|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
110-1221 |
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: 729.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 110 IYGVALGLCGFLSGLCMQHYF-FNSLKAYQVTTNILNErLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGD 188
Cdd:TIGR00957 359 FYTGLLFVCACLQTLILHQYFhICFVSGMRIKTAVMGA-VYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINM 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 189 LISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKS 268
Cdd:TIGR00957 438 IWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELA 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 269 VAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVLFVALAVHAWRGEK--LDAAVIFTCISLFGLLEGPFGDLSRLI 346
Cdd:TIGR00957 518 FLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVI 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 347 SRATNAKVGARRILDYLNEDEVEISTEER---TDGAAVGLQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGK 423
Cdd:TIGR00957 598 SSIVQASVSLKRLRIFLSHEELEPDSIERrtiKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGK 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 424 SSLLMSLLGEVAPREGSLQFvpempgRPRMAYVPQEAYIVNTSLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLR 503
Cdd:TIGR00957 678 SSLLSALLAEMDKVEGHVHM------KGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDR 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 504 TEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLI--FGAWKDVTRIVVTHRLEHLAQFDQV 581
Cdd:TIGR00957 752 TEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVI 831
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 582 IYIQHGRVQGQGTFSELVKTCAPFAEFYKEHGKTQ--------------GEGHEVRPAE--------------------- 626
Cdd:TIGR00957 832 IVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEqqghledswtalvsGEGKEAKLIEngmlvtdvvgkqlqrqlsass 911
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 627 -----TAQEAASI----NTELEAKTTRVTEDEDREVGAVKGSVYWDYISSLGgdgKFTKPLILATLLLGATAAtllpLAQ 697
Cdd:TIGR00957 912 sdsgdQSRHHGSSaelqKAEAKEETWKLMEADKAQTGQVELSVYWDYMKAIG---LFITFLSIFLFVCNHVSA----LAS 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 698 KAWLSYYSG----HQTEWVALTAIGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRI 773
Cdd:TIGR00957 985 NYWLSLWTDdpmvNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNL 1064
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 774 IQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPRY 853
Cdd:TIGR00957 1065 VNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVY 1144
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 854 AHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLISMATAVGVSLSAYygVMDAGTA 933
Cdd:TIGR00957 1145 SHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRH--SLSAGLV 1222
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 934 GLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLKFFSNL----PGEVSVLKPlPEplrpTWPEFGEISVEGLKVRYASH 1009
Cdd:TIGR00957 1223 GLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETekeaPWQIQETAP-PS----GWPPRGRVEFRNYCLRYRED 1297
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1010 LPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIR 1089
Cdd:TIGR00957 1298 LDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLR 1377
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1090 NNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTD 1169
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1170 ALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTEFSQE 1221
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-1222 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 680.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 2 NFFRRLLFTDVTPLVKLAKTKNIEESDLLAL-----PQELNPQHIKVDMQEISWKSPRaLLFSLIRALRDFTRPAYIWYL 76
Cdd:PLN03130 233 NIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLdtwdqTETLYRSFQKCWDEELKKPKPW-LLRALNNSLGGRFWLGGFFKI 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 77 ASSVLALLSPVFVNRFIGTISAGVTAETlptALIYGVALGLCGFLSGLCMQHYFFNSLKAYQVTTNILNERLFKHSLKLS 156
Cdd:PLN03130 312 GNDLSQFVGPLLLNLLLESMQNGEPAWI---GYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLT 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 157 QKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVAKKFTHLD 236
Cdd:PLN03130 389 HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLT 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 237 EEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRrlaKAEVVSSLGYL---AVSTLVLFVALAVH 313
Cdd:PLN03130 469 KEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFR---KAQLLSAFNSFilnSIPVLVTVVSFGVF 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 314 AWRGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRILDYLnedeveiSTEER---------TDGAAVGLQ 384
Cdd:PLN03130 546 TLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELL-------LAEERvllpnpplePGLPAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 385 MQHFSLRHDGAVSdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpempgRPRMAYVPQEAYIVN 464
Cdd:PLN03130 619 NGYFSWDSKAERP-TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI-----RGTVAYVPQVSWIFN 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 TSLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:PLN03130 693 ATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 545 ADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPFAEFYKEHGK---TQGEGHE 621
Cdd:PLN03130 773 AHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKmeeYVEENGE 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 622 V-------------RPAETAQEAASINTELEAKTTRVTEDEdREVGAVKGSVYWDYISSLGGdgkftkPLILATLLLGAT 688
Cdd:PLN03130 853 EeddqtsskpvangNANNLKKDSSSKKKSKEGKSVLIKQEE-RETGVVSWKVLERYKNALGG------AWVVMILFLCYV 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 689 AATLLPLAQKAWLSYYSGHQT--EWVALTAIGIYGLIGVLVLVGSLLNHlFWL-DRGIRAGKNMHDKMLKSVLSSPVRFF 765
Cdd:PLN03130 926 LTEVFRVSSSTWLSEWTDQGTpkTHGPLFYNLIYALLSFGQVLVTLLNS-YWLiMSSLYAAKRLHDAMLGSILRAPMSFF 1004
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 766 DSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFD 845
Cdd:PLN03130 1005 HTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLD 1084
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 846 SVARSPRYAHFKESLQGLVVIRSFNKGPWfMQNFYAKlSHSNRMFYSHVMI--NRWFSSRIPLVGGLIsmatavgVSLSA 923
Cdd:PLN03130 1085 SITRSPVYAQFGEALNGLSTIRAYKAYDR-MAEINGR-SMDNNIRFTLVNMssNRWLAIRLETLGGLM-------IWLTA 1155
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 924 YYGVMD----------AGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLKFFSNLPGEVSvlkPLPEPLRPT--W 991
Cdd:PLN03130 1156 SFAVMQngraenqaafASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAP---LVIENNRPPpgW 1232
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 992 PEFGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLR 1071
Cdd:PLN03130 1233 PSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR 1312
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLAIIPQDPTLFMGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTK 1151
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRR 1392
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1152 ARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTEFSQEE 1222
Cdd:PLN03130 1393 SKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-1222 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 674.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 2 NFFRRLLFTDVTPLVKLAKTKNIEESDLLALPQELNPQHIKVDMQEISWKSPRALLFSLIRALRDFTRPAY----IWYLA 77
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKPWLLRALNNSLGGRFwlggIFKIG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 78 SSVLALLSPVFVNRFIGTISAGVTAETlptALIYGVALGLCGFLSGLCMQHYFFNSLKAYQVTTNILNERLFKHSLKLSQ 157
Cdd:PLN03232 313 HDLSQFVGPVILSHLLQSMQEGDPAWV---GYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTH 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 158 KSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVAKKFTHLDE 237
Cdd:PLN03232 390 EARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 238 EMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRrlaKAEVVSSLGYLAVSTL---VLFVALAVHA 314
Cdd:PLN03232 470 EGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFR---KAQLLSAFNSFILNSIpvvVTLVSFGVFV 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 315 WRGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRILD-YLNEDEVEISTEERTDGA-AVGLQMQHFSLrh 392
Cdd:PLN03232 547 LLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEElLLSEERILAQNPPLQPGApAISIKNGYFSW-- 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 393 DGAVSD-VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpempgRPRMAYVPQEAYIVNTSLLENL 471
Cdd:PLN03232 625 DSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI-----RGSVAYVPQVSWIFNATVRENI 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 QFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLL 551
Cdd:PLN03232 700 LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 552 CERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPFAEFYKEHGKTQGEGHE---------V 622
Cdd:PLN03232 780 FDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVntndenilkL 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 623 RPAETA----QEAASINTELEAKTTRVTEDEdREVGAVKGSVYWDYISSLGGdgkftkPLILATLLLGATAATLLPLAQK 698
Cdd:PLN03232 860 GPTVTIdvseRNLGSTKQGKRGRSVLVKQEE-RETGIISWNVLMRYNKAVGG------LWVVMILLVCYLTTEVLRVSSS 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 699 AWLSYYSGHQT--EWVALTAIGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQR 776
Cdd:PLN03232 933 TWLSIWTDQSTpkSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINR 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 777 FSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPRYAHF 856
Cdd:PLN03232 1013 FSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQF 1092
