833
Cdd:COG3842 92 L---TVAENVAFGlrmrgvPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 834 FLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKlQY--LTHADWIIAMKDGSVLREGT 895
Cdd:COG3842 158 LLDEPLSALDAKLREEMREE--LRRLQRElGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
663-874 |
9.75e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 87.78 E-value: 9.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 663 RPAETEDIAIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNVNES 737
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 738 EPSFEATRSRNRysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDacslqpdidllpfgdqtEIGER--------- 808
Cdd:COG1117 82 DPDVDVVELRRR--VGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELD-----------------EIVEEslrkaalwd 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 809 ---------GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDH---LMQEgiLKflqdDKRTLVLVTHKLQ 874
Cdd:COG1117 143 evkdrlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKieeLILE--LK----KDYTIVIVTHNMQ 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
682-904 |
1.57e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.35 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 682 GSGLATLS-NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNVNESEpsfeatrsrnRYSVAYAAQKPW 760
Cdd:PRK10253 16 GYGKYTVAeNLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQ----------HYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 761 LL--NATVEENITFGSPFNKQRYKAvtdacslQP--------DIDLLPFGDQ----TEIGERGIN-LSGGQRQRICVARA 825
Cdd:PRK10253 85 LLaqNATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 826 LYQNTNIVFLDDPFSALDIhlsDHlmQEGILKFLQDDKR----TLVLVTHKL----QYLTHadwIIAMKDGSVLREGTLK 897
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnqacRYASH---LIALREGKIVAQGAPK 229
|
....*..
gi 110832837 898 DIQTKDV 904
Cdd:PRK10253 230 EIVTAEL 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1327-1535 |
1.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1327 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI---DISKLPlhTLRSRLSIILQDP-ILFSG- 1401
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQ--GIRKLVGIVFQNPeTQFVGr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1402 SIRFNL--DPECKCTddrlwEALEIAQLKNMVKSlPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1479
Cdd:PRK13644 94 TVEEDLafGPENLCL-----PPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1480 DMAT-ENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1535
Cdd:PRK13644 168 DPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1312-1522 |
2.19e-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: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHT--L 1385
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAGLEepdsGSILIDGEDLTDLEDELppL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 RSRLSIILQDPILFSGsirfnldpeckctddrlweaLEIAQlkNMVKSLPGGldavvteggenfsvgQRQLFCLARAFVR 1465
Cdd:cd03229 75 RRRIGMVFQDFALFPH--------------------LTVLE--NIALGLSGG---------------QQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1466 KSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILT-ADLVIVMKRG 1522
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
672-913 |
2.45e-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: 85.75 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESE-PSFEatRSRNRY 750
Cdd:cd03300 1 IELENVSKFYGGFVA-LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHK--RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 SVAYAaqkpwLL-NATVEENITFG---SPFNKQRYKA-VTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVAR 824
Cdd:cd03300 78 FQNYA-----LFpHLTVFENIAFGlrlKKLPKAEIKErVAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 825 ALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIqtk 902
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLE--LKRLQKElGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI--- 218
|
250
....*....|.
gi 110832837 903 dvelYEHWKTL 913
Cdd:cd03300 219 ----YEEPANR 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1526 |
2.65e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.12 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISKLPLHTLR 1386
Cdd:PRK14247 4 IEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1387 SRLSIILQ--DPI----LFSG---SIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLpggLDAVVTEggenFSVGQRQL 1456
Cdd:PRK14247 82 RRVQMVFQipNPIpnlsIFENvalGLKLNrLVKSKKELQERVRWALEKAQLWDEVKDR---LDAPAGK----LSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 1457 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtiltADLVIVMKRGNILE 1526
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
684-874 |
3.00e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEatrsrnRYSV-AYAAQKPWLl 762
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE------RGVVfQNEGLLPWR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 naTVEENITFGspfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:PRK11248 86 --NVQDNVAFG-----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|...
gi 110832837 842 LDIHLSDHlMQEGILKFLQDDKRTLVLVTHKLQ 874
Cdd:PRK11248 159 LDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
688-885 |
4.95e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 767
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ----VSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSPFNKQRykavtdacsLQPDI---DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALD 843
Cdd:PRK10247 99 DNLIFPWQIRNQQ---------PDPAIfldDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110832837 844 IHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM 885
Cdd:PRK10247 170 ES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
667-899 |
5.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.81 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 667 TEDIAIKVTNGYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATR 745
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SRnrysVAYAAQKP--WLLNATVEENITFG---SPFNKQRYKAVTDACSLQPDI-DLLPFGDQteigergiNLSGGQRQR 819
Cdd:PRK13632 83 KK----IGIIFQNPdnQFIGATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMeDYLDKEPQ--------NLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 820 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKD 898
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKK--IMVDLRKTrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
.
gi 110832837 899 I 899
Cdd:PRK13632 229 I 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1327-1522 |
5.47e-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: 84.69 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1327 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR----LSIILQDPILFSGS 1402
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1403 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM- 1481
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIh 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110832837 1482 ATENILQKVVMTAFAD--RTVVTIAHRVHTILTADLVIVMKRG 1522
Cdd:cd03290 175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
688-899 |
7.41e-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: 84.55 E-value: 7.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTlEGKVHWSNVNESEPSFEATRSRnRYSVAYAAQKPWLLNA-T 765
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPT-SGSVLVDGTDLTLLSGKELRKA-RRRIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITF-----GSPfNKQRYKAVTDacslqpdidLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:cd03258 99 VFENVALpleiaGVP-KAEIEERVLE---------LLELVGLEDKADAYPaQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 840 SALDIHLSDhlmqeGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03258 169 SALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1312-1538 |
7.52e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 84.76 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFR----MVDIFDGKIVIDGidiskLPLHTLRS 1387
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTL----LKailgLLPPTSGTVRLFG-----KPPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQD-------PIL--------FSGSIRF--NLDPECKctdDRLWEALE---IAQLKN-MVKSLpggldavvtegg 1446
Cdd:COG1121 76 RIGYVPQRaevdwdfPITvrdvvlmgRYGRRGLfrRPSRADR---EAVDEALErvgLEDLADrPIGEL------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1447 enfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGnI 1524
Cdd:COG1121 141 ---SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRG-L 216
|
250
....*....|....
gi 110832837 1525 LEYDTPESLLAQEN 1538
Cdd:COG1121 217 VAHGPPEEVLTPEN 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
681-872 |
8.14e-18 |
|
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: 84.24 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 681 WGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVHwsnVNESEPSfeatRSRNRYSVAYAAQ 757
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQIL---FNGQPRK----PDQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 758 KPWLL-NATVEENITFGSPF-----NKQRYKAVTDACSLQPDIDLLPFGdqteiGERGINLSGGQRQRICVARALYQNTN 831
Cdd:cd03234 89 DDILLpGLTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110832837 832 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 872
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
687-922 |
9.01e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.83 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ---TLEGKVHWSNVNESEPSFEATRSRNRYSVAYaaQKPWL 761
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNpevTITGSIVYNGHNIYSPRTDTVDLRKEIGMVF--QQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:PRK14239 98 FPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 840 SALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIqtkdvelyehwktLMNRQD 918
Cdd:PRK14239 177 SALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM-------------FMNPKH 240
|
....
gi 110832837 919 QELE 922
Cdd:PRK14239 241 KETE 244
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
691-909 |
9.86e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 86.70 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 691 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNV--NESEPSFEATRSRNRysVAYAAQKPWLL-NATVE 767
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlFDSRKGIFLPPEKRR--IGYVFQEARLFpHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFG-----SPFNKQRYKAVTDACSLQPDIDLLPfGDqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSAL 842
Cdd:TIGR02142 94 GNLRYGmkrarPSERRISFERVIELLGIGHLLGRLP-GR----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 843 DIHLSDHlmqegILKFLQDDKRTL----VLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQ-TKDVELYEH 909
Cdd:TIGR02142 163 DDPRKYE-----ILPYLERLHAEFgipiLYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWaSPDLPWLAR 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
671-899 |
1.01e-17 |
|
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: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 671 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWsnVNESEPSFEATRSRNry 750
Cdd:cd03296 2 SIEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-L--FGGEDATDVPVQERN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 sVAYAAQKPWLL-NATVEENITFGSPFNKQRYKAVTDACSLQPDiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQ 828
Cdd:cd03296 76 -VGFVFQHYALFrHMTVFDNVAFGLRVKPRSERPPEAEIRAKVH-ELLKLVQLDWLADRYPAqLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 829 NTNIVFLDDPFSALDIHLSDHLmqEGILKFLQDDKR-TLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKEL--RRWLRRLHDELHvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
692-894 |
1.18e-17 |
|
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: 83.31 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 692 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--HWSNVNESEPSfeatrsrnRYSVAYAAQKPWLL-NATVEE 768
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVliNGVDVTAAPPA--------DRPVSMLFQENNLFaHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 769 NITFG-SP---FNKQRYKAVTDAcslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 844
Cdd:cd03298 90 NVGLGlSPglkLTAEDRQAIEVA--------LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 845 HLSDHlMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 894
Cdd:cd03298 162 ALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
690-903 |
1.33e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 83.65 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNesepsfeatrsrnrYSVAYAAQKP---------- 759
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD--------------LTALPPAERPvsmlfqennl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 760 -WLLnaTVEENITFG-------SPFNKQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQNTN 831
Cdd:COG3840 83 fPHL--TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 832 IVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKD 903
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLD--LVDELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1307-1506 |
1.45e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.33 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1307 PQEGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVI-DGIDISKLP 1381
Cdd:COG4178 358 SEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAIaglwPYGSGRIARpAGARVLFLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1382 lhtlrsrlsiilQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNmvksLPGGLDaVVTEGGENFSVGQRQLFC 1458
Cdd:COG4178 433 ------------QRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH----LAERLD-EEADWDQVLSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1506
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1312-1526 |
2.02e-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: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYE--NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAffrMVDIFD-GKIVIDGIDISKLP---LH 1383
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILG---GLDRPTsGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1384 TLRSR-LSIILQDpilfsgsirFNLDPE-----------------CKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteg 1445
Cdd:COG1136 82 RLRRRhIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQL------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1446 genfSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFAD---RTVVTIAHRVHTILTADLVIVMKR 1521
Cdd:COG1136 146 ----SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTIVMVTHDPELAARADRVIRLRD 219
|
....*
gi 110832837 1522 GNILE 1526
Cdd:COG1136 220 GRIVS 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1312-1524 |
2.22e-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: 81.29 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVIDGIDISKLPlHTLRS 1387
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTL----IKIilglLKPDSGEIKVLGKDIKKEP-EEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQDPILFSG-SIRFNLDpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRK 1466
Cdd:cd03230 74 RIGYLPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1467 SSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1524
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
688-895 |
2.43e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 87.57 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSL--LL---------AILGEMQTLEgkvhwsnvnesepsfEATRSRNRYSVAYAA 756
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLarLLfrfydvtsgRILIDGQDIR---------------DVTQASLRAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 757 QKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 835
Cdd:COG5265 439 QDTVLFNDTIAYNIAYGRPdASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 836 DDPFSALDIHlSDHLMQEGiLKFLQDDKRTLVlVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:COG5265 519 DEATSALDSR-TERAIQAA-LREVARGRTTLV-IAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1312-1538 |
2.74e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.88 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYEN-----NLKpvlkhvkayIKPGQKVGICGRTGSGKSSLS--LAFFRMVDifDGKIVIDGIDISKLPLHT 1384
Cdd:COG3840 2 LRLDDLTYRYGDfplrfDLT---------IAAGERVAILGPSGAGKSTLLnlIAGFLPPD--SGRILWNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 lrsR-LSIILQDPILFSG-SIRFN----LDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQ 1455
Cdd:COG3840 71 ---RpVSMLFQENNLFPHlTVAQNiglgLRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQL-----------SGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1456 LFCLARAFVRKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPES 1532
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*.
gi 110832837 1533 LLAQEN 1538
Cdd:COG3840 217 LLDGEP 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
679-895 |
3.33e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 679 FSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNVNESEpsfeATRSRNRYSVAYAAQ 757
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDpQSGRILIDGTDIRT----VTRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 758 KPWLLNATVEENITFGSP--FNKQRYKAVTDACSLqpD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 834
Cdd:PRK13657 417 DAGLFNRSIEDNIRVGRPdaTDEEMRAAAERAQAH--DfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 835 LDDPFSALDIHLSDHLmQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT 895
Cdd:PRK13657 495 LDEATSALDVETEAKV-KAALDELMKG--RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1312-1533 |
3.76e-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: 82.62 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1388
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 LSIILQDpilfsgsirFNLDPECKCTDDRLWEALeiAQlKNMVKSLPG-----------------GLDAVVTEGGENFSV 1451
Cdd:cd03256 80 IGMIFQQ---------FNLIERLSVLENVLSGRL--GR-RSTWRSLFGlfpkeekqralaalervGLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1452 GQRQLFCLARAFVRKSSILIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILT-ADLVIVMKRGNI 1524
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
....*....
gi 110832837 1525 LEYDTPESL 1533
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
690-901 |
4.83e-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: 84.77 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNEsEPSFEATRSRN----RYSVAYAAQK----PWL 761
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIR---LGG-EVLQDSARGIFlpphRRRIGYVFQEarlfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 lnaTVEENITFGSPFNKQRYKAVtdacslQPD--IDLLpfgdqtEIG---ERGI-NLSGGQRQRICVARALYQNTNIVFL 835
Cdd:COG4148 93 ---SVRGNLLYGRKRAPRAERRI------SFDevVELL------GIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 836 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 901
Cdd:COG4148 158 DEPLAALDLARKAEILP--YLERLRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
688-899 |
5.50e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 82.00 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEatrsrnRYSVAYAAQKPWLL-NATV 766
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------KRDISYVPQNYALFpHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFGspFNKQRYKAVTDACSLQpdidllpfgdqtEIGER-GIN---------LSGGQRQRICVARALYQNTNIVFLD 836
Cdd:cd03299 89 YKNIAYG--LKKRKVDKKEIERKVL------------EIAEMlGIDhllnrkpetLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 837 DPFSALDIHLSDHLMQEgiLKFLQDDKRTLVL-VTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03299 155 EPFSALDVRTKEKLREE--LKKIRKEFGVTVLhVTHDFeEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
688-891 |
7.14e-17 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 82.26 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 767
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR----LSIILQDPILFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLS 847
Cdd:cd03288 113 FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM-AT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110832837 848 DHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSVL 891
Cdd:cd03288 192 ENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
688-919 |
7.42e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEM---QTLEGKVHW-SNVNESEPSFEATRSRNRYSVAYAAQKPWLLN 763
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELlGRTVQREGRLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 A-TVEENITFG---------------SPFNKQR-YKAVTDacslqpdIDLLPFGDQteigeRGINLSGGQRQRICVARAL 826
Cdd:PRK09984 100 RlSVLENVLIGalgstpfwrtcfswfTREQKQRaLQALTR-------VGMVHFAHQ-----RVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 827 YQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTlkdIQTKDVE 905
Cdd:PRK09984 168 MQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS---SQQFDNE 243
|
250
....*....|....
gi 110832837 906 LYEHWKTLMNRQDQ 919
Cdd:PRK09984 244 RFDHLYRSINRVEE 257
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1312-1538 |
9.17e-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: 9.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFR-MVDIF---DGKIVIDGIDISKL---PLHT 1384
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTL----LRlIVGLLrpdSGEVLIDGEDISGLseaELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 LRSRLSIILQDPILFSG-----SIRFNLDPECKCTDdrlWEALEIAQLK-NMVkSLPGGLDAVVTEggenFSVGQRQLFC 1458
Cdd:cd03261 75 LRRRMGMLFQSGALFDSltvfeNVAFPLREHTRLSE---EEIREIVLEKlEAV-GLRGAEDLYPAE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASID-MATENI------LQKVVmtafaDRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTP 1530
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIddlirsLKKEL-----GLTSIMVTHDLDTAFaIADRIAVLYDGKIVAEGTP 221
|
....*...
gi 110832837 1531 ESLLAQEN 1538
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 ... |
1312-1521 |
1.02e-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: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENN--LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGidiskLPLHTL 1385
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLErptsGEVLVDG-----EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 RSRLSIILQDPILFS-GSIRFN--LDPECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1457
Cdd:cd03293 72 GPDRGYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAreraeELLELVGLSGFENAYPHQL-----------SGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKR 1521
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1312-1548 |
1.53e-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: 80.81 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPILFSG-SIRFNLD--------PECKcTDDRLWEALEIAQL--KNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1460
Cdd:cd03295 80 VIQQIGLFPHmTVEENIAlvpkllkwPKEK-IRERADELLALVGLdpAEFADRYPHEL-----------SGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1461 RAFVRKSSILIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESL 1533
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
250
....*....|....*.
gi 110832837 1534 LA-QENGVFASFVRAD 1548
Cdd:cd03295 224 LRsPANDFVAEFVGAD 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
680-892 |
1.72e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.16 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 680 SWGSG---LATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAY 754
Cdd:PRK10535 13 SYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMniLGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 755 aaQKPWLL-NATVEENITF-----GSPFNKQRYKAvtdacslqpdIDLLP-FGDQTEIGERGINLSGGQRQRICVARALY 827
Cdd:PRK10535 93 --QRYHLLsHLTAAQNVEVpavyaGLERKQRLLRA----------QELLQrLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 828 QNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLR 892
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
684-855 |
1.84e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFeatrsrnRYSVAYA----AQKP 759
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV-------AEACHYLghrnAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 760 WLlnaTVEENITFGSPFNKQRYKAVTDACS---LQPDIDLlPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 836
Cdd:PRK13539 87 AL---TVAENLEFWAAFLGGEELDIAAALEavgLAPLAHL-PFG----------YLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180
....*....|....*....|....*..
gi 110832837 837 DPFSALDIH--------LSDHLMQEGI 855
Cdd:PRK13539 153 EPTAALDAAavalfaelIRAHLAQGGI 179
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1308-1536 |
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 110832837 1308 QEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 1387
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQDPI-LFSGS-----IRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1458
Cdd:PRK13635 82 QVGMVFQNPDnQFVGAtvqddVAFGLENIGVPREEmveRVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1329-1546 |
1.96e-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: 81.15 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1329 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILFS---- 1400
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLPhrtv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1401 -GSIRFNLDPECKCTDDRL---WEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1476
Cdd:cd03294 120 lENVAFGLEVQGVPRAEREeraAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1477 ASIDMATENILQKVVMTAFAD--RTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQ-ENGVFASFVR 1546
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNpANDYVREFFR 262
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
688-890 |
2.03e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnVNESEPSFEAtRSRNRYSVAYAAQKPWllnATVE 767
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL----LAGTAPLAEA-REDTRLMFQDARLLPW---KKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFGSPFN-KQRYKAVTDACSLQPdidllpfgdqtEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhL 846
Cdd:PRK11247 100 DNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA-L 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110832837 847 SDHLMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSV 890
Cdd:PRK11247 168 TRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1312-1535 |
2.03e-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: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1391
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 IL--QDPILFSG-SIRFNLD-PECKCTDDRLWEALEIA-----QLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1462
Cdd:cd03224 78 GYvpEGRRIFPElTVEENLLlGAYARRRAKRKARLERVyelfpRLKERRKQLAGTL-----------SGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1463 FVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1535
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALeIADRAYVLERGRVVLEGTAAELLA 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
688-899 |
2.25e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.07 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAtRSRNRYSVAYAaqkpwLL-NATV 766
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RHVNTVFQSYA-----LFpHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFG-----SPfNKQRYKAVTDACSLqpdIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:PRK09452 104 FENVAFGlrmqkTP-AAEITPRVMEALRM---VQLEEFAQR-----KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 842 LDIHLSDHLMQEgiLKFLQddkRTL----VLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK09452 175 LDYKLRKQMQNE--LKALQ---RKLgitfVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
672-890 |
2.34e-16 |
|
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: 78.24 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnvnesepsfeatrsrnrys 751
Cdd:cd03216 1 LELRGITKRFGGVKA-LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 vayaaqkpwllnatvEENITFGSPFNKQRykavtdacslqpdidllpfgdqteigeRGIN----LSGGQRQRICVARALY 827
Cdd:cd03216 61 ---------------GKEVSFASPRDARR---------------------------AGIAmvyqLSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 828 QNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSV 890
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEvFEIADRVTVLRDGRV 160
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
671-894 |
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 110832837 671 AIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnvneSEPSFEATRSRnry 750
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIL----GQPTRQALQKN--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 SVAYAAQKP---WLLNATVEENITFGS---------PFNKQRyKAVTDACSlqpDIDLLPFgDQTEIGErginLSGGQRQ 818
Cdd:PRK15056 79 LVAYVPQSEevdWSFPVLVEDVVMMGRyghmgwlrrAKKRDR-QIVTAALA---RVDMVEF-RHRQIGE----LSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 819 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKdGSVLREG 894
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK-GTVLASG 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
672-903 |
2.44e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVN-ESEPSFEATRSrnry 750
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvEALSARAASRR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 sVAYAAQKPWL-LNATVEENITFGSPFNKQRYKAVTDACSLQPDiDLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQ 828
Cdd:PRK09536 79 -VASVPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 829 NTNIVFLDDPFSALDIHlsdHLMQE-GILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKD 903
Cdd:PRK09536 157 ATPVLLLDEPTASLDIN---HQVRTlELVRRLVDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
688-909 |
2.47e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEaTRSRN----RYSVAYAAQKP--WL 761
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT---IGERVITAG-KKNKKlkplRKKVGIVFQFPehQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNATVEENITFGsPFN--------KQRYKAVTDACSLQPDI-DLLPFgdqteigergiNLSGGQRQRICVARALYQNTNI 832
Cdd:PRK13634 99 FEETVEKDICFG-PMNfgvseedaKQKAREMIELVGLPEELlARSPF-----------ELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 833 VFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDVELYEH 909
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMM-EMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
677-893 |
2.85e-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: 80.62 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 677 GYFSWGSG-LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNR-----Y 750
Cdd:TIGR02769 15 GGLFGAKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRdvqlvF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 SVAYAAQKPwllNATVEENItfGSPF----------NKQRYKAVTDACSLQPDI-DLLPfgdqteigergINLSGGQRQR 819
Cdd:TIGR02769 95 QDSPSAVNP---RMTVRQII--GEPLrhltsldeseQKARIAELLDMVGLRSEDaDKLP-----------RQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 820 ICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLRE 893
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
684-909 |
3.75e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.19 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESE-PSFEatRSRNRYSVAYAAqkpwLL 762
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQ--RPINMMFQSYAL----FP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 NATVEENITFGSPFNKQRYKAVTDACSlqpdiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:PRK11607 105 HMTVEQNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 842 LDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKdiqtkdvELYEH 909
Cdd:PRK11607 180 LDKKLRDR-MQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE-------EIYEH 240
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1339-1524 |
4.53e-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: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1339 GQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhTLRSRLSIILQDPILFS-----GSIRFNLDP 1409
Cdd:cd03298 24 GEITAIVGPSGSGKSTL----LNLIAGFEtpqsGRVLINGVDVTAAP--PADRPVSMLFQENNLFAhltveQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1410 ECKCT-DDRlwEALEIAQ----LKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 1484
Cdd:cd03298 98 GLKLTaEDR--QAIEVALarvgLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110832837 1485 NILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNI 1524
Cdd:cd03298 165 AEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
672-906 |
4.76e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfEATRSRNRYS 751
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS-KLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWLLNATVEENITFGsPFNkqrykavtdACslQPDIDLLPFGDQTeIGERGI---------NLSGGQRQRICV 822
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAFG-PEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 823 ARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGT----LKD 898
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEpenvLSD 225
|
....*...
gi 110832837 899 IQTKDVEL 906
Cdd:PRK13644 226 VSLQTLGL 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1313-1524 |
5.11e-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: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1313 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiskLPLHTLRSRL--- 1389
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIgyv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 ---SIILQD-PILFSGSIRFNLDPEC------KCTD-DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1458
Cdd:cd03235 74 pqrRSIDRDfPISVRDVVLMGLYGHKglfrrlSKADkAKVDEALERVGLSELADRQIGEL-----------SGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILT-ADLVIVMKRGNI 1524
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1312-1545 |
5.66e-16 |
|
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: 78.92 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlkpVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPlhTLRSRL 1389
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLleTIAGFIKPD--SGKILLNGKDITNLP--PEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPILFSG-SIRFNLDPECKctdDRLWEALEI-AQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 1467
Cdd:cd03299 74 SYVPQNYALFPHmTVYKNIAYGLK---KRKVDKKEIeRKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1468 SILIMDEATASIDMATENILQKVVMTAF--ADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ-ENGVFAS 1543
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKpKNEFVAE 228
|
..
gi 110832837 1544 FV 1545
Cdd:cd03299 229 FL 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
688-899 |
5.78e-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: 78.63 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVN-ESEPSFEatrsRNRYSVAYAAQKPWLL-NAT 765
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHE----RARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITFG-SPFNKQRYKAVTDACslqpdIDLLPfgdqtEIGER----GINLSGGQRQRICVARALYQNTNIVFLDDPFS 840
Cdd:cd03224 92 VEENLLLGaYARRRAKRKARLERV-----YELFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 841 ALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDI 899
Cdd:cd03224 162 GLAPKIVEEIFE--AIRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
668-894 |
7.18e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.59 E-value: 7.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 668 EDIAIKVTNGyfSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSNVNESEPSFeatr 745
Cdd:cd03213 7 RNLTVTVKSS--PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSF---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 srnRYSVAYAAQKPWLL-NATVEENITFgspfnkqrykavtdACSLQpdidllpfgdqteigergiNLSGGQRQRICVAR 824
Cdd:cd03213 81 ---RKIIGYVPQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 825 ALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA--DWIIAMKDGSVLREG 894
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1344-1545 |
9.53e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 80.23 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1344 ICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtLRSrLSIILQDPILF-----SGSIRFNL--DPECKCT 1414
Cdd:TIGR01187 1 LLGPSGCGKTTLlrLLAGFEQPD--SGSIMLDGEDVTNVPPH-LRH-INMVFQSYALFphmtvEENVAFGLkmRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1415 -DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID------MATE--N 1485
Cdd:TIGR01187 77 iKPRVLEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1486 ILQKVVMtafadrTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF-ASFV 1545
Cdd:TIGR01187 146 IQEQLGI------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
669-894 |
9.94e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 9.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 669 DIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRn 748
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 749 rysVAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQ 818
Cdd:PRK13647 81 ---VGLVFQDPddQVFSSTVWDDVAFG-PVNmgldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 819 RICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLREG 894
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1312-1525 |
1.00e-15 |
|
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: 77.79 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTl 1385
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGLlepdAGFATVDGFDVVKEPAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 RSRLSIilqdpilFSGSIRFNldpeckctdDRL--WEALEI---------AQLKNMVKSLPGGLD--AVVTEGGENFSVG 1452
Cdd:cd03266 77 RRRLGF-------VSDSTGLY---------DRLtaRENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1453 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1525
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1312-1536 |
1.11e-15 |
|
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: 80.10 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVlkhvKA------YIKPGQKVGICGRTGSGKSSLSLAFFRMVD---IFDGKIVIDGIDISKLPL 1382
Cdd:COG0444 2 LEVRNLKVYFPTRRGVV----KAvdgvsfDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1383 HTLRS----RLSIILQDPIlfsGSirfnLDPeCKCTDDRLWEALEI------AQLKNMVKSLpggLDAV-VTEGGE---- 1447
Cdd:COG0444 78 KELRKirgrEIQMIFQDPM---TS----LNP-VMTVGDQIAEPLRIhgglskAEARERAIEL---LERVgLPDPERrldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1448 ---NFSVGQRQLFCLARAFVRKSSILIMDEATASIDmATeniLQKVVMTAFADR------TVVTIAHRVHTIL-TADLVI 1517
Cdd:COG0444 147 yphELSGGMRQRVMIARALALEPKLLIADEPTTALD-VT---IQAQILNLLKDLqrelglAILFITHDLGVVAeIADRVA 222
|
250
....*....|....*....
gi 110832837 1518 VMKRGNILEYDTPESLLAQ 1536
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
688-899 |
1.51e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.13 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfeatrSRNRySVAYAAQKPWLL-NATV 766
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-----ARDR-KVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFGS---PFNKQRYKAVTDACSLQpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 842
Cdd:PRK10851 92 FDNIAFGLtvlPRRERPNAAAIKAKVTQ----LLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 843 DIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK10851 168 DAQVRKEL-RRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1312-1510 |
1.78e-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: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1388
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 LSIILQDPILFSG-----SIRFNLdpECKCTDDRLW-----EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1458
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyeNVAFAL--EVTGVPPREIrkrvpAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRVHTI 1510
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHRVIAL 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
672-890 |
1.96e-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: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYfswGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEAT-RSRNRY 750
Cdd:cd03292 4 INVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 SVAYAAQKpWLLNATVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVA 823
Cdd:cd03292 81 GVVFQDFR-LLPDRNVYENVAFalevtGVPPReiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 824 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSV 890
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMN--LLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1312-1480 |
2.16e-15 |
|
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: 76.36 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPLHtLRS 1387
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQDPILFSG-SIRFNLD-----PECKCTDDRLWEALEIAqlknmvkslpgGLDAVVTEGGENFSVGQRQLFCLAR 1461
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALAR 144
|
170
....*....|....*....
gi 110832837 1462 AFVRKSSILIMDEATASID 1480
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALD 163
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
688-899 |
2.42e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.28 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNVNESEPSFEATRS-----RNRYSVAYAAQKPWLL 762
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV---TVDDITITHKTKDKyirpvRKRIGMVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 NATVEENITFGSP-FNKQRYKAVTDACSLqpdidLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFS 840
Cdd:PRK13646 100 EDTVEREIIFGPKnFKMNLDEVKNYAHRL-----LMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 841 ALDIHLSDHLMQegILKFLQ-DDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK13646 175 GLDPQSKRQVMR--LLKSLQtDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKEL 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1312-1526 |
2.87e-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: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSR 1388
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 LSIILQD-PILFSGSIRFNL----------DPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1457
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgksRKEIR---RRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTILTADL-VIVMKRGNILE 1526
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
672-888 |
2.92e-15 |
|
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: 76.41 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQ----TLEGKvhwsNVNESEPSFEATR 745
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPDsgtiIIDGL----KLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SRnrysVAYAAQKPWLL-NATVEENITFGsP---FNKQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRIC 821
Cdd:cd03262 76 QK----VGMVFQQFNLFpHLTVLENITLA-PikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 822 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 888
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLD--VMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
672-908 |
3.06e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.17 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSW--GSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSR 747
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 748 NRYSVAYAAQKPWLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDI--DLLPFgdqteigergiNLSGGQR 817
Cdd:PRK13637 83 KKVGLVFQYPEYQLFEETIEKDIAFG-PINlglseeeiENRVKRAMNIVGLDYEDykDKSPF-----------ELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 818 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGT 895
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK--IKELHKEyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
250
....*....|...
gi 110832837 896 LKDIqTKDVELYE 908
Cdd:PRK13637 229 PREV-FKEVETLE 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
686-908 |
3.16e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.92 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 686 ATLSNIDIRIPTGQLTMIVGQVGCGKSS---LLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRnrysVAYAAQKP--W 760
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK----VGIVFQNPdnQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 761 LLNATVEENITFGSPfNKQ--RYKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDP 838
Cdd:PRK13640 97 FVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 839 FSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYE 908
Cdd:PRK13640 171 TSMLDPAGKEQILK--LIRKLKKKNNlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKE 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
688-895 |
3.36e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.12 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVN-ESEPSFEATRSRnrysvAYAAQK-----PWl 761
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPlADWSPAELARRR-----AVLPQHsslsfPF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 lnaTVEENITFG-SPF--NKQRYKAVTDACSLQpdIDLLPFGD---QTeigerginLSGGQRQRICVARALYQNTN---- 831
Cdd:PRK13548 92 ---TVEEVVAMGrAPHglSRAEDDALVAAALAQ--VDLAHLAGrdyPQ--------LSGGEQQRVQLARVLAQLWEpdgp 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 832 --IVFLDDPFSALDIHLSDHLMQegILK-FLQDDKRTLVLVTHKL----QYlthADWIIAMKDGSVLREGT 895
Cdd:PRK13548 159 prWLLLDEPTSALDLAHQHHVLR--LARqLAHERGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
692-890 |
3.41e-15 |
|
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: 76.05 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 692 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNVNESEPSfeatrsrnRYSVAYAAQKPWLL-NATVEE 768
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGsiKVNDQSHTGLAPY--------QRPVSMLFQENNLFaHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 769 NITFG-SPFNK----QRYKAVTDACSLQPD--IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:TIGR01277 90 NIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110832837 842 LDIHLSDHlMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 890
Cdd:TIGR01277 159 LDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1326-1525 |
3.91e-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: 75.67 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1326 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRSRLSIILQDPILFSgsi 1403
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHP--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1404 rfnldpeckctDDRLWEALEI-AQLknmvKSLPGgldavvteggenfsvGQRQLFCLARAFVRKSSILIMDEATASIDMA 1482
Cdd:cd03213 96 -----------TLTVRETLMFaAKL----RGLSG---------------GERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110832837 1483 TENILQKVVMtAFAD--RTVVTIAHRVHTILTA--DLVIVMKRGNIL 1525
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
672-899 |
4.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRN-RY 750
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL---IKGEPIKYDKKSLLEvRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 751 SVAYAAQKP--WLLNATVEENITFGsPFN-----KQRYKAVTDACSlqpdidllpfgdqtEIGERGI------NLSGGQR 817
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFG-PLNlglskEEVEKRVKEALK--------------AVGMEGFenkpphHLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 818 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSVLREGTL 896
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTP 221
|
...
gi 110832837 897 KDI 899
Cdd:PRK13639 222 KEV 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
747-913 |
4.17e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 RNRYSVAyaAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 825
Cdd:PTZ00265 1295 RNLFSIV--SQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 826 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM----KDGS-VLREGTLKDIQ 900
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGTHEELL 1451
|
170
....*....|...
gi 110832837 901 TKDVELYEHWKTL 913
Cdd:PTZ00265 1452 SVQDGVYKKYVKL 1464
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
671-912 |
4.38e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.80 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 671 AIKVTNGYFSWGSGlATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNVNESEPSFEATR 745
Cdd:PRK14267 4 AIETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SRNRYSVAYAAQKPWLlNATVEENITFGSPFNK---------QRYKAVTDACSLQPDIdllpfgdQTEIGERGINLSGGQ 816
Cdd:PRK14267 83 VRREVGMVFQYPNPFP-HLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 817 RQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHK-LQYLTHADWIIAMKDGSVLREG- 894
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANID-PVGTAKIEELLFELKKE--YTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGp 231
|
250
....*....|....*...
gi 110832837 895 TLKDIQTKDVELYEHWKT 912
Cdd:PRK14267 232 TRKVFENPEHELTEKYVT 249
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
688-871 |
4.80e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.60 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ---TLEGKVhWsnVNESEPSFEATRSRNrysVAYAAQKPWLL-N 763
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEV-L--LNGRRLTALPAEQRR---IGILFQDDLLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 ATVEENITFGSP--FNK-QRYKAVTDAcsLQpDIDLLPFGDQTeIGErginLSGGQRQRICVARALYQNTNIVFLDDPFS 840
Cdd:COG4136 91 LSVGENLAFALPptIGRaQRRARVEQA--LE-EAGLAGFADRD-PAT----LSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|...
gi 110832837 841 ALDIHLSDHLMQegiLKFLQDDKRTL--VLVTH 871
Cdd:COG4136 163 KLDAALRAQFRE---FVFEQIRQRGIpaLLVTH 192
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1312-1538 |
8.82e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.69 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHTLR 1386
Cdd:PRK13650 5 IEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDGLleaeSGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1387 SRLSIILQDPI-LFSGS-----IRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1457
Cdd:PRK13650 81 HKIGMVFQNPDnQFVGAtveddVAFGLENkgiPHEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1458 CLARAFVRKSSILIMDEATASID--------MATENILQKVVMTafadrtVVTIAHRVHTILTADLVIVMKRGNILEYDT 1529
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQMT------VISITHDLDEVALSDRVLVMKNGQVESTST 223
|
....*....
gi 110832837 1530 PESLLAQEN 1538
Cdd:PRK13650 224 PRELFSRGN 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
676-907 |
9.85e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.76 E-value: 9.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 676 NGYFSWGSGLATlSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPsfeATRSRNRYSVA 753
Cdd:PRK11000 8 NVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrMNDVPP---AERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 754 YAAQkPWLlnaTVEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARAL 826
Cdd:PRK11000 84 YALY-PHL---SVAENMSFGLKLAGakkeeinQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 827 YQNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGtlkdiqtKDVE 905
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG-------KPLE 220
|
..
gi 110832837 906 LY 907
Cdd:PRK11000 221 LY 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
688-899 |
1.44e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.93 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 765
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivVSSTSKQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITFGsPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 844
Cdd:PRK13643 102 VLKDVAFG-PQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 845 HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK13643 178 KARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
684-897 |
1.68e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.17 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVnesepSFEATRSRN---------RYSVAY 754
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDI-----TIDTARSLSqqkglirqlRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 755 AAQKPWLL-NATVEENITFGSPFNKQ--RYKAVTDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQNTN 831
Cdd:PRK11264 90 VFQNFNLFpHRTVLENIIEGPVIVKGepKEEATARARELLAKVGLA--GKETSYPRR---LSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 832 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLK 897
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLN--TIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1312-1537 |
1.84e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRL 1389
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALE---IAQLKNmvkslpggldavvtEGGENFSVGQRQLF 1457
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKrtgIEHLKD--------------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1458 CLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLL 1534
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVF 230
|
...
gi 110832837 1535 AQE 1537
Cdd:PRK13636 231 AEK 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1312-1536 |
1.89e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENN----LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP-LHTLR 1386
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1387 SRLSIILQDP------ILFSGSIRF---NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1457
Cdd:PRK13633 85 NKAGMVFQNPdnqivaTIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILTADLVIVMKRGNILEYDTPE 1531
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 110832837 1532 SLLAQ 1536
Cdd:PRK13633 230 EIFKE 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
688-895 |
2.64e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 73.69 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNEsePSFEATRSRNRYSVAYAAQK---PWLLna 764
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY---ING--YSIRTDRKAARQSLGYCPQFdalFDEL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITF-----GSPFNKQRY--KAVTDACSLQPDIDllpfgdqTEIGergiNLSGGQRQRICVARALYQNTNIVFLDD 837
Cdd:cd03263 91 TVREHLRFyarlkGLPKSEIKEevELLLRVLGLTDKAN-------KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 838 PFSALdihlsDHLMQEGILKFLQDDK--RTLVLVTHKLQ---YLthADWIIAMKDGSVLREGT 895
Cdd:cd03263 160 PTSGL-----DPASRRAIWDLILEVRkgRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1329-1534 |
2.66e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1329 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS----RLSIILQDpilfsgsir 1404
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1405 FNLDPECKCTDDRLWeALEIAQLKNMVKSlPGGLDAVVTEGGENF--------SVGQRQLFCLARAFVRKSSILIMDEAT 1476
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1477 ASID--MATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLL 1534
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1312-1540 |
2.91e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPI-LFSGSI-----RFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1462
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDEmhrRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1463 FVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGV 1540
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1327-1536 |
3.20e-14 |
|
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: 74.89 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1327 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1406
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1407 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN- 1485
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1486 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1312-1537 |
3.36e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMV-------DIFDGKIVIDGIDISKLPLHT 1384
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLInglllpdDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 LRSRLSIILQDPI-LFSGS-----IRFNLDpeckctdDRLWEALEIAQLKNMVKSLPGGLDAVVTEGgENFSVGQRQLFC 1458
Cdd:PRK13640 82 IREKVGIVFQNPDnQFVGAtvgddVAFGLE-------NRAVPRPEMIKIVRDVLADVGMLDYIDSEP-ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 110832837 1537 E 1537
Cdd:PRK13640 234 V 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
690-899 |
3.73e-14 |
|
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: 77.03 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNVNESEPSFEATRS-RNRYSVA----YAAQKPWLlna 764
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPlRRRMQVVfqdpFGSLSPRM--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFG--------SPfnKQRYKAVTDAcsLQpDIDLLPfgdqtEIGERGIN-LSGGQRQRICVARALYQNTNIVFL 835
Cdd:COG4172 380 TVGQIIAEGlrvhgpglSA--AERRARVAEA--LE-EVGLDP-----AARHRYPHeFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 836 DDPFSALDIHLsdhlmQEGILKFLQD--DKRTL--VLVTHKLQ---YLTHadWIIAMKDGSVLREGTLKDI 899
Cdd:COG4172 450 DEPTSALDVSV-----QAQILDLLRDlqREHGLayLFISHDLAvvrALAH--RVMVMKDGKVVEQGPTEQV 513
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1307-1522 |
4.02e-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: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1307 PQEGEIKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGidiskL 1380
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDG-----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1381 PLHTLRSRLSIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenf 1449
Cdd:COG1116 74 PVTGPGPDRGVVFQEPALLpwltvLDNVALGLElrgvpkAERR---ERARELLELVGLAGFEDAYPHQL----------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 1450 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILTADLVIVMKRG 1522
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDeAVFLADRVVVLSAR 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
684-901 |
6.01e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 73.24 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNES-EPSFEatrsRNRYSVAYAAQKPWLL 762
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITgLPPHE----IARLGIGRTFQIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 -NATVEENITFGSPFNKQRYKAVTDACSLQPDI-----DLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNI 832
Cdd:cd03219 88 pELTVLENVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 833 VFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQT 901
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVVMsLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1312-1537 |
6.04e-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: 72.96 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaFFRMVDIF---DGKIVIDGIDISKLPLHTlRSR 1388
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTT---FYMIVGLVkpdSGKILLDGQDITKLPMHK-RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 LSIIL--QDPILFSG-SIRFNL--------DPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1457
Cdd:cd03218 75 LGIGYlpQEASIFRKlTVEENIlavleirgLSK-KEREEKLEELLEEFHITHLRKSKASSL-----------SGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1458 CLARAFVRKSSILIMDEATASID-MATENIlQKVVMTaFADRTV-VTIA-HRVHTIL-TADLVIVMKRGNILEYDTPESL 1533
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDpIAVQDI-QKIIKI-LKDRGIgVLITdHNVRETLsITDRAYIIYEGKVLAEGTPEEI 220
|
....