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 857 KESLQGLVVIRSFNKGPWfMQNFYAKLSHSN-RMFYSHVMINRWFSSRIPLVGGLISMATAVGVSLSayYGVMD-----A 930
Cdd:PLN03232 1093 GEALNGLSSIRAYKAYDR-MAKINGKSMDNNiRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLR--NGNAEnqagfA 1169
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 931 GTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLKFFSNLPGEVSVLKPLPEPLrPTWPEFGEISVEGLKVRYASHL 1010
Cdd:PLN03232 1170 STMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPV-SGWPSRGSIKFEDVHLRYRPGL 1248
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1011 PQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRN 1090
Cdd:PLN03232 1249 PPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRF 1328
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1091 NLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDA 1170
Cdd:PLN03232 1329 NIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1171 LLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTEFSQEE 1222
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
52-1217 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 582.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 52 SPRALlfSLIRALRdFTRPAYIWY-----LASSVLALLSPVFVNRFIGTISAGvtaetlPTALIYGVALGLCGFLSGL-- 124
Cdd:PTZ00243 228 TPKRL--SLLRTLF-AALPYYVWWqipfkLLSDVCTLTLPVLLKYFVKFLDAD------NATWGRGLGLVLTLFLTQLiq 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 125 --CMQHYFFNSLKAYQVTTNILNERLFKHSLKLSQKSRQKNQ--VGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVV 200
Cdd:PTZ00243 299 svCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDmnTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 201 AMLFYYIGWSALAALAVLFILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKE 280
Cdd:PTZ00243 379 LLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 281 LTSRRRLAKAEVVSSLGYLAVSTLVLFVALAVHAWRGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRIL 360
Cdd:PTZ00243 459 LRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRIS 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 361 DYLN---------EDEVEISTEERTDGAAVGL-----------------------QMQHFS------------------- 389
Cdd:PTZ00243 539 TFLEcdnatcstvQDMEEYWREQREHSTACQLaavlenvdvtafvpvklprapkvKTSLLSralrmlcceqcrptkrhps 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 390 ----------------LRH--DGAVSDV-----------------------------LHDVNVHVPAGSSLAIVGPVGAG 422
Cdd:PTZ00243 619 psvvvedtdygspssaSRHivEGGTGGGheatptsersaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSG 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 423 KSSLLMSLLGEVAPREGslqfvpEMPGRPRMAYVPQEAYIVNTSLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGL 502
Cdd:PTZ00243 699 KSTLLQSLLSQFEISEG------RVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGL 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 503 RTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVI 582
Cdd:PTZ00243 773 ETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVV 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 583 YIQHGRVQGQGTFSELVKT--CAPFAEFYKE--HGKTQGEGHEVRPAETAQEAASINTELEAKTTRVTEDED-------- 650
Cdd:PTZ00243 853 ALGDGRVEFSGSSADFMRTslYATLAAELKEnkDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDgaaldaaa 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 651 --------REVGAVKGSVYWDYISSLGGdgkftkpLILATLLLGATAAT-LLPLAQKAWLSYYSGHQTEWVALTAIGIYG 721
Cdd:PTZ00243 933 grlmtreeKASGSVPWSTYVAYLRFCGG-------LHAAGFVLATFAVTeLVTVSSGVWLSMWSTRSFKLSAATYLYVYL 1005
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 722 LIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQ 801
Cdd:PTZ00243 1006 GIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFS 1085
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 802 VIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYA 881
Cdd:PTZ00243 1086 ICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALR 1165
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 882 KLSHSNRMFYSHVMINRWFSSRIPLVGGLISMATA-VGVSlsayyGVMDAGTAGLVTLYSLSF------WGFLNWGVRIF 954
Cdd:PTZ00243 1166 RLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIAlIGVI-----GTMLRATSQEIGLVSLSLtmamqtTATLNWLVRQV 1240
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 955 ADIESRMTSIERLKFFSN---------LPGEVSVLKP------------LPEPLRPTWP-----EFGEISVEGLKVRYAS 1008
Cdd:PTZ00243 1241 ATVEADMNSVERLLYYTDevphedmpeLDEEVDALERrtgmaadvtgtvVIEPASPTSAaphpvQAGSLVFEGVQMRYRE 1320
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1009 HLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTI 1088
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTV 1400
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1089 RNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKAR-VIVMDEATASVDVQ 1167
Cdd:PTZ00243 1401 RQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPA 1480
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|
gi 499478341 1168 TDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE 1217
Cdd:PTZ00243 1481 LDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRE 1530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
991-1215 |
3.05e-123 |
|
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: 378.29 E-value: 3.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 991 WPEFGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKL 1070
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1071 RRSLAIIPQDPTLFMGTIRNNLDRYNEYSDDEVMGALKhasmwdyvqslpdgmnsaVSEGGLNLSQGQRQLLCLARALLT 1150
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1151 KARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRP 1215
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-1210 |
2.29e-122 |
|
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: 413.15 E-value: 2.29e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 2 NFFRRLLFTDVTPLVKLAKTKNIEESDLLALPQELNPQHIKvDMQEISW--------KSPRallfsLIRALR-----DFT 68
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLS-ERLEREWdrelasakKNPK-----LLNALRrcffwRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 69 RPAYIWYLASSVLALlSPVFVNRFIGTISAGVTAETlptALIYGVALGLCG-FLSGLCMQHYFFNSLKAYQVTTNI-LNE 146
Cdd:TIGR01271 84 FYGILLYFGEATKAV-QPLLLGRIIASYDPFNAPER---EIAYYLALGLCLlFIVRTLLLHPAIFGLHHLGMQMRIaLFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 147 RLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTN 226
Cdd:TIGR01271 160 LIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 227 YVAKKfthldeeMMEHRD-------RRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYL 299
Cdd:TIGR01271 240 CLGQK-------MMPYRDkragkisERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 300 AVSTLVLFVALAVHAW-RGEKLDAavIFTCISLFGLLEGPfgdLSRLISRATNA---KVGA-RRILDYLNEDE------- 367
Cdd:TIGR01271 313 FSGFFVVFLSVVPYALiKGIILRR--IFTTISYCIVLRMT---VTRQFPGAIQTwydSLGAiTKIQDFLCKEEyktleyn 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 368 -----VEI---------------------STEERTDGAAVGLQMQHFSLRhdgaVSDVLHDVNVHVPAGSSLAIVGPVGA 421
Cdd:TIGR01271 388 lttteVEMvnvtaswdegigelfekikqnNKARKQPNGDDGLFFSNFSLY----VTPVLKNISFKLEKGQLLAVAGSTGS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 422 GKSSLLMSLLGEVAPREGSLQFvpempgRPRMAYVPQEAYIVNTSLLENLQFGeeVSKEELR-RALHNSC-LSRDLKEWS 499
Cdd:TIGR01271 464 GKSSLLMMIMGELEPSEGKIKH------SGRISFSPQTSWIMPGTIKDNIIFG--LSYDEYRyTSVIKACqLEEDIALFP 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 500 GGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQFD 579
Cdd:TIGR01271 536 EKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKAD 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 580 QVIYIQHGRVQGQGTFSEL----------VKTCAPFAEFYKEHGKT-----------QGEGHEVRPAETAQEA------- 631
Cdd:TIGR01271 616 KILLLHEGVCYFYGTFSELqakrpdfsslLLGLEAFDNFSAERRNSiltetlrrvsiDGDSTVFSGPETIKQSfkqpppe 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 632 -----------------------------ASINTE-------LEAKTTRVTEDEDREVGAVKGSVYWD------------ 663
Cdd:TIGR01271 696 faekrkqsiilnpiasarkfsfvqmgpqkAQATTIedavrepSERKFSLVPEDEQGEESLPRGNQYHHglqhqaqrrqsv 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 664 ---------------------------------------YISSLGGDGKF------------------------------ 674
Cdd:TIGR01271 776 lqlmthsnrgenrreqlqtsfrkkssitqqnelaseldiYSRRLSKDSVYeiseeineedlkecfaderenvfetttwnt 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 675 -------TKPLILATLL-----LGATAATLL-----------PLAQKAWLSYYSGHQTEW-VALTAIGIYGLIGVLV-LV 729
Cdd:TIGR01271 856 ylryittNRNLVFVLIFclvifLAEVAASLLglwlitdnpsaPNYVDQQHANASSPDVQKpVIITPTSAYYIFYIYVgTA 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 730 GSLLNHLFWldRG-------IRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQV 802
Cdd:TIGR01271 936 DSVLALGFF--RGlplvhtlLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIV 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 803 IVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAK 882
Cdd:TIGR01271 1014 LGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKA 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 883 LSHSNRMFYSHVMINRWFSSRIPLVGGLISMATAVGVSLSAYYGvmdAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMT 962
Cdd:TIGR01271 1094 LNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDG---EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMR 1170
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 963 SIERLKFFSNLPGEVSVLKPLPEPLRPT-------------WPEFGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGI 1029
Cdd:TIGR01271 1171 SVSRVFKFIDLPQEEPRPSGGGGKYQLStvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGL 1250
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1030 IGRTGSGKSTFFQSLFRFIEAEeGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRYNEYSDDEVMGALKH 1109
Cdd:TIGR01271 1251 LGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEE 1329
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1110 ASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIA 1189
Cdd:TIGR01271 1330 VGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSE 1409
|
1450 1460
....*....|....*....|.