gi 110832837 1534 LAQE 1537
Cdd:cd03218 221 AANE 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1312-1532 |
6.08e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.31 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNL---KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLR 1386
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1387 SRLSIILQDP------------ILFsGSIRFNL-DPECKctdDRLWEALEIAqlknmvkslpgGLDAVVTEGGENF--SV 1451
Cdd:PRK13637 83 KKVGLVFQYPeyqlfeetiekdIAF-GPINLGLsEEEIE---NRVKRAMNIV-----------GLDYEDYKDKSPFelSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1452 GQRQLFCLARAFVRKSSILIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1528
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
....
gi 110832837 1529 TPES 1532
Cdd:PRK13637 228 TPRE 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
672-894 |
6.48e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNesepsfeaTRSRNRYS 751
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQD--------LSRLKRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQK-------PWLL-NATVEENITF-----GSPfNKQRYKAVTDACS---LQPDIDLLPfgdqteigergINLSGG 815
Cdd:COG2884 74 IPYLRRRigvvfqdFRLLpDRTVYENVALplrvtGKS-RKEIRRRVREVLDlvgLSDKAKALP-----------HELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 816 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADW-IIAMKDGSVLREG 894
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIME--LLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1312-1524 |
8.14e-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: 72.18 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRL 1389
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDpilfsgsirFNLDPECK----CTDDRLW-------EALEIA-------QLKNMVKSLPGGLdavvteggenfSV 1451
Cdd:cd03262 79 GMVFQQ---------FNLFPHLTvlenITLAPIKvkgmskaEAEERAlellekvGLADKADAYPAQL-----------SG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 1452 GQRQLFCLARAFVRKSSILIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRGNI 1524
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
641-889 |
8.26e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.38 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 641 TINRkqpgryhLDSYEQSTRRLRPAETEDIAIKVTNGyfswgSGLAT-------------LSNIDIRIPTGQLTMIVGQV 707
Cdd:COG4178 331 TVDR-------LAGFEEALEAADALPEAASRIETSED-----GALALedltlrtpdgrplLEDLSLSLKPGERLLITGPS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 708 GCGKSSLLLAILGemqtlegkvHWsnvnesePSFEATRSR-NRYSVAYAAQKPWLLNATVEENITFGSP---FNKQRYKA 783
Cdd:COG4178 399 GSGKSTLLRAIAG---------LW-------PYGSGRIARpAGARVLFLPQRPYLPLGTLREALLYPATaeaFSDAELRE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 784 VTDACSLQPDIDLLpfgDQTEIGERGinLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDdk 863
Cdd:COG4178 463 ALEAVGLGHLAERL---DEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG-- 534
|
250 260
....*....|....*....|....*.
gi 110832837 864 RTLVLVTHKLQYLTHADWIIAMKDGS 889
Cdd:COG4178 535 TTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1310-1545 |
1.22e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.34 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1310 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLaffRMV----DIFDGKIVIDGIDISKLPLHtl 1385
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTL-L---RMIagleDPTSGEILIGGRDVTDLPPK-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 RSRLSIILQDPILF-SGSIRFNL----------DPEckcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQR 1454
Cdd:COG3839 74 DRNIAMVFQSYALYpHMTVYENIafplklrkvpKAE---IDRRVREAAELLGLEDLLDRKPKQL-----------SGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1455 QLFCLARAFVRKSSILIMDEATASID------MATE--NILQKVVMTafadrTV-VTiaHRVHTILT-ADLVIVMKRGNI 1524
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TIyVT--HDQVEAMTlADRIAVMNDGRI 212
|
250 260
....*....|....*....|..
gi 110832837 1525 LEYDTPESLLAQENGVF-ASFV 1545
Cdd:COG3839 213 QQVGTPEELYDRPANLFvAGFI 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
688-883 |
1.72e-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: 69.88 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnvnesEPSFEAtrsrnrysVAYAAQKPWLLNATVE 767
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-------MPEGED--------LLFLPQRPYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 ENITFgspfnkqrykavtdacslqpdidllPFGDqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 847
Cdd:cd03223 82 EQLIY-------------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*.
gi 110832837 848 DHLMQegilkFLQDDKRTLVLVTHKLQYLTHADWII 883
Cdd:cd03223 128 DRLYQ-----LLKELGITVISVGHRPSLWKFHDRVL 158
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
668-899 |
1.99e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.57 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 668 EDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPSFEATR 745
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SrnrySVAYAAQKP--WLLNATVEENITFGsPFNKQrykavtdacslqpdidlLPfgdQTEIGER--------GIN---- 811
Cdd:PRK13636 82 E----SVGMVFQDPdnQLFSASVYQDVSFG-AVNLK-----------------LP---EDEVRKRvdnalkrtGIEhlkd 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 812 -----LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLT-HADWIIAM 885
Cdd:PRK13636 137 kpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM-KLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVM 215
|
250
....*....|....
gi 110832837 886 KDGSVLREGTLKDI 899
Cdd:PRK13636 216 KEGRVILQGNPKEV 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
672-888 |
2.14e-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: 69.01 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLaTLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNEsepsfeatrsrnrys 751
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQkpwllnatveenitfgspfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTN 831
Cdd:cd03221 65 IGYFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 832 IVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 888
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEE-----ALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1312-1545 |
2.15e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 73.59 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHtlRSRL 1389
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLlrMIAGFETPD--SGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPILF-----SGSIRFNLD------PECKctdDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1458
Cdd:COG3842 80 GMVFQDYALFphltvAENVAFGLRmrgvpkAEIR---ARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASID------MATE--NILQKVVMTAFadrtVVTiaHRVHTILT-ADLVIVMKRGNILEYDT 1529
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDaklreeMREElrRLQRELGITFI----YVT--HDQEEALAlADRIAVMNDGRIEQVGT 219
|
250
....*....|....*..
gi 110832837 1530 PESLLAQENGVF-ASFV 1545
Cdd:COG3842 220 PEEIYERPATRFvADFI 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
688-925 |
2.20e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHW-SNVNESEpsfEATRSRNRYSVAYAAQKPWL 761
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIqltngLIISETGQTIVGDYAIpANLKKIK---EVKRLRKEIGLVFQFPEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNATVEENITFGsPFN-----KQRYKAVTDACSLQPdidlLPfgdqTEIGERG-INLSGGQRQRICVARALYQNTNIVFL 835
Cdd:PRK13645 104 FQETIEKDIAFG-PVNlgenkQEAYKKVPELLKLVQ----LP----EDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 836 DDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGT----------LKDIQTKDV 904
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSpfeifsnqelLTKIEIDPP 253
|
250 260
....*....|....*....|.
gi 110832837 905 ELYEHWKTLMNRQDQELEKDM 925
Cdd:PRK13645 254 KLYQLMYKLKNKGIDLLNKNI 274
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1312-1525 |
2.23e-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: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQkVGICGRTGSGKSSL--SLA-FFRMVDifdGKIVIDGIDISKLPlHTLRSR 1388
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTLmrILAtLTPPSS---GTIRIDGQDVLKQP-QKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 LSIILQDpilFSGSIRFnldpeckctddRLWEALE-IAQLKNMVKS-----LPGGLDAVVTEGGEN-----FSVGQRQLF 1457
Cdd:cd03264 74 IGYLPQE---FGVYPNF-----------TVREFLDyIAWLKGIPSKevkarVDEVLELVNLGDRAKkkigsLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1458 CLARAFVRKSSILIMDEATASID----MATENILQKVVmtafADRTVVTIAHRVHTI-LTADLVIVMKRGNIL 1525
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG----EDRIVILSTHIVEDVeSLCNQVAVLNKGKLV 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
688-899 |
2.36e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.91 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 766
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFGS-----PFNKQRYKAVtDACSlQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:PRK10070 124 LDNTAFGMelagiNAEERREKAL-DALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 842 LDIHLSDHlMQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK10070 195 LDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1327-1537 |
2.37e-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: 75.72 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1327 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 1406
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1407 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-N 1485
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1486 ILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQE 1537
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1324-1534 |
2.44e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1324 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI------DISKLPLHTLRSRLSIILQDPI 1397
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1398 LFSG-SIRFNLDPECKCTDDRlwEALEIAQLKNMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMD 1473
Cdd:PRK14246 101 PFPHlSIYDNIAYPLKSHGIK--EKREIKKIVEECLRKVGLWKEVydrLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1474 EATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLL 1534
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
684-871 |
2.48e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.60 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRsrnrySVAYAAQKPWLLN 763
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-----GLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 A-TVEENITFGSPFNKQryKAVTDACSlqpDIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:cd03231 87 TlSVLENLRFWHADHSD--EQVEEALA---RVGLNGFED------RPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 110832837 842 LDI--------HLSDHLMQEGIlkflqddkrtLVLVTH 871
Cdd:cd03231 156 LDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
672-900 |
2.51e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAT----LSNIDIRIPTGQLTMIVGQVGCGKSS-------LLLAILGEM-----------QTLEGKV 729
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIewifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 730 HWSNVNESEPSFEATRS----RNRYSVAYAAQKPWLLNATVEENITFGsPFN--------KQRYKAVTDACSLqpDIDLL 797
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKikeiRRRVGVVFQFAEYQLFEQTIEKDIIFG-PVSmgvskeeaKKRAAKYIELVGL--DESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 798 ---PFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 874
Cdd:PRK13651 160 qrsPF-----------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLD 226
|
250 260 270
....*....|....*....|....*....|.
gi 110832837 875 Y-LTHADWIIAMKDGSVLREG----TLKDIQ 900
Cdd:PRK13651 227 NvLEWTKRTIFFKDGKIIKDGdtydILSDNK 257
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1312-1522 |
3.02e-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: 68.99 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSRLS 1390
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1391 IILQdpilfsgsirfnldpeckctddrlwealeiaqlknmvkslpggldavvteggenFSVGQRQLFCLARAFVRKSSIL 1470
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 1471 IMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTIL-TADLVIVMKRG 1522
Cdd:cd03216 105 ILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFeIADRVTVLRDG 158
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1312-1506 |
5.25e-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: 68.33 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIdgidisklplhTLRS 1387
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALaglwPWGSGRIGM-----------PEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQDPILFSGSIRfnldpeckctddrlwealeiaqlknmvkslpgglDAVVTEGGENFSVGQRQLFCLARAFVRKS 1467
Cdd:cd03223 65 DLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 110832837 1468 SILIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1506
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1249-1526 |
8.61e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1249 GLGLLYaltITNYLNwVVRNLADLEVQMGAVKKV--NSFLTMESE----------NYEGTMDPSQVPEHWPQEgeIKIHD 1316
Cdd:PRK15134 207 NMGLLF---ITHNLS-IVRKLADRVAVMQNGRCVeqNRAATLFSApthpytqkllNSEPSGDPVPLPEPASPL--LDVEQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1317 LCVRYE---------NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGidiskLPLHTL-- 1385
Cdd:PRK15134 281 LQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDG-----QPLHNLnr 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 ------RSRLSIILQDPilfSGSIRFNLDPEckctdDRLWEALEI-------AQLKNMVKSLPG--GLDAVV-----TEg 1445
Cdd:PRK15134 355 rqllpvRHRIQVVFQDP---NSSLNPRLNVL-----QIIEEGLRVhqptlsaAQREQQVIAVMEevGLDPETrhrypAE- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1446 genFSVGQRQLFCLARAFVRKSSILIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVHTILT-ADLVI 1517
Cdd:PRK15134 426 ---FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY-----LFISHDLHVVRAlCHQVI 497
|
....*....
gi 110832837 1518 VMKRGNILE 1526
Cdd:PRK15134 498 VLRQGEVVE 506
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
688-912 |
1.04e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.94 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL--EGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKP-WLLNA 764
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLL-RVFNRLIELypEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFGSPFNK---------QRYKAVTDACSLQPDIdllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 835
Cdd:PRK14247 98 SIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 836 DDPFSALDIHLSDHLmqEGILKFLQDDKrTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDIQTKDV-ELYEHWKT 912
Cdd:PRK14247 171 DEPTANLDPENTAKI--ESLFLELKKDM-TIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRhELTEKYVT 246
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
688-899 |
1.75e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAIL--------GEMqTLEGK-VHWSNVNESEpsfeatrsrnRYSVAYAAQK 758
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLM-KILsgvyqpdsGEI-LLDGEpVRFRSPRDAQ----------AAGIAIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 759 PWLL-NATVEENITFGSPFNK----------QRYKAVTDacSLQPDIDLlpfgdQTEIGErginLSGGQRQRICVARALY 827
Cdd:COG1129 88 LNLVpNLSVAENIFLGREPRRgglidwramrRRARELLA--RLGLDIDP-----DTPVGD----LSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 828 QNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
684-871 |
2.39e-12 |
|
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: 67.38 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnvnESEPSFEATRSRNRySVAYAAQKPWLLN 763
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW----NGTPLAEQRDEPHE-NILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 A-TVEENITFGSPFNKQRYKAVTDACslqpdidllpfgdqTEIGERGIN------LSGGQRQRICVARALYQNTNIVFLD 836
Cdd:TIGR01189 87 ElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 110832837 837 DPFSALDI--------HLSDHLMQEGIlkflqddkrtLVLVTH 871
Cdd:TIGR01189 153 EPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1312-1547 |
2.77e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDP--ILFSGSIR-------FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARA 1462
Cdd:PRK13647 84 VFQDPddQVFSSTVWddvafgpVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1463 FVRKSSILIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPeSLLAQ 1536
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
250
....*....|.
gi 110832837 1537 ENGVFASFVRA 1547
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1312-1537 |
2.89e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlkpvLK-HVKAYIKPGQKVGICGRTGSGKSSL-SL-AFFRMVDifDGKIVIDGIDisklplHTL--- 1385
Cdd:PRK10771 2 LKLTDITWLYHH-----LPmRFDLTVERGERVAILGPSGAGKSTLlNLiAGFLTPA--SGSLTLNGQD------HTTtpp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 -RSRLSIILQDPILFSG-SIRFN----LDPECKCTDDRLWEALEIAQ---LKNMVKSLPGGLdavvteggenfSVGQRQL 1456
Cdd:PRK10771 69 sRRPVSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1457 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRV---HTILTADLVIVmkRGNILeYDTP- 1530
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLedaARIAPRSLVVA--DGRIA-WDGPt 214
|
....*..
gi 110832837 1531 ESLLAQE 1537
Cdd:PRK10771 215 DELLSGK 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
688-894 |
3.29e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.46 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN-----VNESEPSFEATRS------RNRYSVAYAA 756
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDGQLKVADKnqlrllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 757 QKPWLlNATVEENI------TFGSPFNKQRYKAVTdacslqpdidllpFGDQTEIGERG-----INLSGGQRQRICVARA 825
Cdd:PRK10619 101 FNLWS-HMTVLENVmeapiqVLGLSKQEARERAVK-------------YLAKVGIDERAqgkypVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 826 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 894
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
692-873 |
3.86e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 692 DIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ------TLEGKVHwsnvNESEPSfeatrsrnRYSVAYAAQKPWLLN-A 764
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTpasgslTLNGQDH----TTTPPS--------RRPVSMLFQENNLFShL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFG-------SPFNKQRYKAVTDACSLQPDIDLLPfgdqteiGErginLSGGQRQRICVARALYQNTNIVFLDD 837
Cdd:PRK10771 87 TVAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 110832837 838 PFSALDihlsDHLMQEgILKFLQD--DKR--TLVLVTHKL 873
Cdd:PRK10771 156 PFSALD----PALRQE-MLTLVSQvcQERqlTLLMVSHSL 190
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1312-1537 |
4.11e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.34 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFD----GKIVIDGIDISKLP---L 1382
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINLLErptsGSVLVDGVDLTALSereL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1383 HTLRSRLSIILQDpilfsgsirFNLdpeckctddrLWE---------ALEIA-----QLKNMVKSLpggLDAVVTEGGEN 1448
Cdd:COG1135 78 RAARRKIGMIFQH---------FNL----------LSSrtvaenvalPLEIAgvpkaEIRKRVAEL---LELVGLSDKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1449 F-----SVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENIL---QKVvmtafADR---TVVTIAHRVHTILT-ADL 1515
Cdd:COG1135 136 AypsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIVLITHEMDVVRRiCDR 210
|
250 260
....*....|....*....|....*....
gi 110832837 1516 VIVMKRGNILEYDT-------PESLLAQE 1537
Cdd:COG1135 211 VAVLENGRIVEQGPvldvfanPQSELTRR 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1312-1524 |
5.26e-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: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPlhtLRS 1387
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIagleEPTSGRIYIGGRDVTDLP---PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 R-LSIILQDPILFS-----GSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1457
Cdd:cd03301 72 RdIAMVFQNYALYPhmtvyDNIAFGLKlrkvPK-DEIDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1458 CLARAFVRKSSILIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNI 1524
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
688-899 |
5.83e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.33 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQ----TLEGKvhwsNVNESEPSFEATRSRnrysVAYAAQK--- 758
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPDsgtiTVDGE----DLTDSKKDINKLRRK----VGMVFQQfnl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 759 -PwllNATVEENITFGsP---FNKQRYKAVTDAcslqpdIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNT 830
Cdd:COG1126 89 fP---HLTVLENVTLA-PikvKKMSKAEAEERA------MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 831 NIVFLDDPFSALDIHLSdhlmQE--GILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 899
Cdd:COG1126 156 KVMLFDEPTSALDPELV----GEvlDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
672-924 |
7.03e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.58 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFsW--GSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---VNESEPSFEATRS 746
Cdd:PRK15079 20 IKDGKQWF-WqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 rnrySVAYAAQKPWL-LNA--TVEENI-----TFGSPFNKQ----RYKAVTDACSLQPDIdllpfgdqteigergIN--- 811
Cdd:PRK15079 99 ----DIQMIFQDPLAsLNPrmTIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNL---------------INryp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 812 --LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIA 884
Cdd:PRK15079 160 heFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLV 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 110832837 885 MKDGSVLREGTlkdiqtkDVELYEH-----WKTLMNR---QDQELEKD 924
Cdd:PRK15079 235 MYLGHAVELGT-------YDEVYHNplhpyTKALMSAvpiPDPDLERN 275
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1312-1538 |
7.57e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 67.03 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL-SLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1390
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1391 II---LQDPIL------------FSGSI-RF-NLDPECKCTDDRLWEALEIAQLKNM-VKSLpggldavvteggenfSVG 1452
Cdd:COG1119 82 LVspaLQLRFPrdetvldvvlsgFFDSIgLYrEPTDEQRERARELLELLGLAHLADRpFGTL---------------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1453 QRQLFCLARAFVRKSSILIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILTA-DLVIVMKRGNILEY 1527
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
250
....*....|.
gi 110832837 1528 DTPESLLAQEN 1538
Cdd:COG1119 225 GPKEEVLTSEN 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
683-904 |
7.65e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNVNESEPSfeatrSRNRYSVAYAAQKPW 760
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtlEIGGNPCARLTPA-----KAHQLGIYLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 761 LL-NATVEENITFGSPFNKQRYKAVTD-----ACSLQPDID--LLPFGDQteigerginlsggqrQRICVARALYQNTNI 832
Cdd:PRK15439 97 LFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDSSagSLEVADR---------------QIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 833 VFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 904
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
688-875 |
7.94e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.04 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIlGEMQTLEG--------KVHWSNVNESEPSFEAtrsrnrysvAYAAQKP 759
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSgdlivdglKVNDPKVDERLIRQEA---------GMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 760 WLL-NATVEENITFGSpfnkQRYKAVTDACSLQPDIDLLpfgDQTEIGERG----INLSGGQRQRICVARALYQNTNIVF 834
Cdd:PRK09493 87 YLFpHLTALENVMFGP----LRVRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110832837 835 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY 875
Cdd:PRK09493 160 FDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGF 198
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
675-901 |
1.10e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.02 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 675 TNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNR----- 749
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRdiqmv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 750 YSVAYAAQKP-----WLLNATVEENITFGSPFNKQRYKAVTDACSLQPDI-DLLPfgdqteigergINLSGGQRQRICVA 823
Cdd:PRK10419 95 FQDSISAVNPrktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRP-----------PQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 824 RALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKL---QYLTHAdwIIAMKDGSVLREGTL 896
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQQFgtacLFITHDLrlvERFCQR--VMVMDNGQIVETQPV 236
|
....*
gi 110832837 897 KDIQT 901
Cdd:PRK10419 237 GDKLT 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
688-908 |
1.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.08 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKP--WLLNAT 765
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPesQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITFGsPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGERG-INLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 844
Cdd:PRK13649 103 VLKDVAFG-PQNFGVSQEEAEALARE---KLALVGISESLFEKNpFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 845 HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIqTKDVELYE 908
Cdd:PRK13649 179 KGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDI-FQDVDFLE 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1312-1526 |
1.41e-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: 65.24 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLHtLRSRL 1389
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAktIMGHPKYEVTEGEILFKGEDITDLPPE-ERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIIL--QDPILFSGsirfnldpeckctddrlwealeiAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKS 1467
Cdd:cd03217 78 GIFLafQYPPEIPG-----------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1468 SILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAH--RVHTILTADLVIVMKRGNILE 1526
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1312-1545 |
1.77e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 65.72 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRS 1387
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFEtptsGEILLDGKDITNLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQDPILF-----SGSIRFNLD----PEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1458
Cdd:cd03300 73 PVNTVFQNYALFphltvFENIAFGLRlkklPK-AEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESLL 1534
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
250
....*....|..
gi 110832837 1535 AQENGVF-ASFV 1545
Cdd:cd03300 220 EEPANRFvADFI 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1510 |
1.79e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHT 1384
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 LRSRLSIILQDPILFSGSIRFNLDPECKCT--------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQL 1456
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleiDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 1457 FCLARAFVRKSSILIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1510
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
680-909 |
1.81e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.56 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 680 SWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPsfeatRSRNrysVA---- 753
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEP-----ADRD---IAmvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 754 -YAaqkpwlL--NATVEENITFG-------SPFNKQRYKAVTDACSLQPDIDLLPfgdqteigeRgiNLSGGQRQRICVA 823
Cdd:PRK11650 84 nYA------LypHMSVRENMAYGlkirgmpKAEIEERVAEAARILELEPLLDRKP---------R--ELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 824 RALYQNTNiVFL-DDPFSALDIHLSDHLMQEgiLKFLQddKR---TLVLVTH-KLQYLTHADWIIAMKDGSVLREGTlkd 898
Cdd:PRK11650 147 RAIVREPA-VFLfDEPLSNLDAKLRVQMRLE--IQRLH--RRlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT--- 218
|
250
....*....|.
gi 110832837 899 iqtkDVELYEH 909
Cdd:PRK11650 219 ----PVEVYEK 225
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
689-871 |
2.19e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 689 SNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW--SNVNESEPSFeatrsrnRYSVAY----AAQKPWLl 762
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqgEPIRRQRDEY-------HQDLLYlghqPGIKTEL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 naTVEENITFgspfnkqrykavtdACSLQPDIDllpfGDQT-----EIGERGI------NLSGGQRQRICVARALYQNTN 831
Cdd:PRK13538 90 --TALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110832837 832 IVFLDDPFSALDI--------HLSDHLMQEGIlkflqddkrtLVLVTH 871
Cdd:PRK13538 150 LWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH 187
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
690-899 |
2.66e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.05 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH--WSNVNESepsfeATRSRNRYSV--AYAAqkpwLLNAT 765
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFidGEDVTHR-----SIQQRDICMVfqSYAL----FPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITFG-------SPFNKQRykaVTDACSLqpdIDLLPFGDqteigeRGIN-LSGGQRQRICVARALYQNTNIVFLDD 837
Cdd:PRK11432 95 LGENVGYGlkmlgvpKEERKQR---VKEALEL---VDLAGFED------RYVDqISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 838 PFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK11432 163 PLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
674-899 |
2.75e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 674 VTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLllailGEMQTL-----EGKVHWSNVNESEPSFEATRSRn 748
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTL-----ARLLTMietptGGELYYQGQDLLKADPEAQKLL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 749 RYSVAYAAQKPW-LLN------ATVEE----NITFGSPFNKQRYKAVTDACSLQPD-IDLLP--FgdqteigerginlSG 814
Cdd:PRK11308 91 RQKIQIVFQNPYgSLNprkkvgQILEEplliNTSLSAAERREKALAMMAKVGLRPEhYDRYPhmF-------------SG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 815 GQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKLQYLTH-ADWIIAMKDGS 889
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQELglsyVFISHDLSVVEHiADEVMVMYLGR 232
|
250
....*....|
gi 110832837 890 VLREGTLKDI 899
Cdd:PRK11308 233 CVEKGTKEQI 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1312-1535 |
2.87e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.88 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1390
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1391 IILQDPI-LFSGSIrfnldpeckcTDDRLWEALEIAQL--KNMVKSLPGGLDAV-----VTEGGENFSVGQRQLFCLARA 1462
Cdd:PRK13642 85 MVFQNPDnQFVGAT----------VEDDVAFGMENQGIprEEMIKRVDEALLAVnmldfKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 1463 FVRKSSILIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLA 1535
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1338-1526 |
3.40e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1338 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirfNLDPEcKCT 1414
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-------SLDPR-QTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1415 DDRLWEALEIAQL---KNMVKSLPGGLDAV------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE- 1484
Cdd:PRK10261 421 GDSIMEPLRVHGLlpgKAAAARVAWLLERVgllpehAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRg 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1485 ---NI---LQKVVMTAFA----DRTVVT-IAHRvhtiltadlVIVMKRGNILE 1526
Cdd:PRK10261 501 qiiNLlldLQRDFGIAYLfishDMAVVErISHR---------VAVMYLGQIVE 544
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1311-1545 |
3.44e-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: 65.05 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1311 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLhtlRSR-L 1389
Cdd:cd03296 2 SIEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIILQDPILF-----SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1457
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRvkprserPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADRTVVTIAHRVH----TILTADLVIVMKRGNILEYDTPESL 1533
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTTVFVTHdqeeALEVADRVVVMNKGRIEQVGTPDEV 224
|
250
....*....|...
gi 110832837 1534 LAQENGVF-ASFV 1545
Cdd:cd03296 225 YDHPASPFvYSFL 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1312-1537 |
3.91e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHTL- 1385
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFGRNIYSPDVDPIe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 -RSRLSIILQDPILF---------SGSIRFN-LDPECKCTDDRLWEALEIAQL----KNMVKSLPGgldavvteggeNFS 1450
Cdd:PRK14267 83 vRREVGMVFQYPNPFphltiydnvAIGVKLNgLVKSKKELDERVEWALKKAALwdevKDRLNDYPS-----------NLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1451 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILTADLVIVMKRGNILE--- 1526
Cdd:PRK14267 152 GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgp 231
|
250
....*....|....*
gi 110832837 1527 ----YDTPESLLAQE 1537
Cdd:PRK14267 232 trkvFENPEHELTEK 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
688-906 |
4.32e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.49 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSfEATRSRNRYSVAYaaQKP--WLLNAT 765
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-NLWDIRNKAGMVF--QNPdnQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITFGsPFNkqrykavtdaCSLQPDidllpfgdqtEIGERGIN-----------------LSGGQRQRICVARALYQ 828
Cdd:PRK13633 103 VEEDVAFG-PEN----------LGIPPE----------EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 829 NTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIqTKDVEL 906
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI-FKEVEM 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1328-1537 |
5.14e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1328 VLKHVKAYIKPGQKVGICGRTGSGKSSlslAFFRMVDIF---DGKIVIDGIDISKLPLHTlRSRLSI--ILQDPILFSG- 1401
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVprdAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1402 ----------SIRFNLDPECKctDDRLWEALEIAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKSSILI 1471
Cdd:PRK10895 94 svydnlmavlQIRDDLSAEQR--EDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1472 MDEATASIDMATENILQKVVmTAFADR--TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLAQE 1537
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
688-896 |
5.37e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.45 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNVNESEPSFEATRS-RNRySVAYAAQKPWLL-NA 764
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLL-HLLGGLDTpTSGDVIFNGQPMSKLSSAAKAElRNQ-KLGFIYQFHHLLpDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFgsPF---NKQRYKAVTDACSLqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:PRK11629 103 TALENVAM--PLligKKKPAEINSRALEM-----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 842 LDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTL 896
Cdd:PRK11629 176 LDARNADSIFQ--LLGELNRLQGTAFLvVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1312-1538 |
6.10e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDP--ILFS---------GSIRFNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLA 1460
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEET--VAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1461 RAFVRKSSILIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLA 1535
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 110832837 1536 QEN 1538
Cdd:PRK13652 228 QPD 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
684-922 |
7.88e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKV--HWSNVNESE----PSF-------------- 741
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVALCEKCGyverPSKvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 742 ---------EATRSRNRYSVAYAAQKPWLL--NATVEENITfgSPFNKQRYKAVTdacSLQPDIDLLpfgDQTEIGER-- 808
Cdd:TIGR03269 92 eevdfwnlsDKLRRRIRKRIAIMLQRTFALygDDTVLDNVL--EALEEIGYEGKE---AVGRAVDLI---EMVQLSHRit 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 809 --GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDhLMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAM 885
Cdd:TIGR03269 164 hiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIWL 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 110832837 886 KDGSVLREGTLKDIQTKDVELYEhwktlMNRQDQELE 922
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAVFMEGVS-----EVEKECEVE 274
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
685-916 |
1.06e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.87 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNVNESEPSFEATRSRN-------------RYS 751
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDIYIGDKKNNHELITnpyskkiknfkelRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPD-IDLLPFGdqteigerginLSGGQRQRI 820
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFG-PVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 821 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ--LILDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEI 263
|
250
....*....|....*..
gi 110832837 900 QTkDVELYEHWKTLMNR 916
Cdd:PRK13631 264 FT-DQHIINSTSIQVPR 279
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
672-894 |
1.13e-10 |
|
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: 62.98 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGqLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVnesepsfEATRSRN--R 749
Cdd:cd03264 1 LQLENLTKRYGKKRA-LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ-------DVLKQPQklR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 750 YSVAYAAQKP-WLLNATVEENITF-----GSPfNKQRYKAVTDACSLqpdIDLLPFGDQtEIGErginLSGGQRQRICVA 823
Cdd:cd03264 72 RRIGYLPQEFgVYPNFTVREFLDYiawlkGIP-SKEVKARVDEVLEL---VNLGDRAKK-KIGS----LSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 824 RALYQNTNIVFLDDPFSALD----IHLSDHLMQEGilkflqdDKRTLVLVTHKLQ-YLTHADWIIAMKDGSVLREG 894
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
684-904 |
1.47e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHwsnVNESEPSFEATRSRNRySVAYAAQK-PWL 761
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPpSEGEIL---LDAQPLESWSSKAFAR-KVAYLPQQlPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNATVEENITFG--------SPFNKQRYKAVTDACSLqpdIDLLPFGdqteigERGIN-LSGGQRQRICVARALYQNTNI 832
Cdd:PRK10575 98 EGMTVRELVAIGrypwhgalGRFGAADREKVEEAISL---VGLKPLA------HRLVDsLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 833 VFLDDPFSALDI-HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGTLKDIQTKDV 904
Cdd:PRK10575 169 LLLDEPTSALDIaHQVDVLAL--VHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
671-895 |
1.62e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 671 AIKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTlEGKVHWSNVN---ESEPSFEATRS 746
Cdd:PRK11124 2 SIQLNGINCFYGAHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNHfdfSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 747 RnRYSVAYAAQK----PWLlnaTVEENITfGSP-----FNKQryKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQR 817
Cdd:PRK11124 80 L-RRNVGMVFQQynlwPHL---TVQQNLI-EAPcrvlgLSKD--QALARAEKLLERLRLKPYADRFPL-----HLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 818 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGT 895
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
666-890 |
1.64e-10 |
|
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: 63.72 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 666 ETEDIAIKVTNGyfswgsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTlEGKVHWSNVNESEPSFEATR 745
Cdd:cd03289 4 TVKDLTAKYTEG------GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SrnrySVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARA 825
Cdd:cd03289 77 K----AFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 826 LYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLTHADWIIAMKDGSV 890
Cdd:cd03289 153 VLSKAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1036-1205 |
1.81e-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: 63.60 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1036 VAGFSILCGAGIFLclvTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLT 1115
Cdd:cd18552 45 IIGLFLLRGLASYL---QTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1116 RSTLLCLSAIGMISYA----TPVFLVALLPLGVAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRH 1190
Cdd:cd18552 122 RDPLTVIGLLGVLFYLdwklTLIALVVLPLAALPIRRIGKRLRKISRRSQEsMGDLTS-----VLQETLSGIRVVKAFGA 196
|
170
....*....|....*
gi 110832837 1191 ETRFKQRMLELTDTN 1205
Cdd:cd18552 197 EDYEIKRFRKANERL 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
691-894 |
2.22e-10 |
|
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: 62.39 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 691 IDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRsrnRYSVAYAAQK--PWLlnaTVEE 768
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR---RLGFVSDSTGlyDRL---TARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 769 NITFGSPFNKQRYKAVTDAcsLQPDIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD 848
Cdd:cd03266 98 NLEYFAGLYGLKGDELTAR--LEELADRLGMEELLD--RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110832837 849 HLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 894
Cdd:cd03266 174 ALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
688-889 |
2.32e-10 |
|
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: 61.18 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILgemqtlegkvhwsnvnesepsfeATRSRNRYsvayaaqkpwllnatve 767
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-----------------------YASGKARL----------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 enITFGSPFNKQRYKAVTdacSLQPDIDL----LPFGDQTEigergiNLSGGQRQRICVARALYQNT-NIVF-LDDPFSA 841
Cdd:cd03238 51 --ISFLPKFSRNKLIFID---QLQFLIDVglgyLTLGQKLS------TLSGGELQRVKLASELFSEPpGTLFiLDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110832837 842 LDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGS 889
Cdd:cd03238 120 LHQQDINQLLEV--IKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1324-1533 |
2.57e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1324 NLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQDPiLFS 1400
Cdd:PRK15079 33 TLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddEWRAVRSDIQMIFQDP-LAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1401 GSIRFNLdpeckctDDRLWEALEI-------AQLKNMVKSL---PGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1470
Cdd:PRK15079 111 LNPRMTI-------GEIIAEPLRTyhpklsrQEVKDRVKAMmlkVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1471 IMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHR---VHTIltADLVIVMKRGNILEYDTPESL 1533
Cdd:PRK15079 184 ICDEPVSALDVSIQaqvvNLLQQ--LQREMGLSLIFIAHDlavVKHI--SDRVLVMYLGHAVELGTYDEV 249
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1316-1535 |
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 110832837 1316 DLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIIL 1393
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1394 QDP---ILFS---GSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKslpggldavvtEGGENFSVGQRQLFCLARAF 1463
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRnlgvPEAEITR-RVDEALTLVDAQHFRH-----------QPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1464 VRKSSILIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1535
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYeISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
669-890 |
2.95e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 669 DIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-SNVNesepsfeatrsr 747
Cdd:COG0488 313 KKVLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVK------------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 748 nrysVAYAAQKPWLL--NATVEENITFGSPFNKQRYkaVTDACSlqpdiDLLpF-GDQ--TEIGergiNLSGGQRQRICV 822
Cdd:COG0488 380 ----IGYFDQHQEELdpDKTVLDELRDGAPGGTEQE--VRGYLG-----RFL-FsGDDafKPVG----VLSGGEKARLAL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 823 ARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSV 890
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHDRYFLdRVATRILEFEDGGV 507
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
670-910 |
3.00e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.92 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 670 IAIKVTNGYFSWGSGLAT--LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS--NVNESEPSFEATR 745
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SRNRYSVAYAAQKPWLLNATVEENITFGsPFN------KQRYKAVT--DACSLQPD-IDLLPFgdqteigergiNLSGGQ 816
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFENTVLKDVEFG-PKNfgfsedEAKEKALKwlKKVGLSEDlISKSPF-----------ELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 817 RQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLT-HADWIIAMKDGSVLREGT 895
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHAS 228
|
250
....*....|....*
gi 110832837 896 LKDIQTKDVELYEHW 910
Cdd:PRK13641 229 PKEIFSDKEWLKKHY 243
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1530 |
3.75e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1344 ICGRTGSGKSSLSLAF----------FRMVDIFDG-KIVIDGIDISKLP-----LHTLRSRLSIILQDP--ILFSGSIRf 1405
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFnglikskygtIQVGDIYIGdKKNNHELITNPYSkkiknFKELRRRVSMVFQFPeyQLFKDTIE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1406 nldpeckctDDRLWEALEIAQLKNMVKSLPG------GLDAVVTEGGE-NFSVGQRQLFCLARAFVRKSSILIMDEATAS 1478
Cdd:PRK13631 136 ---------KDIMFGPVALGVKKSEAKKLAKfylnkmGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1479 IDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTP 1530
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLeVADEVIVMDKGKILKTGTP 260
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
812-899 |
3.83e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 62.55 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 812 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TLVLVTHKLQYLTH-ADWIIAMK 886
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiiNLMLE-----LQEKLGiSYIYVSQHLGIVKHiSDKVLVMH 224
|
90
....*....|...
gi 110832837 887 DGSVLREGTLKDI 899
Cdd:COG4167 225 QGEVVEYGKTAEV 237
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
672-908 |
3.87e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWG--SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnESEPSFEATRSRNR 749
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG--ELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 750 YSVAYAAQKPWLLNATVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFgdQTEIGERginLSGGQRQRICVARA 825
Cdd:PRK13642 83 IGMVFQNPDNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLA---VNMLDF--KTREPAR---LSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 826 LYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDV 904
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMR--VIHEIKEKYQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
....
gi 110832837 905 ELYE 908
Cdd:PRK13642 233 DMVE 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
686-901 |
3.88e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 686 ATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKP-WLL 762
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPnPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 NATVEENITFgsPF------NKQRYKAVTDACslqpdidLLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTNI 832
Cdd:PRK14246 104 HLSIYDNIAY--PLkshgikEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 833 VFLDDPFSALDIhlsdhLMQEGILKFLQDDKR--TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQT 901
Cdd:PRK14246 175 LLMDEPTSMIDI-----VNSQAIEKLITELKNeiAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1329-1535 |
4.06e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1329 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPI----------- 1397
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1398 LFSGSIRFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 1476
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPHML-----------APGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1477 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILT---ADLVIVMKRGNILEYDTPESLLA 1535
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMkhiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1065-1193 |
4.12e-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: 62.53 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1065 AKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP-VFLVALL--- 1140
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkLTLVMLLvvp 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 1141 PLGVAFYFIQKYFRVASKDLQE-LDDSTQLpllchfsetAE----GLTTIRAFRHETR 1193
Cdd:cd18573 153 PIAVGAVFYGRYVRKLSKQVQDaLADATKV---------AEerlsNIRTVRAFAAERK 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
685-893 |
4.60e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-----SNVNESEPSfeATRSRNrysVAYAAQKP 759
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplHQMDEEARA--KLRAKH---VGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 760 WL---LNATveENITFGSPFnkqryKAVTDACSLQPDIDLLpfgDQTEIGER----GINLSGGQRQRICVARALYQNTNI 832
Cdd:PRK10584 98 MLiptLNAL--ENVELPALL-----RGESSRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 833 VFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSvLRE 893
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIA-DLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ-LQE 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
683-904 |
5.30e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNV--NESEPSFEAtrsRNRYSVAYaaQKPW 760
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAA---QLGIGIIY--QELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 761 LLNA-TVEENITFGS-PFNKQRYKAVTDACSLQ--PDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 836
Cdd:PRK09700 91 VIDElTVLENLYIGRhLTKKVCGVNIIDWREMRvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 837 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDIQTKDV 904
Cdd:PRK09700 171 EPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
688-871 |
5.34e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnvnesepsfeatrsRNRYSVAYAAQKPWLL-NATV 766
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------------PKGLRIGYLPQEPPLDdDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFG-SPFNK--QRYKAVTDACSlQPDIDLLPFGD-QTEIGER----------------GI----------NLSGGQ 816
Cdd:COG0488 79 LDTVLDGdAELRAleAELEELEAKLA-EPDEDLERLAElQEEFEALggweaearaeeilsglGFpeedldrpvsELSGGW 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 817 RQRICVARALYQNTNIVFLDDPFSALDIhlsdhlmqEGIL---KFLQDDKRTLVLVTH 871
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDL--------ESIEwleEFLKNYPGTVLVVSH 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1313-1483 |
5.78e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.96 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1313 KIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAF--------FRmvdiFDGKIVIDGIDISKLPlhT 1384
Cdd:COG4136 3 SLENLTITLGG--RPLLAPLSLTVAPGEILTLMGPSGSGKSTL-LAAiagtlspaFS----ASGEVLLNGRRLTALP--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 LRSRLSIILQDPILFS-----GSIRFNLDPECKCTD--DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 1457
Cdd:COG4136 74 EQRRIGILFQDDLLFPhlsvgENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPATL-----------SGGQRARV 142
|
170 180
....*....|....*....|....*.