gi 499478341 1190 HRLGTIADCDQIVEISAGEVK 1210
Cdd:TIGR01271 1410 HRVEALLECQQFLVIEGSSVK 1430
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
676-1209 |
1.36e-121 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 388.37 E-value: 1.36e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 676 KPLILATLL--LGATAATLLPLAQKAWLSYYSGHQTEWVALTAIGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKM 753
Cdd:COG1132 21 GLLILALLLllLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 754 LKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRD 833
Cdd:COG1132 101 FEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 834 YRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLISM 913
Cdd:COG1132 181 FGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 914 ATAVGVSLSAYYGVMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLKFFSNLPGEVsVLKPLPEPLRPTwpe 993
Cdd:COG1132 261 LVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI-PDPPGAVPLPPV--- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 994 FGEISVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRS 1073
Cdd:COG1132 337 RGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPTLFMGTIRNNLdRY--NEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTK 1151
Cdd:COG1132 416 IGVVPQDTFLFSGTIRENI-RYgrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKD 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1152 ARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
995-1210 |
8.46e-112 |
|
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: 348.33 E-value: 8.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARV 1154
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1155 IVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVK 1210
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
51-610 |
2.11e-103 |
|
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: 2.11e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 51 KSPRALLFSLIRALRDFTRP---AYIWYLASSVLALLSPVFVNRFIGTISAGVTAETLPTALIYGVALGLCGFLSGLcMQ 127
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLlilALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSY-LQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 128 HYFFNSLkAYQVTTNiLNERLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDF-PMVFGDLISASFLIIGVVAMLFYY 206
Cdd:COG1132 82 RYLLARL-AQRVVAD-LRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFlAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 207 IGWSALAALAVLFILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRR 286
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 287 LAKAEVVSSLGYLAVSTLVLFVALAVHAWR--GEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRILDYLN 364
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLvlSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 365 EDEVEISTEERTDGAAV--GLQMQHFSLRHDGAvSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQ 442
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVrgEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 443 F----VPEMPG---RPRMAYVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLS 514
Cdd:COG1132 399 IdgvdIRDLTLeslRRQIGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 515 GGQKQRVALARAFLRKPQIVLLDDPLSAVDADTenllcERLIFGA----WKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQ 590
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTET-----EALIQEAlerlMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570 580
....*....|....*....|
gi 499478341 591 GQGTFSELVKTCAPFAEFYK 610
Cdd:COG1132 554 EQGTHEELLARGGLYARLYR 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
679-1209 |
8.76e-88 |
|
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: 300.21 E-value: 8.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 679 ILATLLLGATAATLLPLAqkawLSYYS---------GHQTEWVALTAIGIygliGVLVLVGSLLNHL--FWLDR-GIRAG 746
Cdd:COG2274 157 LLLQVLLASLLINLLALA----TPLFTqvvidrvlpNQDLSTLWVLAIGL----LLALLFEGLLRLLrsYLLLRlGQRID 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 747 KNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFsRDVESV-DVYLQWSFDSAVHcALQVIVSIVLIL---GLMPLMVFVIAP 822
Cdd:COG2274 229 LRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIrEFLTGSLLTALLD-LLFVLIFLIVLFfysPPLALVVLLLIP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 823 VMALY-YVLQRDYRRPAREVkrfdSVARSPRYAHFKESLQGLVVIRSFNKGPWFM---QNFYAKLSHSNrmfYSHVMINR 898
Cdd:COG2274 307 LYVLLgLLFQPRLRRLSREE----SEASAKRQSLLVETLRGIETIKALGAESRFRrrwENLLAKYLNAR---FKLRRLSN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 899 WFSSriplVGGLISMATAVGVSLSAYYGVMDAG-TAG-LVTLYSLSfWGFLNWGVRI---FADIESRMTSIERLKFFSNL 973
Cdd:COG2274 380 LLST----LSGLLQQLATVALLWLGAYLVIDGQlTLGqLIAFNILS-GRFLAPVAQLiglLQRFQDAKIALERLDDILDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 974 PGEVSVLKPLPEPLRPTwpefGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEG 1053
Cdd:COG2274 455 PPEREEGRSKLSLPRLK----GDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1054 SISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRYNEY-SDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGL 1132
Cdd:COG2274 531 RILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1133 NLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
678-971 |
8.22e-87 |
|
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: 283.63 E-value: 8.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILATLLLGATAATLLPLAQKAWLSYYSGHQTEWVALTAIGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSV 757
Cdd:cd18580 3 LLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 758 LSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRP 837
Cdd:cd18580 83 LRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 838 AREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLISMATAV 917
Cdd:cd18580 163 SRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVAL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 918 GVSLSAYYgvMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLKFFS 971
Cdd:cd18580 243 LAVLLRSS--ISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
383-588 |
1.55e-84 |
|
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: 273.58 E-value: 1.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSD---VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRprMAYVPQE 459
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS----VPGS--IAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 460 AYIVNTSLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:cd03250 75 PWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 540 LSAVDADTENLLCERLIFGAWKDV-TRIVVTHRLEHLAQFDQVIYIQHGR 588
Cdd:cd03250 155 LSAVDAHVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
51-611 |
2.40e-84 |
|
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: 290.58 E-value: 2.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 51 KSPRALLFSLIRALRDFTRPAYIWYLASSVLALLSPVFVNRFIGTIsagVTAETLPTALIYGVALGLCGFLSGL--CMQH 128
Cdd:COG2274 141 PFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRV---LPNQDLSTLWVLAIGLLLALLFEGLlrLLRS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 129 YFFnsLKAYQVTTNILNERLFKHSLKLSQKSRQKNQVGDIVNHMSsDSDNVSDFpmVFGDLISAS----FLIIGVVAMLF 204
Cdd:COG2274 218 YLL--LRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREF--LTGSLLTALldllFVLIFLIVLFF 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 205 YYiGWSALAALAVLFILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFA--------WEKSVAKEVtev 276
Cdd:COG2274 293 YS-PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGaesrfrrrWENLLAKYL--- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 277 rEKELTSRRRLAKAEVVSSLGYLAVSTLVLFV-ALAVHAwrgEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVG 355
Cdd:COG2274 369 -NARFKLRRLSNLLSTLSGLLQQLATVALLWLgAYLVID---GQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 356 ARRILDYLNEdEVEISTEER---TDGAAVGLQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG 432
Cdd:COG2274 445 LERLDDILDL-PPEREEGRSklsLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 433 EVAPREGSLQF---------VPEMpgRPRMAYVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGL 502
Cdd:COG2274 524 LYEPTSGRILIdgidlrqidPASL--RRQIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 503 RTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLiFGAWKDVTRIVVTHRLEHLAQFDQVI 582
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL-RRLLKGRTVIIIAHRLSTIRLADRII 680
|
570 580
....*....|....*....|....*....