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDMAT 1483
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAAL 168
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1312-1537 |
7.06e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:PRK09536 4 IDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPilfsgSIRFNLDPE----------------CKCTDDRLWE-ALEiaqlknmvkslPGGLDAVVTEGGENFSVGQR 1454
Cdd:PRK09536 82 VPQDT-----SLSFEFDVRqvvemgrtphrsrfdtWTETDRAAVErAME-----------RTGVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1455 QLFCLARAFVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLTA---DLVIVMKRGNILEYDTP 1530
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPP 223
|
....*..
gi 110832837 1531 ESLLAQE 1537
Cdd:PRK09536 224 ADVLTAD 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
684-905 |
7.57e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWSnvnESEPSFEATRSRNRYSVAYAAQKPWL 761
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWS---GSPLKASNIRDTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 L-NATVEENITFGS----PFNKQRYKAVTDAC-------SLQPDIDLLPFGDqteigerginLSGGQRQRICVARALYQN 829
Cdd:TIGR02633 90 VpELSVAENIFLGNeitlPGGRMAYNAMYLRAknllrelQLDADNVTRPVGD----------YGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 830 TNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKDVE 905
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLD--IIRDLKAHGVACVYISHKL------NEVKAVCDTiCVIRDG--QHVATKDMS 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1278-1540 |
9.05e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1278 AVKKVNSFltmESENYEGTMDPSQVPEHWPQegeIKIHDLCVRYENN---LKPVlkhvKAYIKPGQKVGICGRTGSGKSS 1354
Cdd:PRK10522 295 AFNKLNKL---ALAPYKAEFPRPQAFPDWQT---LELRNVTFAYQDNgfsVGPI----NLTIKRGELLFLIGGNGSGKST 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1355 LSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSirfnLDPECKCTDDRLWEA-LEIAQLKNMVKs 1433
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLE- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1434 lpggldavvTEGGE----NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRV 1507
Cdd:PRK10522 440 ---------LEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDD 510
|
250 260 270
....*....|....*....|....*....|...
gi 110832837 1508 HTILTADLVIVMKRGNILEYDTPESLLAQENGV 1540
Cdd:PRK10522 511 HYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
684-894 |
1.32e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRYSVAYAAQKPWLL- 762
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---IDGQEMRFASTTAALAAGVAIIYQELHLVp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 NATVEENITFGS-P-----FNKQRYKAVTDACSLQPDIDLLPfgdQTEIGErginLSGGQRQRICVARALYQNTNIVFLD 836
Cdd:PRK11288 93 EMTVAENLYLGQlPhkggiVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 837 DPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREG 894
Cdd:PRK11288 166 EPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
687-899 |
1.40e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.80 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNVNESEPSfEATRSRNRYSVAYAAQKP--WLLNA 764
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI---TVGGMVLS-EETVWDVRRQVGMVFQNPdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFGSPFN----KQRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 840
Cdd:PRK13635 98 TVQDDVAFGLENIgvprEEMVERVDQALRQ---VGMEDFLNREPH-----RLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 841 ALDIHLSDHLMqeGILKFLQDDKRTLVL-VTHKLQYLTHADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK13635 170 MLDPRGRREVL--ETVRQLKEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1311-1505 |
1.44e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1311 EIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI--SKLPLH 1383
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1384 TLRSRLSIILQDPILFSGSIRFNLDPECKCT------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQLF 1457
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1505
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
690-899 |
1.49e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.43 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPS-FEATRSRNrysVAYAAQKPWLL-NAT 765
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvLFDAEKGiCLPPEKRR---IGYVFQDARLFpHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 844
Cdd:PRK11144 93 VRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 845 HLSDHLMQegILKFLQDDKRTLVL-VTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK11144 162 PRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
688-909 |
1.51e-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: 59.46 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEmqtlegkvhwsnvnesePSFEATRSRnrysVAYAAQKpwLLNATVE 767
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-----------------PKYEVTEGE----ILFKGED--ITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 768 EN------ITFGSPFnkqRYKAVTDAcslqpdiDLLpfgdqteigeRGIN--LSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:cd03217 73 ERarlgifLAFQYPP---EIPGVKNA-------DFL----------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 840 SALDIhlsDHL-MQEGILKFLQDDKRTLVLVTHKLQYLTH--ADWIIAMKDGSVLREGtlkdiqtkDVELYEH 909
Cdd:cd03217 133 SGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSG--------DKELALE 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1326-1545 |
1.56e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 61.78 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1326 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLHtlRSRLSIILQDPILF-- 1399
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEqptaGQIMLDGVDLSHVPPY--QRPINMMFQSYALFph 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1400 ---SGSIRFNLD----PECKCTDdRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 1472
Cdd:PRK11607 106 mtvEQNIAFGLKqdklPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1473 DEATASID------MATE--NILQKVVMTAfadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF-A 1542
Cdd:PRK11607 174 DEPMGALDkklrdrMQLEvvDILERVGVTC------VMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYsA 247
|
...
gi 110832837 1543 SFV 1545
Cdd:PRK11607 248 EFI 250
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1312-1505 |
1.81e-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: 57.84 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmvdifdgkividgidisklplhtlrsrLSI 1391
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPILFSGSIRFNldpeckctddrlwEALEIAQLknmvkslpggldavvteggENFSVGQRQLFCLARAFVRKSSILI 1471
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 110832837 1472 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1505
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1255-1536 |
1.85e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.13 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1255 ALTITNYLNWVVRNLADLEVQM--GAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHV 1332
Cdd:TIGR03269 221 SMVLTSHWPEVIEDLSDKAIWLenGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKAV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1333 KAY---IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI----DGIDISKlPLHTLRSR----LSIILQDPILFSG 1401
Cdd:TIGR03269 301 DNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTK-PGPDGRGRakryIGILHQEYDLYPH 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1402 SIRFnldpeckctdDRLWEAL------EIAQLKNMVKSLPGGLD-----AVVTEGGENFSVGQRQLFCLARAFVRKSSIL 1470
Cdd:TIGR03269 380 RTVL----------DNLTEAIglelpdELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1471 IMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLdVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
989-1205 |
1.94e-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: 60.64 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 989 GGFFLLILMIFSKLLKHSVIVAIDYWLATWtseysinntgkadqtyYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNL 1068
Cdd:cd07346 11 ATALGLALPLLTKLLIDDVIPAGDLSLLLW----------------IALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1069 HHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPL---GV 1144
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALViLFYLNWKLTLVALLLLplyVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1145 AFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTN 1205
Cdd:cd07346 155 ILRYFRRRIRKASREVREsLAELSA-----FLQESLSGIRVVKAFAAEEREIERFREANRDL 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1329-1540 |
1.99e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1329 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP----LHTLRSRLSIILQDP-------- 1396
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQFPesqlfedt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1397 ----ILFsGSIRFNLDPEcKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIM 1472
Cdd:PRK13646 103 vereIIF-GPKNFKMNLD-EVKNYAHRLLMDLGFSRDVMSQSPFQM-----------SGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1473 DEATASIDMATenilQKVVMTAFA------DRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGV 1540
Cdd:PRK13646 170 DEPTAGLDPQS----KRQVMRLLKslqtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1327-1524 |
2.33e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1327 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfdGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG-- 1401
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDS--GTLEIGGNPCARLtPAKAHQLGIYLVPQEPLLFPNls 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1402 ---SIRFNLdPEckctddrlwEALEIAQLKNMVKSLPGGLDAVVTEGgeNFSVGQRQLFCLARAFVRKSSILIMDEATAS 1478
Cdd:PRK15439 103 vkeNILFGL-PK---------RQASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110832837 1479 IDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNI 1524
Cdd:PRK15439 171 LTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1311-1537 |
2.37e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1311 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 1390
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1391 IILQDPILFSG-SIR----------FNLDPECKCTDDRLWE-ALEIAQLKNMVkslpgglDAVVTEggenFSVGQRQLFC 1458
Cdd:PRK11231 80 LLPQHHLTPEGiTVRelvaygrspwLSLWGRLSAEDNARVNqAMEQTRINHLA-------DRRLTD----LSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTP 228
|
.
gi 110832837 1537 E 1537
Cdd:PRK11231 229 G 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
688-909 |
2.38e-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: 59.71 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEM-----QTLE------GKVHWSNVnesepsfeatRSRNRYsVAYAA 756
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygNDVRlfgerrGGEDVWEL----------RKRIGL-VSPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 757 QKPWLLNATVEENIT---FGSPFnkqRYKAVTDAcslqpDI----DLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQ 828
Cdd:COG1119 88 QLRFPRDETVLDVVLsgfFDSIG---LYREPTDE-----QRerarELLELLGLAHLADRPFGtLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 829 NTNIVFLDDPFSALDIHlsdhlMQEGILKFL----QDDKRTLVLVTHKLQYL----THAdwiIAMKDGSVLREGTLKDIQ 900
Cdd:COG1119 160 DPELLILDEPTAGLDLG-----ARELLLALLdklaAEGAPTLVLVTHHVEEIppgiTHV---LLLKDGRVVAAGPKEEVL 231
|
250
....*....|.
gi 110832837 901 TKDV--ELYEH 909
Cdd:COG1119 232 TSENlsEAFGL 242
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
991-1203 |
2.44e-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: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 991 FFLLILMIFSKLLkhsvIVAIDYWLATWTSEYSINNTGKADQTY-YVAGFSILCGAGIFLCLVTSLTVEWMGLTAA---- 1065
Cdd:cd18547 2 ILVIILAIISTLL----SVLGPYLLGKAIDLIIEGLGGGGGVDFsGLLRILLLLLGLYLLSALFSYLQNRLMARVSqrtv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1066 KNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPLGV 1144
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLImMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 1145 AFYFI-------QKYFRVASKDLQELDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTD 1203
Cdd:cd18547 158 SLLVTkfiakrsQKYFRKQQKALGELNGYIE--------EMISGQKVVKAFNREEEAIEEFDEINE 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1327-1534 |
2.93e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1327 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRLSIILQdpilfsgsiR 1404
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQ---------Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1405 FNLDPECKCTDDRLWEALEI-----AQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1477
Cdd:PRK09493 86 FYLFPHLTALENVMFGPLRVrgaskEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1478 SIDmatENILQKV--VMTAFADR----TVVT----IAHRVHTILtadlvIVMKRGNILEYDTPESLL 1534
Cdd:PRK09493 166 ALD---PELRHEVlkVMQDLAEEgmtmVIVTheigFAEKVASRL-----IFIDKGRIAEDGDPQVLI 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1312-1483 |
4.41e-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: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKL---PLHTL 1385
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPTsGTVRLAGQDLFALdedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1386 RSR-LSIILQD---------------PILFSGsirfnlDPECKctdDRLWEALEIAQLKNMVKSLPGGLdavvtEGGEnf 1449
Cdd:COG4181 88 RARhVGFVFQSfqllptltalenvmlPLELAG------RRDAR---ARARALLERVGLGHRLDHYPAQL-----SGGE-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 110832837 1450 svgqRQLFCLARAFVRKSSILIMDEATASIDMAT 1483
Cdd:COG4181 152 ----QQRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1328-1540 |
5.12e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.32 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1328 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKLPLHTLRSRLSIILQDP--ILFSGSI 1403
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1404 R-------FNLdpeckctddrlweALEIAQLKNMVKSlpgGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILI 1471
Cdd:PRK13639 97 EedvafgpLNL-------------GLSKEEVEKRVKE---ALKAVGMEGFENkpphhLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1472 MDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYDTPESLLAQENGV 1540
Cdd:PRK13639 161 LDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
639-871 |
5.36e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.84 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 639 PKTINRKQPGRYHLDSYEQSTRRlrPAETEDIAIKVTNGYFSWGsGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI 718
Cdd:PRK13536 11 PRRLELSPIERKHQGISEAKASI--PGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 719 LGEMQTLEGKVhwSNVNESEPSfEATRSRNRYSVAyaAQKPWL-LNATVEEN-ITFGSPF--NKQRYKAVTDAcslqpdi 794
Cdd:PRK13536 88 LGMTSPDAGKI--TVLGVPVPA-RARLARARIGVV--PQFDNLdLEFTVRENlLVFGRYFgmSTREIEAVIPS------- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 795 dLLPFGD-QTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKrTLVLVTH 871
Cdd:PRK13536 156 -LLEFARlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1312-1531 |
5.42e-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: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYeNNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHtLRS 1387
Cdd:cd03219 1 LEVRGLTKRF-GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLISGFlrptSGSVLFDGEDITGLPPH-EIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSII--LQDPILFSG-SIRFNLD-----------------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvtegge 1447
Cdd:cd03219 74 RLGIGrtFQIPRLFPElTVLENVMvaaqartgsglllararREEREARERAEELLERVGLADLADRPAGEL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1448 nfSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNIL 1525
Cdd:cd03219 145 --SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
....*.
gi 110832837 1526 EYDTPE 1531
Cdd:cd03219 223 AEGTPD 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
683-905 |
6.43e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG--EMQTLEGKVHWS-------NVNESEpsfeatrsrnRYSVA 753
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEgeelqasNIRDTE----------RAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 754 YAAQKPWLL-NATVEENITFGS---PFNKQRYKAVTDACS-----LQPDIDLlpfgdQTEIGergiNLSGGQRQRICVAR 824
Cdd:PRK13549 86 IIHQELALVkELSVLENIFLGNeitPGGIMDYDAMYLRAQkllaqLKLDINP-----ATPVG----NLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 825 ALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLqylthaDWIIAMKDG-SVLREGtlKDIQTKD 903
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLD--IIRDLKAHGIACIYISHKL------NEVKAISDTiCVIRDG--RHIGTRP 226
|
..
gi 110832837 904 VE 905
Cdd:PRK13549 227 AA 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
688-893 |
6.52e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.56 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRYsVAYAAQKPwLL----N 763
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL---IDGKDVTKLPEYKRAKY-IGRVFQDP-MMgtapS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 ATVEENI----------TFGSPFNKQRYKAVTDACSlqpDIDL-----LpfgdQTEIGergiNLSGGQRQRICVARALYQ 828
Cdd:COG1101 97 MTIEENLalayrrgkrrGLRRGLTKKRRELFRELLA---TLGLglenrL----DTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 829 NTNIVFLDDPFSALDIHLSDHLMQegiL--KFLQDDKRTLVLVTHKLQY-LTHADWIIAMKDGSVLRE 893
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRLIMMHEGRIILD 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
685-888 |
8.46e-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: 57.83 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILgEMQTlEGKVHWSNVNESEPSFEA-TRSRNRySVAYAAQKPWL 761
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLglLAGL-DRPT-SGTVRLAGQDLFALDEDArARLRAR-HVGFVFQSFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNA-TVEENIT-----FGSPFNKQRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVARALYQNTNIVFL 835
Cdd:COG4181 102 LPTlTALENVMlplelAGRRDARARARALLERVGLGHRLDHYP--AQ---------LSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 836 DDPFSALDIHLSDHLMQegiLKF-LQDDKR-TLVLVTHKLQYLTHADWIIAMKDG 888
Cdd:COG4181 171 DEPTGNLDAATGEQIID---LLFeLNRERGtTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
687-890 |
9.55e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.20 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 687 TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnVNESEPSFEATRSRNRYSVAYAAQKP--WLLNA 764
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI----IIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFGSPfNK-----QRYKAVTDACSLqpdIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:PRK13650 98 TVEDDVAFGLE-NKgipheEMKERVNEALEL---VGMQDFKEREPA-----RLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 840 SALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSV 890
Cdd:PRK13650 169 SMLDPEGRLELIKT-IKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
688-899 |
1.12e-08 |
|
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: 58.53 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNVN---ESEPSFEATRSRNrysVAYAAQKPwl 761
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDllkLSEKELRKIRGRE---IQMIFQDP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNA-----TVEENIT-------FGSPfnKQRYKAVtdacslqpdIDLLpfgdqteigER-GIN------------LSGGQ 816
Cdd:COG0444 96 MTSlnpvmTVGDQIAeplrihgGLSK--AEARERA---------IELL---------ERvGLPdperrldrypheLSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 817 RQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL---QYLthADWIIAMKDGS 889
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITHDLgvvAEI--ADRVAVMYAGR 228
|
250
....*....|
gi 110832837 890 VLREGTLKDI 899
Cdd:COG0444 229 IVEEGPVEEL 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
666-903 |
1.32e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 666 ETEDIAikvtngyFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnVNESEPSFEATR 745
Cdd:PRK13652 5 ETRDLC-------YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV----LIRGEPITKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 746 SRNRYSVAYAAQKP--WLLNATVEENITFGsPFN--------KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGG 815
Cdd:PRK13652 74 REVRKFVGLVFQNPddQIFSPTVEQDIAFG-PINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 816 QRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmqegiLKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSV 890
Cdd:PRK13652 142 EKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL-----IDFLNDLPEtygmTVIFSTHQLDLVPEmADYIYVMDKGRI 216
|
250
....*....|...
gi 110832837 891 LREGTLKDIQTKD 903
Cdd:PRK13652 217 VAYGTVEEIFLQP 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
683-890 |
1.38e-08 |
|
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: 56.29 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRYSVAYAA----QK 758
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT---LDGKPVTRRSPRDAIRAGIAYVPedrkRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 759 PWLLNATVEENITFGSPfnkqrykavtdacslqpdidllpfgdqteigerginLSGGQRQRICVARALYQNTNIVFLDDP 838
Cdd:cd03215 88 GLVLDLSVAENIALSSL------------------------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110832837 839 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSV 890
Cdd:cd03215 132 TRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
688-894 |
1.55e-08 |
|
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: 56.52 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvnesEPSFEATRSRnrysVAYAAQKPWL-LNATV 766
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNR----IGYLPEERGLyPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EEN-ITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 845
Cdd:cd03269 88 IDQlVYLAQLKGLKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110832837 846 LSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 894
Cdd:cd03269 163 NVELLKDV--IRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1336-1544 |
2.22e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.81 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1336 IKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKlplHTLRSR-LSIILQDPILFSG-SIRFNL-- 1407
Cdd:PRK11432 29 IKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmSLGENVgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1408 --------DPECKctdDRLWEALEIAQLKnmvkslpGGLDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI 1479
Cdd:PRK11432 102 glkmlgvpKEERK---QRVKEALELVDLA-------GFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1480 D------MaTENI--LQKVVmtafaDRTVVTIAH-RVHTILTADLVIVMKRGNILEYDTPESLLAQENGVF-ASF 1544
Cdd:PRK11432 168 DanlrrsM-REKIreLQQQF-----NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFmASF 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1312-1538 |
2.30e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 1391
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPIL-FSGS----IRFNLDP--ECKCTDDRLWEA----LEIAQLKNmvKSLPggldavVTEGGENfsvgQR-QlfcL 1459
Cdd:PRK13548 81 LPQHSSLsFPFTveevVAMGRAPhgLSRAEDDALVAAalaqVDLAHLAG--RDYP------QLSGGEQ----QRvQ---L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1460 ARAFVR------KSSILIMDEATASIDMATenilQKVVMTA---FADR---TVVTIAHRVH-TILTADLVIVMKRGNILE 1526
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDLAH----QHHVLRLarqLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVA 221
|
250
....*....|..
gi 110832837 1527 YDTPESLLAQEN 1538
Cdd:PRK13548 222 DGTPAEVLTPET 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
703-947 |
2.42e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.41 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 703 IVGQVGCGKSSLLLAILGEMQTLEGkvhwsnvnesepsfEATRSRNrYSVAYAAQKPWL-LNATVEENITFGSPFNKQ-- 779
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQPG-IKVGYLPQEPQLdPTKTVRENVEEGVAEIKDal 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 780 -RYKAVTDACS---------------LQPDIDL------------------LPFGDQtEIGergiNLSGGQRQRICVARA 825
Cdd:TIGR03719 101 dRFNEISAKYAepdadfdklaaeqaeLQEIIDAadawdldsqleiamdalrCPPWDA-DVT----KLSGGERRRVALCRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 826 LYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG-SVLREGTlkdiq 900
Cdd:TIGR03719 176 LLSKPDMLLLDEP--------TNHLDAESVAwleRHLQEYPGTVVAVTHDRYFLDNvAGWILELDRGrGIPWEGN----- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 110832837 901 tkdvelYEHW---KTlmNRQDQElEKDMEADQTTLERKT--LRRAMYSREAK 947
Cdd:TIGR03719 243 ------YSSWleqKQ--KRLEQE-EKEESARQKTLKRELewVRQSPKGRQAK 285
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1312-1528 |
2.51e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHT-- 1384
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 LRSRLSIILQDPILFSGSI--------RFNLDPECKCTDDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQL 1456
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1457 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEYD 1528
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYN 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1327-1531 |
3.47e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1327 PVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LA-FFRMvDifDGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFSG- 1401
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMkiLSgVYQP-D--SGEILLDGEPVRFRsPRDAQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1402 SIRFNL------------DpeckctddrlWEALeIAQLKNMVKSLpgGLD----AVVteggENFSVGQRQLFCLARAFVR 1465
Cdd:COG1129 95 SVAENIflgreprrggliD----------WRAM-RRRARELLARL--GLDidpdTPV----GDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1466 KSSILIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRG-NILEYDTPE 1531
Cdd:COG1129 158 DARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGrLVGTGPVAE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
660-899 |
4.02e-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: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 660 RRLRPAETEDIAIKVTN---GYFSWGSGLA-TLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH----- 730
Cdd:TIGR03269 268 EKECEVEVGEPIIKVRNvskRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgd 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 731 -WsnVNESEPSFEAtRSRNRYSVAYAAQKPWLL-NATVEENIT----FGSPFNKQRYKAVtdacslqpdIDLLPFGDQTE 804
Cdd:TIGR03269 348 eW--VDMTKPGPDG-RGRAKRYIGILHQEYDLYpHRTVLDNLTeaigLELPDELARMKAV---------ITLKMVGFDEE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 805 IGERGIN-----LSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQY-LTH 878
Cdd:TIGR03269 416 KAEEILDkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMD-PITKVDVTHSILKAREEMEQTFIIVSHDMDFvLDV 494
|
250 260
....*....|....*....|.
gi 110832837 879 ADWIIAMKDGSVLREGTLKDI 899
Cdd:TIGR03269 495 CDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
671-894 |
4.06e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 671 AIKVTNGYfswgSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRS--RN 748
Cdd:PRK14271 24 AVNLTLGF----AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDvlEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 749 RYSVAYAAQKPWLLNATVEENITFGSPFNK----QRYKAVTDACSLQPDI-DLLpfgdQTEIGERGINLSGGQRQRICVA 823
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVGLwDAV----KDRLSDSPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 824 RALYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFLQD--DKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREG 894
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTT-----EKIEEFIRSlaDRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1339-1536 |
4.14e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1339 GQKVGICGRTGSGKSSLSLAFFRMV---DIFDGKIVIDGIDISKLP---LHTLRS-RLSIILQDPILfsgsirfNLDPEC 1411
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGLLaanGRIGGSATFNGREILNLPekeLNKLRAeQISMIFQDPMT-------SLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1412 KCTDdrlwEALEIAQL-KNMVKSLP-----GGLDAV--------VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 1477
Cdd:PRK09473 115 RVGE----QLMEVLMLhKGMSKAEAfeesvRMLDAVkmpearkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1478 SID-------MATENILQKVVMTAfadrtVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:PRK09473 191 ALDvtvqaqiMTLLNELKREFNTA-----IIMITHDLGVVAgICDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
688-899 |
4.46e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.01 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLL--LAILgEMQTlEGKVHWSNVNESepSFEATRSRN-RYSVAYAAQKPWLLNA 764
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLL-ERPT-SGSVLVDGVDLT--ALSERELRAaRRKIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 -TVEENITF-----GSPfNKQRYKAVTDacslqpdidLLPFgdqTEIGERG----INLSGGQRQRICVARALYQNTNIVF 834
Cdd:COG1135 97 rTVAENVALpleiaGVP-KAEIRKRVAE---------LLEL---VGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 835 LDDPFSALDIHLSDhlmqeGILKFLQDDKR----TLVLVTH------KLqylthADWIIAMKDGSVLREGTLKDI 899
Cdd:COG1135 164 CDEATSALDPETTR-----SILDLLKDINRelglTIVLITHemdvvrRI-----CDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1316-1528 |
4.52e-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: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1316 DLCVRYENNLKPVlkHVK-AYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDG---IDISK---LPLHt 1384
Cdd:cd03297 1 MLCVDIEKRLPDF--TLKiDFDLNEEVTGIFGASGAGKSTL----LRCIagleKPDGGTIVLNGtvlFDSRKkinLPPQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 lRSRLSIILQDPILFSG-SIRFNLD---PECKCTDDRLW--EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFC 1458
Cdd:cd03297 74 -QRKIGLVFQQYALFPHlNVRENLAfglKRKRNREDRISvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1459 LARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYD 1528
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQLLPELkqIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1312-1535 |
5.86e-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: 57.12 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD---GKIV----------------- 1371
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1372 ----------------IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFnLDPECKCTDDRLWEALE----IAQLKNMV 1431
Cdd:TIGR03269 78 vgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTV-LDNVLEALEEIGYEGKEavgrAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1432 KslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHT 1509
Cdd:TIGR03269 157 Q-----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|....*..
gi 110832837 1510 IL-TADLVIVMKRGNILEYDTPESLLA 1535
Cdd:TIGR03269 232 IEdLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
683-843 |
6.16e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.58 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI---LGEMQTLEGKVHWSNVNESEpsfeaTRSRNRYSVAYAAQK- 758
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKE-----FAEKYPGEIIYVSEEd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 759 ---PWLlnaTVEENITFgspfnkqrykavtdACSLQpdidllpfGDQTEigeRGInlSGGQRQRICVARALYQNTNIVFL 835
Cdd:cd03233 93 vhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEALVSRASVLCW 142
|
....*...
gi 110832837 836 DDPFSALD 843
Cdd:cd03233 143 DNSTRGLD 150
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1328-1531 |
6.51e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1328 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLplHTLRSRLSIILQDPILF---- 1399
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIIAGLEhqtsGHIRFHGTDVSRL--HARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1400 -SGSIRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 1471
Cdd:PRK10851 91 vFDNIAFGLTvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1472 MDEATASIDMATENILQKVVMTAFADR--TVVTIAH-RVHTILTADLVIVMKRGNILEYDTPE 1531
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
688-899 |
7.25e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 54.86 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVN-ESEPSFEatrsRNRYSVAYAAQKPWLL-NAT 765
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDiTKLPMHK----RARLGIGYLPQEASIFrKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENI-----TFGSPFNKQRYKAVtdacSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFS 840
Cdd:cd03218 92 VEENIlavleIRGLSKKEREEKLE----ELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 841 ALD-IHLSDhlMQEgILKFLQdDKRTLVLVT----HKLQYLTHADWIIamKDGSVLREGTLKDI 899
Cdd:cd03218 163 GVDpIAVQD--IQK-IIKILK-DRGIGVLITdhnvRETLSITDRAYII--YEGKVLAEGTPEEI 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1319-1519 |
7.70e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1319 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 1398
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1399 FSGSIRFNLD-PeckctddrlWEALEIA-QLKNMVKSLP--GGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDE 1474
Cdd:PRK10247 93 FGDTVYDNLIfP---------WQIRNQQpDPAIFLDDLErfALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110832837 1475 ATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILTADLVIVM 1519
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1312-1537 |
8.13e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRL 1389
Cdd:CHL00131 8 LEIKNLHASVNEN--EILKGLNLSINKGEIHAIMGPNGSGKSTLSkvIAGHPAYKILEGDILFKGESILDLE-PEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1390 SIIL--QDPILFSGS-----IRFNLDPECKCTDDRLWEALE----IAQLKNMVKSLPGGLDAVVTEGgenFSVGQRQLFC 1458
Cdd:CHL00131 85 GIFLafQYPIEIPGVsnadfLRLAYNSKRKFQGLPELDPLEfleiINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1459 LARAFVRKSSILIMDEATASIDM-ATENILQKVVMTAFADRTVVTIAH--RVHTILTADLVIVMKRGNILEydTPESLLA 1535
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIdALKIIAEGINKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK--TGDAELA 239
|
..
gi 110832837 1536 QE 1537
Cdd:CHL00131 240 KE 241
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
683-872 |
8.74e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.07 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMqtlegkvhWsnvnesePSFEATRSRNRY-SVAYAAQKPWL 761
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLF-RILGEL--------W-------PVYGGRLTKPAKgKLFYVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 LNATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLpfgDQTEIGERGIN----------LSGGQRQRICVARALYQNTN 831
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDK-DLEQILDNV---QLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110832837 832 IVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHK 872
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYR-----LCREFGITLFSVSHR 638
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1068-1282 |
9.22e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 55.64 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1068 LHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGM---ISYA-TPVFLVALLPLG 1143
Cdd:cd18557 75 LFSSLLRQ----EIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIIlfiLSWKlTLVLLLVIPLLL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1144 VAFYFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAF----RHETRFKQRMLELTDTNN---IAYLFLSAA 1215
Cdd:cd18557 151 IASKIYGRYIRKLSKEVQDaLAKAGQ-----VAEESLSNIRTVRSFsaeeKEIRRYSEALDRSYRLARkkaLANALFQGI 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1216 NRWLEvrtdYLGACIVLtasiasisgSSNSGLVGLG----------LLYALTITNYLNWVVRNLADLEVQMGAVKKV 1282
Cdd:cd18557 226 TSLLI----YLSLLLVL---------WYGGYLVLSGqltvgeltsfILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
688-895 |
9.44e-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: 54.93 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL---------------GEMQTLEGKVHWS---NVNESEP-----SFEAT 744
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLEHIDkviVIDQSPIgrtprSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 745 RSR---------------NRY-----SVAYAAQK-PWLLNATVEENITFGSPFNKQRYKAVTdacsLQpDIDLlpfgDQT 803
Cdd:cd03271 91 YTGvfdeirelfcevckgKRYnretlEVRYKGKSiADVLDMTVEEALEFFENIPKIARKLQT----LC-DVGL----GYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 804 EIGERGINLSGGQRQRICVARALYQNTN---IVFLDDPFSALdiHLSD--HLMQegILKFLQDDKRTLVLVTHKLQYLTH 878
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL--HFHDvkKLLE--VLQRLVDKGNTVVVIEHNLDVIKC 237
|
250 260
....*....|....*....|...
gi 110832837 879 ADWIIAM------KDGSVLREGT 895
Cdd:cd03271 238 ADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
367-605 |
1.29e-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: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 367 TFLQASYYVTIETGI--NLRGALlamiYNKILRLSTSNLSmgEMTLGQINNLVAIETNQLMWFLF-LCPNLWAMPVQIIM 443
Cdd:cd07346 56 SYLRRYLAARLGQRVvfDLRRDL----FRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 444 GVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWE----HIFCKSVE 519
Cdd:cd07346 130 ALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 520 ETRMKELSSLKTFALYTSLSIFMNAAIPIAAVL--ATFVthayaSGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVK 597
Cdd:cd07346 210 DLRDANLRAARLSALFSPLIGLLTALGTALVLLygGYLV-----LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQ 284
|
....*...
gi 110832837 598 AIISVQKL 605
Cdd:cd07346 285 ALASLERI 292
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
672-895 |
1.38e-07 |
|
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: 53.91 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 672 IKVTNGYFSWGSGLAtLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRys 751
Cdd:cd03265 1 IEVENLVKKYGDFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT---VAGHDVVREPREVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 752 VAYAAQKPWLLNA-TVEENI-TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDqteigERGINLSGGQRQRICVARALYQN 829
Cdd:cd03265 75 IGIVFQDLSVDDElTGWENLyIHARLYGVPGAERRERIDELLDFVGLLEAAD-----RLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 830 TNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHklqYLTHA----DWIIAMKDGSVLREGT 895
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVW-EYIEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGT 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
688-874 |
1.51e-07 |
|
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: 54.26 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNVNESEPSFEATRSRNRYSVAYAaQKPWL------ 761
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV---RVAGLVPWKRRKKFLRRIGVVFG-QKTQLwwdlpv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 -----LNATVeenitFGSPfnKQRYKAVTDACSlqpdiDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLD 836
Cdd:cd03267 113 idsfyLLAAI-----YDLP--PARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110832837 837 DPFSALDIHlsdhlMQEGILKFLQDDKR----TLVLVTHKLQ 874
Cdd:cd03267 179 EPTIGLDVV-----AQENIRNFLKEYNRergtTVLLTSHYMK 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1314-1505 |
1.70e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.84 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1314 IHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVID-GIDISKLPlhtlrsr 1388
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILagelEPDSGEVSIPkGLRIGYLP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1389 lsiilQDPILFSG-SIRFNL----------------------DPECKCTD-DRLWEALEIA---QLKNMVKSLPGGL--- 1438
Cdd:COG0488 68 -----QEPPLDDDlTVLDTVldgdaelraleaeleeleaklaEPDEDLERlAELQEEFEALggwEAEARAEEILSGLgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1439 ----DAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT----ENILQK----VVMT----AFADRTVVT 1502
Cdd:COG0488 143 eedlDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNypgtVLVVshdrYFLDRVATR 218
|
...
gi 110832837 1503 IAH 1505
Cdd:COG0488 219 ILE 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
684-888 |
2.00e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnvnesepSFEATRSRN------RYSVAYAAQ 757
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS-------GHDITRLKNrevpflRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 758 KPWLL-NATVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQN 829
Cdd:PRK10908 87 DHHLLmDRTVYDNVAIpliiaGASGDdiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 830 TNIVFLDDPFSALDIHLSdhlmqEGILKFLQDDKR---TLVLVTHKLQYLTHADW-IIAMKDG 888
Cdd:PRK10908 156 PAVLLADEPTGNLDDALS-----EGILRLFEEFNRvgvTVLMATHDIGLISRRSYrMLTLSDG 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1314-1533 |
2.33e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1314 IHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI-------------VIDGIDIS 1378
Cdd:PRK10261 15 VENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1379 KLPLHTLR-SRLSIILQDPIL-----------FSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvt 1443
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEPMTslnpvftvgeqIAESIRLHQGasrEEAMVEAKRMLDQVRIPEAQTILSRYPHQL----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1444 eggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMTAFADRTVVTIAHRVHTIL-TADLVIVMK 1520
Cdd:PRK10261 170 ------SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaQILQLIkVLQKEMSMGVIFITHDMGVVAeIADRVLVMY 243
|
250
....*....|...
gi 110832837 1521 RGNILEYDTPESL 1533
Cdd:PRK10261 244 QGEAVETGSVEQI 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1329-1512 |
2.43e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1329 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSRLSIILQD---------- 1395
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDhhllmdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1396 -----PILFSGSirfnldpeckCTDD---RLWEALEIAQLKNMVKSLPggldaVVTEGGENFSVGqrqlfcLARAFVRKS 1467
Cdd:PRK10908 98 dnvaiPLIIAGA----------SGDDirrRVSAALDKVGLLDKAKNFP-----IQLSGGEQQRVG------IARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110832837 1468 SILIMDEATASIDMA-TENILQ------KVVMTAF-ADRTVVTIAHRVHTILT 1512
Cdd:PRK10908 157 AVLLADEPTGNLDDAlSEGILRlfeefnRVGVTVLmATHDIGLISRRSYRMLT 209
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1034-1282 |
2.73e-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: 54.09 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1034 YYVAGFSILCG------AGIFLcLVTSLTVEWMGLTaaknLHHNLLNKiilgPIRFFDTTPLGLILNRFSADTNIIDQHI 1107
Cdd:cd18572 40 LLLLLLSVLSGlfsglrGGCFS-YAGTRLVRRLRRD----LFRSLLRQ----DIAFFDATKTGELTSRLTSDCQKVSDPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1108 PPTLESLTRSTLLCLSAIGMISYATP----VFLVALLPLGVAFYFIQKYFRVASKDLQElddstqlpLLCHFSETAE--- 1180
Cdd:cd18572 111 STNLNVFLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQD--------ALAEANQVAEeal 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1181 -GLTTIRAFRHET----RFKQRMLELTDTN---NIAYLFLSAANRWLevrtDYLGACIVLtasiasisgssnsgLVGLGL 1252
Cdd:cd18572 183 sNIRTVRSFATEErearRYERALDKALKLSvrqALAYAGYVAVNTLL----QNGTQVLVL--------------FYGGHL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 110832837 1253 ---------------LYALTITNYLNWVVRNLADLEVQMGAVKKV 1282
Cdd:cd18572 245 vlsgrmsagqlvtfmLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1312-1396 |
2.97e-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: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRY--ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKLPLHTL 1385
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSEREL 86
|
90
....*....|....*
gi 110832837 1386 R----SRLSIILQDP 1396
Cdd:COG4172 87 RrirgNRIAMIFQEP 101
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
688-899 |
5.22e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.65 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTlEGKVHWSNVNESEPSFEATRsRNRYSVAYAAQKPWLLNA-T 765
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCInLLERPT-SGRVLVDGQDLTALSEKELR-KARRQIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITF-----GSPfNKQRYKAVTDacslqpdidLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:PRK11153 99 VFDNVALplelaGTP-KAEIKARVTE---------LLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 840 SALDIHLSDhlmqeGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK11153 169 SALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1328-1535 |
5.54e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.44 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1328 VLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVD---IFDGKIVIDG---IDISKLPLHTLRSRLSIILQDpilf 1399
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEagtIRVGDITIDTarsLSQQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1400 sgsirFNLDPEckctddrlWEALE-IAQLKNMVKSLPGG---------LDAVVTEGGEN-----FSVGQRQLFCLARAFV 1464
Cdd:PRK11264 94 -----FNLFPH--------RTVLEnIIEGPVIVKGEPKEeatararelLAKVGLAGKETsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1465 RKSSILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNILEYDTPESLLA 1535
Cdd:PRK11264 161 MRPEVILFDEPTSALDpeLVGE-VLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
812-873 |
5.73e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.20 E-value: 5.73e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 812 LSGGQRQRICVARALYQNTNIVFLDDPFSALDihLSdhlMQEGILKFLQDDKR----TLVLVTHKL 873
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD--VS---IQAQVLNLLEDLQDelglTYLFISHDL 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
688-894 |
6.23e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--VNESEPSFEATRSRnrysVAYAAQKP--WLLN 763
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQ----VATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 ATVEENITFgspfnKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSAL 842
Cdd:PRK13638 93 TDIDSDIAF-----SLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 110832837 843 DIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREG 894
Cdd:PRK13638 168 DPAGRTQMI--AIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
690-899 |
6.39e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.21 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNVNESEPSFEATRSRNRYS-----VAYAAQKPWL-LN 763
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMAEKLEFNGQDLQRISEKERRNlvgaeVAMIFQDPMTsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 764 A--TVEENIT-------FGSpfNKQRYKAVTDACSLQ--PD----IDLLPFgdqteigergiNLSGGQRQRICVARALYQ 828
Cdd:PRK11022 104 PcyTVGFQIMeaikvhqGGN--KKTRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 829 NTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQII-ELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
694-882 |
6.67e-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: 52.37 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 694 RIPT---GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV----HWSNV------NESEPSFEATRS---RNRYSVAYAAQ 757
Cdd:cd03236 19 RLPVpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDEIldefrgSELQNYFTKLLEgdvKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 758 KPWLLNATVEENITFGSPFNKQRYkaVTDACSLQPdidllpfgdqteIGERGI-NLSGGQRQRICVARALYQNTNIVFLD 836
Cdd:cd03236 99 IPKAVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 110832837 837 DPFSALDIHlsDHLMQEGILKFLQDDKRTLVLVTHKLQYLTH-ADWI 882
Cdd:cd03236 165 EPSSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1326-1535 |
6.74e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.79 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1326 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI-SKLPLHTLRSRLSIILQDPILF 1399
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1400 SGSIRFNLDPECKCtdDRLWEALEIAQLKNMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 1476
Cdd:PRK14271 114 PMSIMDNVLAGVRA--HKLVPRKEFRGVAQARLTEVGLWDAVkdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 1477 ASIDMATENILQKVVMTaFADR-TVVTIAHRV-HTILTADLVIVMKRGNILEYDTPESLLA 1535
Cdd:PRK14271 192 SALDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
690-871 |
7.12e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 690 NIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNVNESEPSfEATRSRNRYSVAyaaqkPWLLNA----T 765
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI--SLCGEPVPS-RARHARQRVGVV-----PQFDNLdpdfT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENI-TFGspfnkqRYKAVTDACSLQPDIDLLPFGD-----QTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:PRK13537 97 VRENLlVFG------RYFGLSAAAARALVPPLLEFAKlenkaDAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190
....*....|....*....|....*....|..