gi 499478341 583 YIQHGRVQGQGTFSELVKTCAPFAEFYKE 611
Cdd:COG2274 681 VLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
71-359 |
3.46e-79 |
|
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: 262.04 E-value: 3.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 71 AYIWYLASSVLALLSPVFVNRFIGTISAGvTAETLPTALIYGVALGLCGFLSGLCMQHYFFNSLKAYQVTTNILNERLFK 150
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSY-PDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 151 HSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVAK 230
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 231 KFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVLFVAL 310
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499478341 311 AVHAWRGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18579 241 ATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
147-610 |
5.30e-79 |
|
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: 271.25 E-value: 5.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 147 RLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPM-VFGDLISASFLIIGVVAMLFYY---IGWSALAALAVLFILA 222
Cdd:COG4987 93 RLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLrVLLPLLVALLVILAAVAFLAFFspaLALVLALGLLLAGLLL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 223 PLTNYVAKKftHLDEEMMEHRDRRVTLMTQAMNAIRVVKYF-AWEKSVAKevTEVREKELT-SRRRLAKAE-VVSSLGYL 299
Cdd:COG4987 173 PLLAARLGR--RAGRRLAAARAALRARLTDLLQGAAELAAYgALDRALAR--LDAAEARLAaAQRRLARLSaLAQALLQL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 300 AVSTLVLFV-ALAVHAWRGEKLD----AAVIFTCISLFGLLeGPFGDLSRLISRATNAkvgARRILDYLN-EDEVEISTE 373
Cdd:COG4987 249 AAGLAVVAVlWLAAPLVAAGALSgpllALLVLAALALFEAL-APLPAAAQHLGRVRAA---ARRLNELLDaPPAVTEPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 374 ERTDGAAVGLQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG 449
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdLRDLDE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 450 ---RPRMAYVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALAR 525
Cdd:COG4987 405 ddlRRRIAVVPQRPHLFDTTLRENLRLArPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALAR 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 526 AFLRKPQIVLLDDPLSAVDADTENLLCeRLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPF 605
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALL-ADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
....*
gi 499478341 606 AEFYK 610
Cdd:COG4987 564 RQLYQ 568
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
681-968 |
1.04e-77 |
|
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: 258.17 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 681 ATLLLGATAATLLPLAQKAWLSYYSGHQTEWVALTA--------IGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDK 752
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPsevsvlyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 753 MLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQR 832
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 833 DYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLIS 912
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 913 MATAVgvsLSAYYGVMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLK 968
Cdd:cd18604 242 FATAA---LLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQ 294
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
700-968 |
3.49e-75 |
|
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: 251.24 E-value: 3.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 700 WLSYYSGHQ----TEWVALTA--IGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRI 773
Cdd:cd18603 21 WLSEWSDDPalngTQDTEQRDyrLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 774 IQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPRY 853
Cdd:cd18603 101 LNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 854 AHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLISMATAVgvsLSAYY-GVMDAGT 932
Cdd:cd18603 181 SHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAAL---FAVLSrDSLSPGL 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 499478341 933 AGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLK 968
Cdd:cd18603 258 VGLSISYALQITQTLNWLVRMTSELETNIVSVERIK 293
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
676-1222 |
3.80e-74 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 257.38 E-value: 3.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 676 KPLILATLLlgATAATLLPLAQkAWL------SYYSGHQTEWVALTAIGiyGLIGVLVLVGSLLnhlFWLDR-----GIR 744
Cdd:COG4988 17 RWLALAVLL--GLLSGLLIIAQ-AWLlasllaGLIIGGAPLSALLPLLG--LLLAVLLLRALLA---WLRERaafraAAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 745 AGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQwSFDSAVhcALQVIVSIVLILGLMP------LMVF 818
Cdd:COG4988 89 VKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFA-RYLPQL--FLAALVPLLILVAVFPldwlsgLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 819 VIAPV----MALYYVLQRDYRRparevKRFDSVAR-SpryAHFKESLQGLVVIRSFNKGPWFMQNFyAKLSHSNR---M- 889
Cdd:COG4988 166 VTAPLiplfMILVGKGAAKASR-----RQWRALARlS---GHFLDRLRGLTTLKLFGRAKAEAERI-AEASEDFRkrtMk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 890 -----FYSHVMINrWFSSriplvgglISMA-TAVGVSLSAYYGVMDAGTAGLVTLYSLSFwgFLNwgVRIF-ADIESRMT 962
Cdd:COG4988 237 vlrvaFLSSAVLE-FFAS--------LSIAlVAVYIGFRLLGGSLTLFAALFVLLLAPEF--FLP--LRDLgSFYHARAN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 963 SI---ERLKFFSNLPGEVSVLKPLPEPlrptWPEFGEISVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKST 1039
Cdd:COG4988 304 GIaaaEKIFALLDAPEPAAPAGTAPLP----AAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKST 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1040 FFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRYN-EYSDDEVMGALKHASMWDYVQS 1118
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1119 LPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADC 1198
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
570 580
....*....|....*....|....
gi 499478341 1199 DQIVEISAGEVKSIRRPTEFSQEE 1222
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
73-359 |
5.91e-72 |
|
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: 242.40 E-value: 5.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 73 IWYLASSVLALLSPVFVNRFIGTISAGvTAETLPTALIYGVALGLCGFLSGLCMQHYFFNSLKAYQVTTNILNERLFKHS 152
Cdd:cd18596 4 LLAVLSSVLSFAPPFFLNRLLRYLEDP-GEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 153 LKL-------------------SQKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALA 213
Cdd:cd18596 83 LRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 214 ALAVLFILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVV 293
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 294 SSLGYLAVSTLVLFVALAVHAW-RGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLvMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
677-967 |
3.73e-66 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 225.43 E-value: 3.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 677 PLILATLLLgATAATLLplaQKAWLSYYSGHQTEWVALTAIGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKS 756
Cdd:cd18606 2 PLLLLLLIL-SQFAQVF---TNLWLSFWTEDFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 757 VLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRR 836
Cdd:cd18606 78 VLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 837 PAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLISMATA 916
Cdd:cd18606 158 SSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 917 VGVSLSAYygVMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERL 967
Cdd:cd18606 238 LLCVTRRF--SISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERL 286
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
672-1209 |
1.03e-65 |
|
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: 233.46 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 672 GKFTKPLILATLLLGATAAT--LLPLAQKAWLSYYSGHQTE----WVALTAIGIYGLIGVLVLVGSLLnhLFWLDRGIRa 745
Cdd:TIGR02203 10 RPYKAGLVLAGVAMILVAATesTLAALLKPLLDDGFGGRDRsvlwWVPLVVIGLAVLRGICSFVSTYL--LSWVSNKVV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 746 gKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGL---MPLMVFVIAP 822
Cdd:TIGR02203 87 -RDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYswqLTLIVVVMLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 823 VMA-LYYVLQRDYRRPAREVKrfDSVARSPRYAhfKESLQGLVVIRSFNkGPWFMQNFYAKLSHSNRMFYSHVMINRWFS 901
Cdd:TIGR02203 166 VLSiLMRRVSKRLRRISKEIQ--NSMGQVTTVA--EETLQGYRVVKLFG-GQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 902 SriPLVGGLISMATAVGVSLSAYYGVMDAGTAGLVTLYSLSFwGFLNWGVRIFADIESRM----TSIERLKFFSNLPGEV 977
Cdd:TIGR02203 241 S--PITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAM-IALIRPLKSLTNVNAPMqrglAAAESLFTLLDSPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 978 SVLKPLPEPLRptwpefGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISI 1057
Cdd:TIGR02203 318 DTGTRAIERAR------GDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1058 DGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNL--DRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLS 1135
Cdd:TIGR02203 392 DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIayGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1136 QGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
995-1211 |
3.82e-65 |
|
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: 220.17 E-value: 3.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDRYNEYSDDE-VMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKAR 1153
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEeVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKS 1211
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
995-1222 |
5.76e-65 |
|
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: 220.94 E-value: 5.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARV 1154