gi 110832837 840 SALDIHlSDHLMQEGiLKFLQDDKRTLVLVTH 871
Cdd:PRK13537 167 TGLDPQ-ARHLMWER-LRSLLARGKTILLTTH 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
697-871 |
9.24e-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: 50.06 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 697 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnVNESEPSFEATRSRNRysvayaaqkpwllnatveenitfgspf 776
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---YIDGEDILEEVLDQLL--------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 777 nkqrykavtdacslqpdidllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEG-- 854
Cdd:smart00382 51 -------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEel 105
|
170
....*....|....*....
gi 110832837 855 --ILKFLQDDKRTLVLVTH 871
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTN 124
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1312-1527 |
1.36e-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: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV-DIF---DGKIVIDGIDISKLPLHT--- 1384
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTT----IRMIlGIIlpdSGEVLFDGKPLDIAARNRigy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1385 ------LRSRLSIilQDPILFSGSIRfNLDP-ECKCTDDRLWEALEIAQLKNmvKSLpggldavvteggENFSVGQRQLF 1457
Cdd:cd03269 75 lpeergLYPKMKV--IDQLVYLAQLK-GLKKeEARRRIDEWLERLELSEYAN--KRV------------EELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI-LTADLVIVMKRGNILEY 1527
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLY 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
813-894 |
1.77e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 813 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKR-TLVLVTHKLQY---LTHAdwIIAMKDG 888
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQKHQlAYLFISHDLHVvraLCHQ--VIVLRQG 502
|
....*.
gi 110832837 889 SVLREG 894
Cdd:PRK15134 503 EVVEQG 508
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1326-1545 |
1.94e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.87 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1326 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLP-----LHTlrsrlsiILQDPIL 1398
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVlrLIAGFETPD--SGRIMLDGQDITHVPaenrhVNT-------VFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1399 FSG-SIRFNLDPECKC-------TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSIL 1470
Cdd:PRK09452 98 FPHmTVFENVAFGLRMqktpaaeITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1471 IMDEATASID------MATE-NILQKVVMTAFadrtvVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQENGVF- 1541
Cdd:PRK09452 167 LLDESLSALDyklrkqMQNElKALQRKLGITF-----VFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKNLFv 241
|
....
gi 110832837 1542 ASFV 1545
Cdd:PRK09452 242 ARFI 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1338-1536 |
2.09e-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: 51.64 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1338 PGQKV-GICGRTGSGKSSLslafFRMV------DifDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SI 1403
Cdd:COG4148 23 PGRGVtALFGPSGSGKTTL----LRAIaglerpD--SGRIRLGGevlQDSARgifLPPH--RRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1404 RFNLD--------PECKCTDDRLWEALEIAQLknmVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 1475
Cdd:COG4148 95 RGNLLygrkraprAERRISFDEVVELLGIGHL---LDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1476 TASIDMATEN----ILQKVvmtafADRT---VVTIAHRVHTILT-ADLVIVMKRGNILEYDTPESLLAQ 1536
Cdd:COG4148 161 LAALDLARKAeilpYLERL-----RDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1319-1528 |
2.10e-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: 50.79 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1319 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIVIDGIDISKLPL------HTLRSRLSII 1392
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTT-------LKILSGLLQPTSGEVRVAGLvpwkrrKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1393 L------------QDPILFSGSIrFNLDP-ECKCTDDRLWEALEIAQLknmvkslpggLDAVVteggENFSVGQRQLFCL 1459
Cdd:cd03267 100 FgqktqlwwdlpvIDSFYLLAAI-YDLPPaRFKKRLDELSELLDLEEL----------LDTPV----RQLSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1460 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILT-ADLVIVMKRGNILeYD 1528
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLL-YD 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
811-894 |
2.57e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 811 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ-YLTHADWIiamkdgS 889
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKLReVMAIADRV------T 212
|
....*
gi 110832837 890 VLREG 894
Cdd:COG3845 213 VLRRG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
688-948 |
2.62e-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: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ----TLEGKVHWSNVNESEpsfeaTRSRNRYSVAYAAQK----P 759
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEE-----IKKHYRGDVVYNAETdvhfP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 760 WLlnaTVEENITFG----SPFNkqRYKAVT--DACSLQPDIDLLPFG----DQTEIGE---RGInlSGGQRQRICVARAL 826
Cdd:TIGR00956 152 HL---TVGETLDFAarckTPQN--RPDGVSreEYAKHIADVYMATYGlshtRNTKVGNdfvRGV--SGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 827 YQNTNIVFLDDPFSALD--------------IHLSDHLMQEGILKFLQD-----DKRTLV---------LVTHKLQYL-- 876
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDsatalefiralktsANILDTTPLVAIYQCSQDayelfDKVIVLyegyqiyfgPADKAKQYFek 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 877 ---------THADWIIAMKDGS--VLREGTLKDIQTKDVELYEHWKTLMNRqdQELEKDMEA----DQTTLERKTLRRAM 941
Cdd:TIGR00956 305 mgfkcpdrqTTADFLTSLTSPAerQIKPGYEKKVPRTPQEFETYWRNSPEY--AQLMKEIDEyldrCSESDTKEAYRESH 382
|
....*..
gi 110832837 942 YSREAKA 948
Cdd:TIGR00956 383 VAKQSKR 389
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
812-885 |
3.57e-06 |
|
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: 49.95 E-value: 3.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 812 LSGGQRQRICVARALYQN-TNIVF-LDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAM 885
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGlTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
685-899 |
4.57e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 685 LATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN----------VNESEPSFEATRSRNRYSVAY 754
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 755 AAQKPWL-LNA--TVEENITFGSPFNK--QRYKAVTDACSLqpdIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQ 828
Cdd:PRK10261 109 IFQEPMTsLNPvfTVGEQIAESIRLHQgaSREEAMVEAKRM---LDQVRIPEAQTILSRYPHqLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 829 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRT-LVLVTHKLQYLTH-ADWIIAMKDGSVLREGTLKDI 899
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMSMgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
812-899 |
5.80e-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: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 812 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRT----LVLVTHKLQYLTH-ADWIIAMK 886
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLGVVRRfADRVAVMR 231
|
90
....*....|...
gi 110832837 887 DGSVLREGTLKDI 899
Cdd:COG4172 232 QGEIVEQGPTAEL 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1336-1491 |
6.53e-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: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1336 IKPGQKVGICGRTGSGKSSLS--LAFFRMVDIFDGKIVIDGIDISKLPLH-TLRSRLSIILQDPILFSG-SIRFN--LDP 1409
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVPElSVAENifLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1410 ECKCTDDRLWEALEIAQLKNMVKSLPggLDAV-VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ 1488
Cdd:TIGR02633 104 EITLPGGRMAYNAMYLRAKNLLRELQ--LDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILL 181
|
...
gi 110832837 1489 KVV 1491
Cdd:TIGR02633 182 DII 184
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
684-888 |
6.60e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVnesEPSFEATRSRNRYSVAYAAQKPWL-L 762
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFKSSKEALENGISMVHQELNLvL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 NATVEENITFG-----SPF--NKQRYKAvTDACSLQPDIDLLPfgdqteiGERGINLSGGQRQRICVARALYQNTNIVFL 835
Cdd:PRK10982 87 QRSVMDNMWLGryptkGMFvdQDKMYRD-TKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110832837 836 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTH-ADWIIAMKDG 888
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1322-1530 |
6.90e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1322 ENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIV---IDG-IDISKLP-LHTLRSRLS------ 1390
Cdd:PLN03140 890 EDRLQ-LLREVTGAFRPGVLTALMGVSGAGKTTL-------MDVLAGRKTggyIEGdIRISGFPkKQETFARISgyceqn 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1391 ------IILQDPILFSGSIRfnLDPECKCTD-----DRLWEALEIAQLKNMVKSLPGgldavVTeggeNFSVGQRQLFCL 1459
Cdd:PLN03140 962 dihspqVTVRESLIYSAFLR--LPKEVSKEEkmmfvDEVMELVELDNLKDAIVGLPG-----VT----GLSTEQRKRLTI 1030
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 1460 ARAFVRKSSILIMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVHT-ILTA-DLVIVMKRGNILEYDTP 1530
Cdd:PLN03140 1031 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSIdIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
684-911 |
9.03e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.74 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNVNESEPSFEATRSRNRYSVAYAAQKPWL-- 761
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI---IIDDEDISLLPLHARARRGIGYLPQEASIfr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 -------LNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLpfgdqteigerGINLSGGQRQRICVARALYQNTNIVF 834
Cdd:PRK10895 92 rlsvydnLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 835 LDDPFSALD-IHLSDhlmQEGILKFLQDDKRTLVLVTHKL-QYLTHADWIIAMKDGSVLREGT----LKDIQTKDVELYE 908
Cdd:PRK10895 161 LDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTpteiLQDEHVKRVYLGE 237
|
...
gi 110832837 909 HWK 911
Cdd:PRK10895 238 DFR 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
647-844 |
9.11e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 647 PGRYHLDSYEQSTRRLRPAETEDIA-----IKVTN--GYFSWGSGL--------ATLSNIDIRIPTGQLTMIVGQVGCGK 711
Cdd:PRK10261 284 PRRFPLISLEHPAKQEPPIEQDTVVdgepiLQVRNlvTRFPLRSGLlnrvtrevHAVEKVSFDLWPGETLSLVGESGSGK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 712 SSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRySVAYAAQKPWllnATVEENITFG-SPFNKQRYKAVTDACSL 790
Cdd:PRK10261 364 STTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDPY---ASLDPRQTVGdSIMEPLRVHGLLPGKAA 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 791 QPDIDLL--PFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDI 844
Cdd:PRK10261 440 AARVAWLleRVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1011-1222 |
9.25e-06 |
|
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: 49.40 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1011 IDYWLATwtseysiNNTGKADQTyyvagFSILCGAGIFLCLVTSL---TVEWMGLTAAKNLHHNLLNKIILGPIRFFDTT 1087
Cdd:cd18575 23 IDQGFAA-------GNTALLNRA-----FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1088 PLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VFLVALLPLGVA-FYFIQKYFRVASKDLQE- 1162
Cdd:cd18575 91 RTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQDr 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1163 LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTDTNniaylfLSAANRWLEVR 1222
Cdd:cd18575 171 LADLSA-----FAEETLSAIKTVQAFTREDAERQRFATAVEAA------FAAALRRIRAR 219
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
800-947 |
1.38e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 800 GDQ-TEIGERginLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQ-----EGILKFLQDDKRTLVLVTHKL 873
Cdd:PRK10636 421 GDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEalidfEGALVVVSHDRHLLRSTTDDL 497
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 874 qYLTHadwiiamkDGSVlregtlkDIQTKDVELYEHWktLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAK 947
Cdd:PRK10636 498 -YLVH--------DGKV-------EPFDGDLEDYQQW--LSDVQKQENQTDEAPKENNANSAQARKDQKRREAE 553
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
765-899 |
1.51e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.10 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENI-----TFGSPFNKQRYKAVtdacSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPF 839
Cdd:COG1137 94 TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 840 SALD-IHLSDhlMQEgILKFLQDdkRTL-VLVT-HK----LQ-----YLthadwiiaMKDGSVLREGTLKDI 899
Cdd:COG1137 165 AGVDpIAVAD--IQK-IIRHLKE--RGIgVLITdHNvretLGicdraYI--------ISEGKVLAEGTPEEI 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
688-898 |
2.10e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.11 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVHWSNVNESEPSFEATRSRNRYSVAYaaqkPWLlnaT 765
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKQILKRTGFVTQDDILY----PHL---T 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 766 VEENITFGS----PFNKQRYKAVTDACSLQPDIDLLPFGDqTEIGE---RGInlSGGQRQRICVARALYQNTNIVFLDDP 838
Cdd:PLN03211 157 VRETLVFCSllrlPKSLTKQEKILVAESVISELGLTKCEN-TIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 839 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHA--DWIIAMKDGSVLREGTLKD 898
Cdd:PLN03211 234 TSGLDATAAYRLVL--TLGSLAQKGKTIVTSMHQPSSRVYQmfDSVLVLSEGRCLFFGKGSD 293
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
807-899 |
2.61e-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: 48.86 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 807 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPfsALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWII 883
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEP--SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|..
gi 110832837 884 AM------KDGSVLREGTLKDI 899
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEI 582
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
810-883 |
2.81e-05 |
|
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: 46.41 E-value: 2.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 810 INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQeGILKFLQDDKRTLVLVTHKLQYLTH-ADWII 883
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR-AIRRLSEEGKKTALVVEHDLAVLDYlSDRIH 143
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1310-1525 |
2.85e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1310 GEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKIVIDGIDISKlplHTLRs 1387
Cdd:PLN03211 67 HKPKISDETRQIQE--RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1388 RLSIILQDPILFSG-SIRFNLdpeCKCTDDRLWEALEiAQLKNMVKslpgglDAVVTEGG----EN----------FSVG 1452
Cdd:PLN03211 141 RTGFVTQDDILYPHlTVRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGG 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 1453 QRQLFCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILtaDLVIVMKRGNIL 1525
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCL 286
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1336-1531 |
2.86e-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: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1336 IKPGQKVGICGRTGSGKSSLslafFRMV------DifDGKIVIDGIDISKLPLHtLRSRLSII--LQDPILFSG------ 1401
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTL----FNLItgfyrpT--SGRILFDGRDITGLPPH-RIARLGIArtFQNPRLFPEltvlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1402 --------------SIRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFV 1464
Cdd:COG0411 100 vlvaaharlgrgllAALLRLPRarrEEREARERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1465 RKSSILIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILT-ADLVIVMKRGNILEYDTPE 1531
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEeTEELAELIRrLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1288-1506 |
3.67e-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: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1288 MESENYEGTMDP--------SQVPEHWPQEGEIKIHDLCVRYEN------NLKPVLKHVKAYIKPGQKVGICGRTGSGKS 1353
Cdd:TIGR00954 413 VKSGNFKRPRVEeiesgregGRNSNLVPGRGIVEYQDNGIKFENiplvtpNGDVLIESLSFEVPSGNNLLICGPNGCGKS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1354 SLslafFRMVD----IFDGKIVIDG----IDISKLPLHTLRSrlsiiLQDPILFSGSIrfnLDPECK-CTDDRLWEALEI 1424
Cdd:TIGR00954 493 SL----FRILGelwpVYGGRLTKPAkgklFYVPQRPYMTLGT-----LRDQIIYPDSS---EDMKRRgLSDKDLEQILDN 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1425 AQLKNMVKSlPGGLDAVvTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA--SIDM--ATENILQKVVMTAFadrtv 1500
Cdd:TIGR00954 561 VQLTHILER-EGGWSAV-QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSavSVDVegYMYRLCREFGITLF----- 633
|
....*.
gi 110832837 1501 vTIAHR 1506
Cdd:TIGR00954 634 -SVSHR 638
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
698-904 |
3.84e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.85 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 698 GQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNVNESEPSfEATRSRNRysvAYAAQK-PWLLNATVEENITFGSPF 776
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWS-AAELARHR---AYLSQQqTPPFAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 777 NKQRY---KAVTDACSLQPDIDLLPfgdqteigeRGIN-LSGGQRQRICVARALYQ-------NTNIVFLDDPFSALDI- 844
Cdd:PRK03695 97 KTRTEavaSALNEVAEALGLDDKLG---------RSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVa 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 845 ------HLSDHLMQEGIlkflqddkrTLVLVTHKLQY-LTHADWIIAMKDGSVLREGTLKDIQTKDV 904
Cdd:PRK03695 168 qqaaldRLLSELCQQGI---------AVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
688-871 |
4.13e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.12 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNVNESEPsfeATRSRNRYSVAYAAQKPWLLNA-TV 766
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLM-NALAFRSPKGVKGSGSVLLNGMP---IDAKEMRAISAYVQQDDLFIPTlTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFGSPF----------NKQRYKAVTDACSLQPDIDllpfgdqTEIGERGI--NLSGGQRQRICVARALYQNTNIVF 834
Cdd:TIGR00955 117 REHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCAN-------TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 110832837 835 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTH 871
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
703-882 |
4.26e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 703 IVGQVGCGKSSLLLAILGEMQTLEGkvhwsnvnesepsfEATRSRNrYSVAYAAQKPWL-LNATVEENIT--FGSPFNKQ 779
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG--------------EARPAPG-IKVGYLPQEPQLdPEKTVRENVEegVAEVKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 780 -RYKAVTDACS---------------LQPDIDL------------------LPFGDqTEIGergiNLSGGQRQRICVARA 825
Cdd:PRK11819 103 dRFNEIYAAYAepdadfdalaaeqgeLQEIIDAadawdldsqleiamdalrCPPWD-AKVT----KLSGGERRRVALCRL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 826 LYQNTNIVFLDDPfsaldihlSDHLMQEGIL---KFLQDDKRTLVLVTHKLQYLTH-ADWI 882
Cdd:PRK11819 178 LLEKPDMLLLDEP--------TNHLDAESVAwleQFLHDYPGTVVAVTHDRYFLDNvAGWI 230
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
990-1210 |
4.31e-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: 47.38 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 990 GFFLLILMIFSKLLKHSVI-VAIDywlatwtsEYSINNTGKADQTYYVAGFSILCGAGIFLCL-VTSLTVEWMGLTAAKN 1067
Cdd:cd18544 4 ALLLLLLATALELLGPLLIkRAID--------DYIVPGQGDLQGLLLLALLYLGLLLLSFLLQyLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1068 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISY----ATPVFLVALLPLG 1143
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLlnwrLALISLLVLPLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1144 VAFYFIQKYFRVASKDLQEL--DDSTQLpllchfSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYL 1210
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKlsRLNAFL------QESISGMSVIQLFNREKREFEEFDEINQEYRKANL 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1317-1482 |
4.48e-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: 46.20 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1317 LCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP 1396
Cdd:TIGR01189 7 ACSRGE---RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1397 ILFSGSIRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMD 1473
Cdd:TIGR01189 84 LKPELSALENLHfwaAIHGGAQRTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 110832837 1474 EATASIDMA 1482
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
683-873 |
6.30e-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: 48.09 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 683 SGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvNESEPSFEATRSrnrySVAYAAQKPWLL 762
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-KDIETNLDAVRQ----SLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 N-ATVEENITFGSPFNKQRYkavtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 841
Cdd:TIGR01257 1016 HhLTVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190
....*....|....*....|....*....|..
gi 110832837 842 LDIHlSDHLMQEGILKFlqDDKRTLVLVTHKL 873
Cdd:TIGR01257 1092 VDPY-SRRSIWDLLLKY--RSGRTIIMSTHHM 1120
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
813-894 |
7.05e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 813 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLqddkRTLV--------LVTHKL---QYLTHAdw 881
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLL----RGLVrelglavvIVTHDLavaRLLAHR-- 221
|
90
....*....|...
gi 110832837 882 IIAMKDGSVLREG 894
Cdd:PRK11701 222 LLVMKQGRVVESG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1336-1537 |
7.92e-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: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1336 IKPGQKVGICGRTGSGKSSLSLAFFRMVD-IFDGKIVIDG--IDIsKLPLHTLRSRLSIILQD-------PIL------- 1398
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDI-RNPAQAIRAGIAMVPEDrkrhgivPILgvgknit 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1399 ------FSGSIRFNLDPECKCTDdrlwEALEIAQLKNMVKSLP-GGLdavvteggenfSVGQRQLFCLARAFVRKSSILI 1471
Cdd:TIGR02633 362 lsvlksFCFKMRIDAAAELQIIG----SAIQRLKVKTASPFLPiGRL-----------SGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110832837 1472 MDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNiLEYDTPESLLAQE 1537
Cdd:TIGR02633 427 LDEPTRGVDVgAKYEIYKLINQLAQEGVAIIVVSSELAEVLgLSDRVLVIGEGK-LKGDFVNHALTQE 493
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1312-1528 |
8.06e-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: 45.60 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLKP--------------------VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 1371
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1372 IDGIDISKLPLHT-LRSRLSIIlqDPILFSGSIrFNLDPecKCTDDRLWEALEIAQLKNM----VKslpggldavvtegg 1446
Cdd:cd03220 81 VRGRVSSLLGLGGgFNPELTGR--ENIYLNGRL-LGLSR--KEIDEKIDEIIEFSELGDFidlpVK-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1447 eNFSVGQ--RQLFCLARAFvrKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-TADLVIVMKRG 1522
Cdd:cd03220 142 -TYSSGMkaRLAFAIATAL--EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKrLCDRALVLEKG 218
|
....*.
gi 110832837 1523 NILEYD 1528
Cdd:cd03220 219 KIRFDG 224
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1059-1201 |
8.51e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 46.32 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1059 WMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATP---VF 1135
Cdd:cd18576 62 RVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLL 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1136 LVALLP-LGVAFYFIQKYFRVASKDLQ-ELDDSTQlpllcHFSETAEGLTTIRAFRHE----TRFKQRMLEL 1201
Cdd:cd18576 142 MLATVPvVVLVAVLFGRRIRKLSKKVQdELAEANT-----IVEETLQGIRVVKAFTREdyeiERYRKALERV 208
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
688-895 |
1.03e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAIL---------------GEMQTLEGKVHWS---NVNESEP-----SFEAT 744
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanrlngaktvpGRYTSIEGLEHLDkviHIDQSPIgrtprSNPAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 745 ------------------RSR----NRYSV-----AYAA---------QKPWLLNATVEENITFGSPFNKQ----RYKAV 784
Cdd:TIGR00630 704 ytgvfdeirelfaetpeaKVRgytpGRFSFnvkggRCEAcqgdgvikiEMHFLPDVYVPCEVCKGKRYNREtlevKYKGK 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 785 TDACSLQ-------------PDID-----LLPFGDQ-TEIGERGINLSGGQRQRICVARALYQNTN---IVFLDDPFSAL 842
Cdd:TIGR00630 784 NIADVLDmtveeayeffeavPSISrklqtLCDVGLGyIRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL 863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110832837 843 diHLSD--HLMQegILKFLQDDKRTLVLVTHKLQYLTHADWII------AMKDGSVLREGT 895
Cdd:TIGR00630 864 --HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTVVASGT 920
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1338-1517 |
1.06e-04 |
|
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: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1338 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIdgIDISKLPLHTLRSRLSIILQDPILFSGSIRfnldpeckctddr 1417
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGEL------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1418 lwealeiaqlknmvkslpggldavvteggenfsvGQRQLFclARAFVRKSSILIMDEATASIDMATENILQKVVMTAF-- 1495
Cdd:smart00382 66 ----------------------------------RLRLAL--ALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180
....*....|....*....|....*..
gi 110832837 1496 -----ADRTVVTIAHRVHTILTADLVI 1517
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRR 136
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1312-1528 |
1.08e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.60 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRM----VDIFDGKIVI-DGIDISKLPlhtlr 1386
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLlageLEPDSGTVKLgETVKIGYFD----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1387 srlsiilQDpilfsgsiRFNLDPeckctDDRLWEAL-------EIAQLKNMVKSL--PGglDAVVTEGGeNFSVGQRQLF 1457
Cdd:COG0488 385 -------QH--------QEELDP-----DKTVLDELrdgapggTEQEVRGYLGRFlfSG--DDAFKPVG-VLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1458 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTaFaDRTVVTIAH------RVhtiltADLVIVMKRGNILEYD 1528
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-F-PGTVLLVSHdryfldRV-----ATRILEFEDGGVREYP 511
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1336-1526 |
1.13e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.27 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1336 IKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIV-----IDGIDISKLPLHTLR----SRLSIILQDPILfsgsirfN 1406
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISEKERRnlvgAEVAMIFQDPMT-------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1407 LDPeCKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEG-----------GENFSVGQRQLFCLARAFVRKSSILIMDEA 1475
Cdd:PRK11022 102 LNP-CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGipdpasrldvyPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1476 TASIDMATE--------NILQKVVMtafadrTVVTIAHRVHTIL-TADLVIVMKRGNILE 1526
Cdd:PRK11022 181 TTALDVTIQaqiielllELQQKENM------ALVLITHDLALVAeAAHKIIVMYAGQVVE 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
688-894 |
1.28e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsNVNESEPSFEATRSRNRYSVAYAAQKPWLLNAT-V 766
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-DVPDNQFGREASLIDAIGRKGDFKDAVELLNAVgL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 767 EENITFGSPFNkqrykavtdacslqpdidllpfgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 846
Cdd:COG2401 125 SDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 110832837 847 SdHLMQEGILKFLQDDKRTLVLVTHklqyltHADWIIAMKDGSVLREG 894
Cdd:COG2401 172 A-KRVARNLQKLARRAGITLVVATH------HYDVIDDLQPDLLIFVG 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1326-1480 |
1.31e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 45.98 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1326 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSIILQdpilFSgsirf 1405
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FD----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1406 NLDPECKCTDD------------RLWEA-----LEIAQLKNMVkslpgglDAVVTEggenFSVGQRQLFCLARAFVRKSS 1468
Cdd:PRK13536 124 NLDLEFTVRENllvfgryfgmstREIEAvipslLEFARLESKA-------DARVSD----LSGGMKRRLTLARALINDPQ 192
|
170
....*....|..
gi 110832837 1469 ILIMDEATASID 1480
Cdd:PRK13536 193 LLILDEPTTGLD 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
812-888 |
1.59e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 812 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMK 886
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 110832837 887 DG 888
Cdd:PRK15134 232 NG 233
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1060-1203 |
1.60e-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: 45.50 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1060 MGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADT----NIIDQHIPptlESLTRSTLLCLSAIGMISYATPVF 1135
Cdd:cd18551 63 TGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELITSGLP---QLVTGVLTVVGAVVLMFLLDWVLT 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110832837 1136 LVALLPLGVAF---YFIQKYFRVASKDLQE-LDDSTQlpllcHFSETAEGLTTIRAFRHETRFKQRMLELTD 1203
Cdd:cd18551 140 LVTLAVVPLAFliiLPLGRRIRKASKRAQDaLGELSA-----ALERALSAIRTVKASNAEERETKRGGEAAE 206
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1068-1197 |
1.74e-04 |
|
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: 45.32 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1068 LHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG---MISYA-TPVFLVALLPLG 1143
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVfmfTTSWKlTLVMLSVVPPLS 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1144 VAFYFIQKYFRVASKDLQ-ELDDStqlpllchfSETAE----GLTTIRAFRHETRFKQR 1197
Cdd:cd18780 157 IGAVIYGKYVRKLSKKFQdALAAA---------STVAEesisNIRTVRSFAKETKEVSR 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1438-1522 |
2.24e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1438 LDAVVteggENFSVGQRQLFCLARAFVRKSSILIMDEATASI-DMATENILQkvVMTAFAD--RTVVTIAHRVHTILT-A 1513
Cdd:COG3845 135 PDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE--ILRRLAAegKSIIFITHKLREVMAiA 208
|
....*....
gi 110832837 1514 DLVIVMKRG 1522
Cdd:COG3845 209 DRVTVLRRG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1317-1530 |
5.71e-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: 45.00 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1317 LCVR-----YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSI 1391
Cdd:TIGR01257 929 VCVKnlvkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQDPILF-----SGSIRFNLDpeckcTDDRLWEALEIaQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRK 1466
Cdd:TIGR01257 1008 CPQHNILFhhltvAEHILFYAQ-----LKGRSWEEAQL-EMEAMLEDT--GLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110832837 1467 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRV-HTILTADLVIVMKRGNILEYDTP 1530
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PduV-EutP |
pfam10662 |
Ethanolamine utilization - propanediol utilization; Members of this family function in ... |
701-817 |
7.09e-04 |
|
Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.
Pssm-ID: 402341 [Multi-domain] Cd Length: 137 Bit Score: 41.50 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 701 TMIVGQVGCGKSSLLLAILGE------MQTLEgkvhWSNVNESEPSfEATRSRNRYSV----AYAAQKPWLL-NATVEEN 769
Cdd:pfam10662 4 IMLIGPTGCGKTTLCQALSGEelkykkTQAIE----FYDNAIDTPG-EYLENRRYYSAlivtSADADVIALVqDATEPES 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 110832837 770 I---TFGSPFNKQRYKAVTdacslqpDIDLLPFGDQTEIGERGINLSGGQR 817
Cdd:pfam10662 79 TfppGFASMFNKPVIGIIT-------KIDLAKDEANIEIAEEWLSLAGAQK 122
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
688-872 |
7.45e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNVNESEPSFEAtrsrnrySVAYAAQKPW-LLNA 764
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgvITGGDRLVNGRPLDSSFQR-------SIGYVQQQDLhLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 765 TVEENITFgSPFNKQRyKAVTDACS---LQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTN-IVFLDDP 838
Cdd:TIGR00956 852 TVRESLRF-SAYLRQP-KSVSKSEKmeyVEEVIKLLEMESYADavVGVPGEGLNVEQRKRLTIGVELVAKPKlLLFLDEP 929
|
170 180 190
....*....|....*....|....*....|....
gi 110832837 839 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 872
Cdd:TIGR00956 930 TSGLDSQTAWSICK--LMRKLADHGQAILCTIHQ 961
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1338-1481 |
7.62e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 43.71 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1338 PGQKV-GICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG---IDISK---LPLHtlRSRLSIILQDPILFSG-SIRFNLDP 1409
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPE--KRRIGYVFQDARLFPHyKVRGNLRY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110832837 1410 ECKCTD----DRLWEALEIAQLknmVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDM 1481
Cdd:PRK11144 100 GMAKSMvaqfDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1080-1215 |
8.82e-04 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 43.17 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1080 PIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIG-MISYATPVFLVALLPL---GVAFYFIQKYFRV 1155
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVmMFTISPKLTLIALLPLpllALLVYRLGKKIHK 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 1156 ASKDLQE----LDDSTQlpllchfsETAEGLTTIRAFRHETRFKQRMLELTDTN---NIAYLFLSAA 1215
Cdd:cd18541 167 RFRKVQEafsdLSDRVQ--------ESFSGIRVIKAFVQEEAEIERFDKLNEEYvekNLRLARVDAL 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1312-1480 |
9.37e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.26 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1312 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 1391
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1392 ILQdpilFSgsirfNLDPECKCTDDRL----WEALEIAQLKNMVKSL------PGGLDAVVTEggenFSVGQRQLFCLAR 1461
Cdd:PRK13537 85 VPQ----FD-----NLDPDFTVRENLLvfgrYFGLSAAAARALVPPLlefaklENKADAKVGE----LSGGMKRRLTLAR 151
|
170
....*....|....*....
gi 110832837 1462 AFVRKSSILIMDEATASID 1480
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLD 170
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
698-871 |
9.70e-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: 42.78 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 698 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVnesepsfeatrsrnrySVAYaaqKPWLLNA----TVEENItfg 773
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD----------------TVSY---KPQYIKAdyegTVRDLL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 774 spfnkqrYKAVTDACS---LQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsDHL 850
Cdd:cd03237 83 -------SSITKDFYThpyFKTEI-AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRL 152
|
170 180
....*....|....*....|..
gi 110832837 851 MQEGILK-FLQDDKRTLVLVTH 871
Cdd:cd03237 153 MASKVIRrFAENNEKTAFVVEH 174
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1025-1217 |
1.14e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 42.79 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1025 NNTGKADQTYYVAGFSILCGAGIFLCL------VTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSA 1098
Cdd:cd18554 32 GSSLTLDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVIN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1099 DTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVA---LLPL-GVAFYFIQKYFRVASKDL-QELDDstqlpLLC 1173
Cdd:cd18554 112 DVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFyILAVKYFFGRLRKLTKERsQALAE-----VQG 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110832837 1174 HFSETAEGLTTIRAFRHETRFKQrmlELTDTNNiayLFLSAANR 1217
Cdd:cd18554 187 FLHERIQGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
813-899 |
1.20e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.79 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 813 SGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLTH-ADWIIAMKD 887
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDLGVVAGiCDKVLVMYA 237
|
90
....*....|..
gi 110832837 888 GSVLREGTLKDI 899
Cdd:PRK09473 238 GRTMEYGNARDV 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
684-900 |
1.27e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 684 GLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNvneSEPSFEATRSRNRYSVAYAAQKPWLL- 762
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSQEAGIGIIHQELNLIp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 763 NATVEENITFG----SPFNKQRYKAVTDacslQPDIDL----LPFGDQTEIGErginLSGGQRQRICVARALYQNTNIVF 834
Cdd:PRK10762 93 QLTIAENIFLGrefvNRFGRIDWKKMYA----EADKLLarlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110832837 835 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-THADWIIAMKDGSVLREGTLKDIQ 900
Cdd:PRK10762 165 MDEPTDALTDTETESLFR--VIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADLT 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1339-1496 |
1.62e-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: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1339 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDR 1417
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHAdHSDEQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 1418 LWEALEIAQLkNMVKSLPGGldavvteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILqkvvMTAFA 1496
Cdd:cd03231 106 VEEALARVGL-NGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF----AEAMA 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
812-899 |
1.80e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 42.08 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 812 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSD---HLMQEgilkfLQDDKR-TLVLVTHKLQYLTH-ADWIIAMK 886
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqliNLMLE-----LQEKQGiSYIYVTQHLGMMKHiSDQVLVMH 224
|
90
....*....|...
gi 110832837 887 DGSVLREGTLKDI 899
Cdd:PRK15112 225 QGEVVERGSTADV 237
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
688-843 |
2.34e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 688 LSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEpsfeatrsrnrysvayaAQKPWL------ 761
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-----------------IAKPYCtyighn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 762 ----LNATVEENITFGSPFnkqrYKAVTdacSLQPDIDLLPFGDQteIGERGINLSGGQRQRICVARALYQNTNIVFLDD 837
Cdd:PRK13541 79 lglkLEMTVFENLKFWSEI----YNSAE---TLYAAIHYFKLHDL--LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
....*.
gi 110832837 838 PFSALD 843
Cdd:PRK13541 150 VETNLS 155
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1071-1233 |
2.52e-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: 41.53 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1071 NLLNK-IILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTllcLSAIGMI------SYATPVFLVALLPL- 1142
Cdd:cd18784 73 NLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSL---VKAIGVIvfmfklSWQLSLVTLIGLPLi 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1143 -GVAFYFiQKYFRVASKDLQeldDStqlplLCHFSETAE----GLTTIRAFRHET----RFK---QRMLELTDTNNIAYL 1210
Cdd:cd18784 150 aIVSKVY-GDYYKKLSKAVQ---DS-----LAKANEVAEetisSIRTVRSFANEDgeanRYSeklKDTYKLKIKEALAYG 220
|
170 180
....*....|....*....|....*..
gi 110832837 1211 FLSAANRWLE----VRTDYLGACIVLT 1233
Cdd:cd18784 221 GYVWSNELTElaltVSTLYYGGHLVIT 247
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
813-876 |
2.79e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110832837 813 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFlqddKRTLVLVTHKLQYL 876
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKW----PKTFIVVSHAREFL 404
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
807-940 |
3.69e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 807 ERGIN-LSGGQRQRICVARAL-YQNTNIVF-LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLTHADWII 883
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLgAELIGITYiLDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 884 ------AMKDGSVLREGTLKDIQTKDVELYEHWKtlmnRQDQELEKDmEADQTTLERKTLRRA 940
Cdd:PRK00635 549 digpgaGIFGGEVLFNGSPREFLAKSDSLTAKYL----RQELTIPIP-EKRTNSLGTLTLSKA 606
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
811-873 |
3.76e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.69 E-value: 3.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110832837 811 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKL 873
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
805-908 |
4.79e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 805 IGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK--LQYLTHADW 881
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT--VRNTVDTGRTVVCTIHQpsIDIFEAFDE 1089
|
90 100
....*....|....*....|....*...
gi 110832837 882 IIAMK-DGSVLREGTLKDIQTKDVELYE 908
Cdd:PLN03140 1090 LLLMKrGGQVIYSGPLGRNSHKIIEYFE 1117
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1336-1524 |
5.27e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1336 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKlPLHTLRSrlSIIL------QDPILFSGSIRFNL 1407
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS-PRDAIRA--GIMLcpedrkAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1408 DPECK-------CTDDRLWEA----LEIAQLKnmVKSlPGGLDAVVteggeNFSVGQRQLFCLARAFVRKSSILIMDEAT 1476
Cdd:PRK11288 353 NISARrhhlragCLINNRWEAenadRFIRSLN--IKT-PSREQLIM-----NLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110832837 1477 ASIDM-ATENILQKVVMTAFADRTVVTIAHRVHTIL-TADLVIVMKRGNI 1524
Cdd:PRK11288 425 RGIDVgAKHEIYNVIYELAAQGVAVLFVSSDLPEVLgVADRIVVMREGRI 474
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
803-844 |
6.70e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 6.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 110832837 803 TEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 844
Cdd:PRK13409 203 ENILDRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1073-1197 |
7.17e-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: 40.12 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1073 LNKIILGPIRFFDTTPLGLILNRFSaDTNIIDQHIPPTLESLTRSTLLCL-SAIGMISYATPVFLVALLPL---GVAFYF 1148
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIiSGIILFFYNWKLFLITLLIIplyILIILL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 110832837 1149 IQKYFRVASKDLQELDDSTQlpllCHFSETAEGLTTIRAFRHETRFKQR 1197
Cdd:cd18570 161 FNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKK 205
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1344-1505 |
7.27e-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: 39.51 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1344 ICGRTGSGKSSLslaffrmvdifdgkivIDGIDISKLPLHTLRSRLSIILQDPIlFSGSIRFNLDPECKCTDDRLWEAL- 1422
Cdd:cd03240 27 IVGQNGAGKTTI----------------IEALKYALTGELPPNSKGGAHDPKLI-REGEVRAQVKLAFENANGKKYTITr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1423 EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFC------LARAFVRKSSILIMDEATASIDmaTENILQKVV----- 1491
Cdd:cd03240 90 SLAILENVIFCHQGESNWPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLD--EENIEESLAeiiee 167
|
170
....*....|....
gi 110832837 1492 MTAFADRTVVTIAH 1505
Cdd:cd03240 168 RKSQKNFQLIVITH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
805-916 |
7.31e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 805 IGERGINLSGGQRQRICVARALY---QNTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQYLTHADW 881
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQ--LRTLVSLGHSVIYIDHDPALLKQADY 1770
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 110832837 882 IIAM------KDGSVLREGTLKDIQ-TKDVELyehwKTLMNR 916
Cdd:PRK00635 1771 LIEMgpgsgkTGGKILFSGPPKDISaSKDSLL----KTYMCN 1808
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
1043-1209 |
7.37e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain] Cd Length: 289 Bit Score: 40.40 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1043 CGAGIFLCLVTSLTvewmgltaaKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCL 1122
Cdd:cd18590 55 LRGGLFMCTLSRLN---------LRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110832837 1123 SAIG-MISYATPVFLVALL--PLGVAfyfIQK----YFRVASKDLQE-LDDSTQLPllchfSETAEGLTTIRAFRHET-- 1192
Cdd:cd18590 126 GMLGfMLSLSWQLTLLTLIemPLTAI---AQKvyntYHQKLSQAVQDsIAKAGELA-----REAVSSIRTVRSFKAEEee 197
|
170 180
....*....|....*....|..
gi 110832837 1193 --RFKQ---RMLELTDTNNIAY 1209
Cdd:cd18590 198 acRYSEaleRTYNLKDRRDTVR 219
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
812-886 |
7.68e-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: 38.88 E-value: 7.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110832837 812 LSGGQRQRICVARAL----YQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLqDDKRTLVLVTHKLQYLTHADWIIAMK 886
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA-EAILEHL-VKGAQVIVITHLPELAELADKLIHIK 154
|
|
| |