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1155 IVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE-FSQEE 1222
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENlLAQED 246
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
700-968 |
2.03e-64 |
|
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: 220.86 E-value: 2.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 700 WLSYYSGHQTEWVALTA-------IGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGR 772
Cdd:cd18605 21 WLSYWVSHSNNSFFNFIndsfnffLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 773 IIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPR 852
Cdd:cd18605 101 ILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 853 YAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLIsmatAVGVSLSA-----YYGV 927
Cdd:cd18605 181 YTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLI----VTFVALTAvvqhfFGLS 256
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499478341 928 MDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLK 968
Cdd:cd18605 257 IDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVR 297
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
771-1217 |
4.55e-64 |
|
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: 228.50 E-value: 4.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 771 GRIIQRFSRDVESVD-VYLQWSFDSAVHCALQVIVSIV---------LILGLMPLMVFVIAPVMAlyYVLQRdyrRPARE 840
Cdd:COG4987 112 GDLLNRLVADVDALDnLYLRVLLPLLVALLVILAAVAFlaffspalaLVLALGLLLAGLLLPLLA--ARLGR---RAGRR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 841 VKRfdsvARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAK----LSHSNRMfyshvminRWFSSRIPLVGGLISMATA 916
Cdd:COG4987 187 LAA----ARAALRARLTDLLQGAAELAAYGALDRALARLDAAearlAAAQRRL--------ARLSALAQALLQLAAGLAV 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 917 VGVSLSAYYGVMDAGTAG----LVTLYSLSFwgFLNWG--VRIFADIESRMTSIERLKFFSNLPGEVsvlkplPEPLRPT 990
Cdd:COG4987 255 VAVLWLAAPLVAAGALSGpllaLLVLAALAL--FEALAplPAAAQHLGRVRAAARRLNELLDAPPAV------TEPAEPA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 991 W-PEFGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEK 1069
Cdd:COG4987 327 PaPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 LRRSLAIIPQDPTLFMGTIRNNLdRY--NEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARA 1147
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENL-RLarPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARA 485
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1148 LLTKARVIVMDEATASVDVQT-DALLQKvIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE 1217
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATeQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
51-601 |
2.36e-62 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 223.48 E-value: 2.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 51 KSPRALLFSLIRALRDFTRPAYIWYLASSVLALLSPVFVNRFI-GTISAGVTAETLPTALIYGVALGLCGFLSGLCMQHY 129
Cdd:COG4988 2 KPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 130 ffnSLKAYQVTTNILNERLFKHSLKLSQKSRQKNQVGDIVNHMSsdsDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGW 209
Cdd:COG4988 82 ---AFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLT---EGVEALDGYFARYLPQLFLAALVPLLILVAVFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 210 SALAALAVLFILAPLT-------NYVAKKfthldeEMMEHRDRRVTLMTQAMNAIR---VVKYFAWEKSVAKEVTEVREK 279
Cdd:COG4988 156 LDWLSGLILLVTAPLIplfmilvGKGAAK------ASRRQWRALARLSGHFLDRLRgltTLKLFGRAKAEAERIAEASED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 280 eltSRRRlakaevvsSLGYLAV---STLVL--FVALAVhAWrgekldAAVIFtcisLFGLLEG----------------- 337
Cdd:COG4988 230 ---FRKR--------TMKVLRVaflSSAVLefFASLSI-AL------VAVYI----GFRLLGGsltlfaalfvlllapef 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 338 --PFGDLSRLISRATNAKVGARRILDYLNEDEVEISTEERT--DGAAVGLQMQHFSLRHDGAVsDVLHDVNVHVPAGSSL 413
Cdd:COG4988 288 flPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPlpAAGPPSIELEDVSFSYPGGR-PALDGLSLTIPPGERV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 414 AIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG---RPRMAYVPQEAYIVNTSLLENLQFGE-EVSKEELRRA 485
Cdd:COG4988 367 ALVGPSGAGKSTLLNLLLGFLPPYSGSILIngvdLSDLDPaswRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 486 LHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFGAWKDVTR 565
Cdd:COG4988 447 LEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI-LQALRRLAKGRTV 525
|
570 580 590
....*....|....*....|....*....|....*.
gi 499478341 566 IVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKT 601
Cdd:COG4988 526 ILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
717-967 |
1.08e-61 |
|
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: 213.23 E-value: 1.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 717 IGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAV 796
Cdd:cd18602 53 ISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 797 HCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFM 876
Cdd:cd18602 133 RFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 877 QNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLISMATAVGVSLSAYYGVMDAGTAGLVTLYSLSFWGFLNWGVRIFAD 956
Cdd:cd18602 213 QQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLAD 292
|
250
....*....|.
gi 499478341 957 IESRMTSIERL 967
Cdd:cd18602 293 VEMQMNSVERV 303
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
997-1208 |
7.63e-61 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 205.69 E-value: 7.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMGTIRNNLdryneysddevmgalkhasmwdyvqslpdgmnsavsegglnLSQGQRQLLCLARALLTKARVIV 1156
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1157 MDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGE 1208
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
997-1217 |
1.72e-60 |
|
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: 207.08 E-value: 1.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMGTIRNNLdRYN--EYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARV 1154
Cdd:cd03253 80 VPQDTVLFNDTIGYNI-RYGrpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1155 IVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE 1217
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEE 221
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
700-967 |
7.68e-56 |
|
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: 196.63 E-value: 7.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 700 WLSYY----SGHQTEWVALTAIG---------------IYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSS 760
Cdd:cd18599 25 WLSYWlkqgSGNTTNNVDNSTVDsgnisdnpdlnfyqlVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 761 PVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDsavhCALQVIVSIVLILGLM----PLMVFVIAPVMALYYVLQRDYRR 836
Cdd:cd18599 105 PMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLE----NFLQNVLLVVFSLIIIaivfPWFLIALIPLAIIFVFLSKIFRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 837 PAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLISMATA 916
Cdd:cd18599 181 AIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITA 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 917 VGVSLSAyyGVMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERL 967
Cdd:cd18599 261 LLVVLLK--GSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERI 309
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
997-1209 |
1.36e-55 |
|
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: 193.22 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMGTIRNNLdRYN--EYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARV 1154
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGrpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1155 IVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
910-1209 |
8.66e-55 |
|
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: 202.36 E-value: 8.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 910 LISMATAVGVSLSAYY---GVMDAG-----TAGLVTLY-SLSFWGFlnwgvrIFADIESRMTSIERLkfFSNL--PGEVS 978
Cdd:COG5265 272 IIALGLTAMMLMAAQGvvaGTMTVGdfvlvNAYLIQLYiPLNFLGF------VYREIRQALADMERM--FDLLdqPPEVA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 979 VlKPLPEPLRPTWpefGEISVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISID 1058
Cdd:COG5265 344 D-APDAPPLVVGG---GEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILID 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1059 GVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLdRY--NEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQ 1136
Cdd:COG5265 419 GQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI-AYgrPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSG 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1137 GQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
71-359 |
1.45e-53 |
|
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: 189.22 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 71 AYIWYLASSVLALLSPVFVNRFIGTISAGvtAETLPTALIYGVALGLCGFLSGLCMQHYFFnslKAYQVTTNI---LNER 147
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDP--DEPLWKGYLYAVLLFLVSIIQSLLLHQYFH---RCFRLGMRIrtaLTSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 148 LFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNY 227
Cdd:cd18595 77 IYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 228 VAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVLF 307
Cdd:cd18595 157 LARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 308 VALAVHAWRGEK--LDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18595 237 ATFATYVLSDPDnvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
676-966 |
2.75e-53 |
|
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: 189.45 E-value: 2.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 676 KPLILATLLLGATAATLLPLAQKAWLSYYSGHQTEWVALTA--------------------IGIYGLIGVLVLVGSLLNH 735
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDrvqgenstnvdiedldrdfnLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 736 LFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPL 815
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 816 MVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVM 895
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 896 INRWFSSRIPLVGGLISMATAVGVSLSAYYgvMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIER 966
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAES--LDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVER 309
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
997-1209 |
3.17e-52 |
|
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: 183.51 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlP--QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:cd03249 1 IEFKNVSFRYPSR-PdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLdRY--NEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKA 1152
Cdd:cd03249 80 GLVSQEPVLFDGTIAENI-RYgkPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1153 RVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
995-1210 |
3.41e-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: 181.98 E-value: 3.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEeGSISIDGVNTASVPLEKLRRSL 1074
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARV 1154
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1155 IVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVK 1210
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVR 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
995-1209 |
8.13e-51 |
|
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: 178.94 E-value: 8.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDRYNEYSDDE-VMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKAR 1153
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
70-359 |
8.21e-51 |
|
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: 181.50 E-value: 8.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 70 PAYIWYLASSVLALLSPVFVNRFIGTIS-AGVTAETLPTALIYGVALGLCG--FLSGLCMQHYFFNSLK-AYQVTTnILN 145
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEdAYLGGPPPSIGYGIGYAIGLFLlqLLSSLLLNHFFYRSMLtGAQVRA-ALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 146 ERLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLT 225
Cdd:cd18597 80 KAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 226 NYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRL--AKAEVVS-SLGYLAVS 302
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLqiLRSILTAvAFSLPVLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 303 TLVLFVALAVHawrGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18597 240 SMLSFITYYAT---GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
677-1202 |
4.48e-50 |
|
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: 186.34 E-value: 4.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 677 PLILATLLLGATAATLLPLAQkAWLSYYSGHQTEWVALTAIGIYGLIGVLVLVGSLLNHLFWL-----DR-GIRAGKNMH 750
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQ-AWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLqeraaARaAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 751 DKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCalqVIVSIVLILGLMP------LMVFVIAPVM 824
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLA---VIVPLAILAAVFPqdwisgLILLLTAPLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 825 ALYYVLQrDYRRPAREVKRFDSVARSPryAHFKESLQGLVVIRSFNKGPWFMqnfyAKLSHSNRMFYSHVM-INR--WFS 901
Cdd:TIGR02857 158 PIFMILI-GWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQA----AAIRRSSEEYRERTMrVLRiaFLS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 902 SRIPLVGGLISMA-TAVGVSLSAYYGVMDAGTAGLVTLYSLSFWGFL-NWGVRIFADIESRMTSIERLKFFSNLPGEVSV 979
Cdd:TIGR02857 231 SAVLELFATLSVAlVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLrQLGAQYHARADGVAAAEALFAVLDAAPRPLAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 980 LKPLPeplrptWPEFGEISVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG 1059
Cdd:TIGR02857 311 KAPVT------AAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1060 VNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRY-NEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQ 1138
Cdd:TIGR02857 384 VPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLArPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQ 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1139 RQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIV 1202
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
997-1209 |
1.18e-48 |
|
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: 173.44 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMGTIRNNLDRYNEYSD-DEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVI 1155
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1156 VMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
383-588 |
1.43e-48 |
|
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: 170.26 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG---RPRMAY 455
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdgvdLRDLDLeslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEAYIVNTSLLENLqfgeevskeelrralhnsclsrdlkewsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVL 535
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 536 LDDPLSAVDADTENLLCERlIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGR 588
Cdd:cd03228 120 LDEATSALDPETEALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
147-572 |
3.88e-48 |
|
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: 180.63 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 147 RLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSD------FPMVFGDLISASFliIGVVAMLFYYIGWSALAALAVLFI 220
Cdd:TIGR02868 91 RVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlyvrviVPAGVALVVGAAA--VAAIAVLSVPAALILAAGLLLAGF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 221 LAPLTNYVAKKFTHLDEEMM-EHRDRRVTLMTQAMNAIRVvkYFAWEKSVAKevTEVREKELTS-RRRLAKAEVVSSLGY 298
Cdd:TIGR02868 169 VAPLVSLRAARAAEQALARLrGELAAQLTDALDGAAELVA--SGALPAALAQ--VEEADRELTRaERRAAAATALGAALT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 299 LAV--STLVLFVALAVHAWRGEKLD----AAVIFTCISLFGllegPFGDLSRLISRATNAKVGARRILDYL----NEDEV 368
Cdd:TIGR02868 245 LLAagLAVLGALWAGGPAVADGRLApvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLdaagPVAEG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 369 EISTEERTDGAAVGLQMQHFSLRHDGAvSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREG-------SL 441
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevtldgvPV 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 442 QFVPEMPGRPRMAYVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQR 520
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLArPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQR 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 499478341 521 VALARAFLRKPQIVLLDDPLSAVDADTENLLCERLiFGAWKDVTRIVVTHRL 572
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
73-359 |
4.80e-48 |
|
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: 173.12 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 73 IWYLASSVLALLSPVFVNRFIGTISAGVTAETlpTALIYGVALGLCGFLSGLCMQHYFFN----SLKAYQVTTNILnerl 148
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLS--DGYLYALGLVLSSLLGALLSSHYNFQmnkvSLKVRAALVTAV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 149 FKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYV 228
Cdd:cd18598 78 YRKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 229 AKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTS--RRRLAKAEVVsslgYL--AVSTL 304
Cdd:cd18598 158 AKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKAlkGRKYLDALCV----YFwaTTPVL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 305 VLFVALAVHAWRGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18598 234 ISILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
711-1210 |
5.13e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 178.67 E-value: 5.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 711 WVALTAIGIYGLIGVLVLVGSLLnhLFWLdrgirAGK---NMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDvy 787
Cdd:PRK11176 66 WMPLVVIGLMILRGITSFISSYC--ISWV-----SGKvvmTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVA-- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 788 lqwsfdSAVHCALQVIV----SIVLILGLM-------PLMVFVIAPVMALYyvlqrdyrrpAREV-KRFDSVARSPR--- 852
Cdd:PRK11176 137 ------SSSSGALITVVregaSIIGLFIMMfyyswqlSLILIVIAPIVSIA----------IRVVsKRFRNISKNMQntm 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 853 ---YAHFKESLQGLVVIRSFNkGPWFMQNFYAKLShsNRM-FYSHVMINrwfSSRI--PLVGGLISMATAVGVSLSAYYG 926
Cdd:PRK11176 201 gqvTTSAEQMLKGHKEVLIFG-GQEVETKRFDKVS--NRMrQQGMKMVS---ASSIsdPIIQLIASLALAFVLYAASFPS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 927 VMDAGTAGLVTLYSLSFWGF---LNWGVRIFADIESRMTSIERLKFFSNLPGEVSVLKPLPEPLRptwpefGEISVEGLK 1003
Cdd:PRK11176 275 VMDTLTAGTITVVFSSMIALmrpLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIERAK------GDIEFRNVT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1004 VRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTL 1083
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1084 FMGTIRNNL--DRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEAT 1161
Cdd:PRK11176 429 FNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499478341 1162 ASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVK 1210
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
631-1209 |
1.54e-46 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 179.53 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 631 AASINTELEAKTTRVTEDEDREVGAvkGSVYWDYISSLGGDGKFtkpLILATLLL--GATAATLLPlaqkawlsYYSGHQ 708
Cdd:TIGR00958 121 AAALWAVLSSAGASEKEAEQGQSET--ADLLFRLLGLSGRDWPW---LISAFVFLtlSSLGEMFIP--------FYTGRV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 709 TEWV-------ALT-AIGIYGLIGVL------VLVGSLLNHLFWLDRGIRAgknmhdKMLKSVLSSPVRFFDSTPVGRII 774
Cdd:TIGR00958 188 IDTLggdkgppALAsAIFFMCLLSIAssvsagLRGGSFNYTMARINLRIRE------DLFRSLLRQDLGFFDENKTGELT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 775 QRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFV----IAPVMALYYVLQRDYRRPAREVKrfDSVARS 850
Cdd:TIGR00958 262 SRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVtlinLPLVFLAEKVFGKRYQLLSEELQ--EAVAKA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 851 PRYAhfKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSsripLVGGLISMATAVGVslsAYYGV--- 927
Cdd:TIGR00958 340 NQVA--EEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYL----WTTSVLGMLIQVLV---LYYGGqlv 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 928 ----MDAGtaGLVT--LYSLSFWGFLNWGVRIFADIESRMTSIERLkfFSNLPGEVSVlkPLPEPLRPTWPEfGEISVEG 1001
Cdd:TIGR00958 411 ltgkVSSG--NLVSflLYQEQLGEAVRVLSYVYSGMMQAVGASEKV--FEYLDRKPNI--PLTGTLAPLNLE-GLIEFQD 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1002 LKVRYASHlP--QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVntasvPLEK-----LRRSL 1074
Cdd:TIGR00958 484 VSFSYPNR-PdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-----PLVQydhhyLHRQV 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDR-YNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKAR 1153
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYgLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1154 VIVMDEATASVDVQTDALLQKviRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
672-1192 |
3.28e-46 |
|
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: 175.24 E-value: 3.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 672 GKFTKPLILATLLLGATAAtLLPLAqkAWLSYYSGHQTE----WVALTAIGIYGLI-GVLVLVGSLLNHLFWLDRGIRAG 746
Cdd:TIGR02868 13 RRLALAVLLGALALGSAVA-LLGVS--AWLISRAAEMPPvlylSVAAVAVRAFGIGrAVFRYLERLVGHDAALRSLGALR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 747 KNMHDKMLKSVLSSPVRFfdstPVGRIIQRFSRDVESV-DVYLQWSFDSAVhcALQVIVSIV-----------LILGLMP 814
Cdd:TIGR02868 90 VRVYERLARQALAGRRRL----RRGDLLGRLGADVDALqDLYVRVIVPAGV--ALVVGAAAVaaiavlsvpaaLILAAGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 815 LMVFVIAPVMALyyvlqRDYRRPAREVKRfdsvARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHV 894
Cdd:TIGR02868 164 LLAGFVAPLVSL-----RAARAAEQALAR----LRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 895 MINRWFSSRIPLVGGL-ISMATAVGVSLSAYyGVMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERLKFFSNL 973
Cdd:TIGR02868 235 AATALGAALTLLAAGLaVLGALWAGGPAVAD-GRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 974 PGEVS-VLKPLPEPLRPTWPEfgeISVEGLKVRYASHlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEE 1052
Cdd:TIGR02868 314 AGPVAeGSAPAAGAVGLGKPT---LELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1053 GSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRYN-EYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGG 1131
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1132 LNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRL 1192
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
383-594 |
1.05e-44 |
|
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: 161.12 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGS-------LQFVPEMPGRPRMAY 455
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSilidgvdISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEAYIVNTSLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVL 535
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 536 LDDPLSAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGT 594
Cdd:cd03244 163 LDEATASVDPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
386-600 |
1.45e-44 |
|
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: 161.24 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 386 QHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqfvpEMPG-----------RPRMA 454
Cdd:cd03251 4 KNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI----LIDGhdvrdytlaslRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 455 YVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQI 533
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 534 VLLDDPLSAVDADTENLL---CERLIfgawKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVK 600
Cdd:cd03251 160 LILDEATSALDTESERLVqaaLERLM----KNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
679-1209 |
5.10e-44 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 171.29 E-value: 5.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 679 ILATLLLGATAATLLPLAqkawlsyysghqTEWVALTAI--GIYGLIGVLVL---VGSLLNHLFWLDRGI-------RAG 746
Cdd:TIGR03797 141 ILAMGLLGTLLGMLVPIA------------TGILIGTAIpdADRSLLVQIALallAAAVGAAAFQLAQSLavlrletRMD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 747 KNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFS-----RDVESVDVY--LQWSFDSAVHCALQVIVSIVLILGLMpLMVFV 819
Cdd:TIGR03797 209 ASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMgisqiRRILSGSTLttLLSGIFALLNLGLMFYYSWKLALVAV-ALALV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 820 IAPVMALYYVLQRDYRRPAREVKrfdsvarspryahfkESLQGLVV--IRSFNK-------GPWFMqnFYAKL-SHSNRM 889
Cdd:TIGR03797 288 AIAVTLVLGLLQVRKERRLLELS---------------GKISGLTVqlINGISKlrvagaeNRAFA--RWAKLfSRQRKL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 890 FYSHVMINRW---FSSRIPLVGGL------ISMATAVGVSLSAYYGVMDAGTAGLVTLYSLSfwgflnwgvRIFADIESR 960
Cdd:TIGR03797 351 ELSAQRIENLltvFNAVLPVLTSAalfaaaISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLS---------NTLISILAV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 961 MTSIERLK-FFSNLPgEVSVLKPLPEPLRptwpefGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKST 1039
Cdd:TIGR03797 422 IPLWERAKpILEALP-EVDEAKTDPGKLS------GAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1040 FFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQSL 1119
Cdd:TIGR03797 495 LLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAM 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1120 PDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTdallQKVIRTSFAG--VTMLIIAHRLGTIAD 1197
Cdd:TIGR03797 575 PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLERlkVTRIVIAHRLSTIRN 650
|
570
....*....|..
gi 499478341 1198 CDQIVEISAGEV 1209
Cdd:TIGR03797 651 ADRIYVLDAGRV 662
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
676-1209 |
8.57e-44 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 169.13 E-value: 8.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 676 KPLILATLLLGATAATllPLAQKAWLSYY-----SGHQTEWVALTAIGIyGLIGVLVLVGSLlnHLFWLDRGIRAG---- 746
Cdd:PRK10790 23 KPLGLAVLMLWVAAAA--EVSGPLLISYFidnmvAKGNLPLGLVAGLAA-AYVGLQLLAAGL--HYAQSLLFNRAAvgvv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 747 KNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESV-DVYlqwsfdsaVHCALQVIVSIVLI-------------LGL 812
Cdd:PRK10790 98 QQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIrDLY--------VTVVATVLRSAALIgamlvamfsldwrMAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 813 MPLMVF-VIAPVMALYyvlQRdYRRP-AREVKRF-----DSvarspryahFKESLQGLVVIRSFNKgpwfMQNFYAKLSH 885
Cdd:PRK10790 170 VAIMIFpAVLVVMVIY---QR-YSTPiVRRVRAYladinDG---------FNEVINGMSVIQQFRQ----QARFGERMGE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 886 SNRmfySHVMiNRWFSSRIP--LVGGLISMATA-VGVSLSAYYGVMDAGTAGLVTLYS-LSFWGFLN------------- 948
Cdd:PRK10790 233 ASR---SHYM-ARMQTLRLDgfLLRPLLSLFSAlILCGLLMLFGFSASGTIEVGVLYAfISYLGRLNeplielttqqsml 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 949 -----WGVRIFADIESRMTSIerlkffsnlpGEVSvlKPLpeplrptwpEFGEISVEGLKVRYASHLPqVLKGITFKVEA 1023
Cdd:PRK10790 309 qqavvAGERVFELMDGPRQQY----------GNDD--RPL---------QSGRIDIDNVSFAYRDDNL-VLQNINLSVPS 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1024 GSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRYNEYSDDEV 1103
Cdd:PRK10790 367 RGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1104 MGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGV 1183
Cdd:PRK10790 447 WQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT 526
|
570 580
....*....|....*....|....*.
gi 499478341 1184 TMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:PRK10790 527 TLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
398-611 |
1.71e-42 |
|
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: 155.47 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPEMPGRPRMAYVPQEAYIVNTSLLEN 470
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdireVTLDSLRRAIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 471 LQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTen 549
Cdd:cd03253 95 IRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 550 llcERLIFGAWKDV----TRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPFAEFYKE 611
Cdd:cd03253 173 ---EREIQAALRDVskgrTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
356-611 |
2.91e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 164.25 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 356 ARRILDYLNEDEVEISTEERT--DGAAVGLQMQHFS-LRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG 432
Cdd:PRK11174 321 AESLVTFLETPLAHPQQGEKElaSNDPVTIEAEDLEiLSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 433 eVAPREGSLQF-------VPEMPGRPRMAYVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRT 504
Cdd:PRK11174 399 -FLPYQGSLKIngielreLDPESWRKHLSWVGQNPQLPHGTLRDNVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDT 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 505 EIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIfGAWKDVTRIVVTHRLEHLAQFDQVIYI 584
Cdd:PRK11174 478 PIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN-AASRRQTTLMVTHQLEDLAQWDQIWVM 556
|
250 260
....*....|....*....|....*..
gi 499478341 585 QHGRVQGQGTFSELVKTCAPFAEFYKE 611
Cdd:PRK11174 557 QDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1011-1209 |
3.88e-42 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 163.98 E-value: 3.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1011 PQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRN 1090
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1091 NLDRYNE-YSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTD 1169
Cdd:PRK13657 428 NIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499478341 1170 ALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:PRK13657 508 AKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
399-600 |
1.14e-41 |
|
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: 152.76 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqFVPEMPG--------RPRMAYVPQEAYIVNTSLLEN 470
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGIDIrdisrkslRSMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 471 LQFGEEVSKEE----LRRALHNSCLSRDLKEwsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDAD 546
Cdd:cd03254 97 IRLGRPNATDEevieAAKEAGAHDFIMKLPN---GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 547 TENLL---CERLIfgawKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVK 600
Cdd:cd03254 174 TEKLIqeaLEKLM----KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
399-610 |
1.85e-41 |
|
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: 152.69 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF---------VPEMpgRPRMAYVPQEAYIVNTSLLE 469
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgvdirdlnLRWL--RSQIGLVSQEPVLFDGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTE 548
Cdd:cd03249 96 NIRYGkPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 549 NLLCERLIfGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPFAEFYK 610
Cdd:cd03249 176 KLVQEALD-RAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
60-598 |
3.05e-41 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 163.35 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 60 LIRALRdFTRPAYIWYLASSVLALLS-------PVFVNRFIGTISAGVTAETLPTAL----IYGVALGLCGFLSGLCMQH 128
Cdd:TIGR00958 149 LFRLLG-LSGRDWPWLISAFVFLTLSslgemfiPFYTGRVIDTLGGDKGPPALASAIffmcLLSIASSVSAGLRGGSFNY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 129 yffnslkAYQVTTNILNERLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSD-FPMVFGDLISAsfLIIGVVAMLFYYI 207
Cdd:TIGR00958 228 -------TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRsLSLNVNVLLRN--LVMLLGLLGFMLW 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 208 GWSALAAlaVLFILAPLTNYVAKKFT----HLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKsvaKEVTEVREKeLTS 283
Cdd:TIGR00958 299 LSPRLTM--VTLINLPLVFLAEKVFGkryqLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEE---GEASRFKEA-LEE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 284 RRRLAKAEVVSSLGYLAVSTLV-LFVALAVHAWRGEK-LDAAVIFTCISLFGLLEGPFGD----LSRLISRATNAKVGAR 357
Cdd:TIGR00958 373 TLQLNKRKALAYAGYLWTTSVLgMLIQVLVLYYGGQLvLTGKVSSGNLVSFLLYQEQLGEavrvLSYVYSGMMQAVGASE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 358 RILDYLN-EDEVEISTEERTDGAAVGLQMQHFSL----RHDgavSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG 432
Cdd:TIGR00958 453 KVFEYLDrKPNIPLTGTLAPLNLEGLIEFQDVSFsypnRPD---VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 433 EVAPREGSLQfvpeMPGRP-----------RMAYVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSG 500
Cdd:TIGR00958 530 LYQPTGGQVL----LDGVPlvqydhhylhrQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPN 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 501 GLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLifgAWKDVTRIVVTHRLEHLAQFDQ 580
Cdd:TIGR00958 606 GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESR---SRASRTVLLIAHRLSTVERADQ 682
|
570
....*....|....*...
gi 499478341 581 VIYIQHGRVQGQGTFSEL 598
Cdd:TIGR00958 683 ILVLKKGSVVEMGTHKQL 700
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
995-1209 |
7.66e-41 |
|
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: 162.04 E-value: 7.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:TIGR03796 476 GYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSV 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDRYNE-YSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKAR 1153
Cdd:TIGR03796 556 AMVDQDIFLFEGTVRDNLTLWDPtIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPS 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRTSfaGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:TIGR03796 636 ILILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKV 689
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
371-582 |
9.05e-41 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 158.99 E-value: 9.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 371 STEERTDGAAVGLQMQHFSLRHDGAvSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGS-------LQF 443
Cdd:TIGR02857 310 GKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 444 VPEMPGRPRMAYVPQEAYIVNTSLLENLQFGE-EVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVA 522
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 523 LARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFGAwKDVTRIVVTHRLEHLAQFDQVI 582
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALADRIV 527
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
965-1210 |
2.32e-40 |
|
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: 158.37 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 965 ERL-KFFSNLPGEVSVLkPLPEPLrptwpefGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQS 1043
Cdd:COG4618 306 RRLnELLAAVPAEPERM-PLPRPK-------GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1044 LFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGM 1123
Cdd:COG4618 378 LVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1124 NSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTIADCDQIV 1202
Cdd:COG4618 458 DTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAVDKLL 537
|
....*...
gi 499478341 1203 EISAGEVK 1210
Cdd:COG4618 538 VLRDGRVQ 545
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
189-609 |
7.04e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 156.91 E-value: 7.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 189 LIS---ASFLIIGVVAMLFYYIGWS-AL----AALAVLFILAPLTNYVAKKFThldEEMMEHRDRRVTLMTQAMNAIRVV 260
Cdd:PRK11160 137 LISplvAALVVILVLTIGLSFFDLTlALtlggILLLLLLLLPLLFYRLGKKPG---QDLTHLRAQYRVQLTEWLQGQAEL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 261 KYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVS--TLVLFVALAVHAWRG----EKLDAAVIFT---CISL 331
Cdd:PRK11160 214 TLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANglTVVLMLWLAAGGVGGnaqpGALIALFVFAalaAFEA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 332 FGLLEGPFGDLSRLISratnakvGARRILDYLN-EDEVEISTEERTDGAAVGLQMQHFSLRHDGAVSDVLHDVNVHVPAG 410
Cdd:PRK11160 294 LMPVAGAFQHLGQVIA-------SARRINEITEqKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 411 SSLAIVGPVGAGKSSLLmSLL--------GEVAPREGSLQFVPEMPGRPRMAYVPQEAYIVNTSLLENLQFG-EEVSKEE 481
Cdd:PRK11160 367 EKVALLGRTGCGKSTLL-QLLtrawdpqqGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAaPNASDEA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 482 LRRALHNSCLSrDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCErLIFGAWK 561
Cdd:PRK11160 446 LIEVLQQVGLE-KLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILE-LLAEHAQ 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 499478341 562 DVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPFAEFY 609
Cdd:PRK11160 524 NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
141-609 |
7.68e-40 |
|
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: 158.75 E-value: 7.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 141 TNILNERL--------FKHSLKLSQKSRQKNQVGDIVNHMSSDSDNV----SDFPMVFGDL--ISASFLIIGVVAMLFYY 206
Cdd:TIGR01193 220 LNVLGQRLsidiilsyIKHLFELPMSFFSTRRTGEIVSRFTDASSIIdalaSTILSLFLDMwiLVIVGLFLVRQNMLLFL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 207 IGWSALAALAVLFILapltnyVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRR 286
Cdd:TIGR01193 300 LSLLSIPVYAVIIIL------FKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFK 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 287 LAKAEVVSSLgYLAVSTLVLFValaVHAWRG------EKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRIL 360
Cdd:TIGR01193 374 YQKADQGQQA-IKAVTKLILNV---VILWTGaylvmrGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 361 D-YLNEDEVEISTEERTDGAAVG-LQMQHFSLRHdGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPRE 438
Cdd:TIGR01193 450 EvYLVDSEFINKKKRTELNNLNGdIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 439 GSLQFVPEMPG-------RPRMAYVPQEAYIVNTSLLENLQFG--EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEK 509
Cdd:TIGR01193 529 GEILLNGFSLKdidrhtlRQFINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 510 GVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFgaWKDVTRIVVTHRLEHLAQFDQVIYIQHGRV 589
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
490 500
....*....|....*....|
gi 499478341 590 QGQGTFSELVKTCAPFAEFY 609
Cdd:TIGR01193 687 IEQGSHDELLDRNGFYASLI 706
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
383-589 |
1.51e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.16 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VPEMPGRPRMAYVPQEA 460
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgKPPRRARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 461 YI-----------VNTSLLENLQFGEEVSKEELRRALHnsCLSR----DLKewsgglRTEIGEkgvnLSGGQKQRVALAR 525
Cdd:COG1121 85 EVdwdfpitvrdvVLMGRYGRRGLFRRPSRADREAVDE--ALERvgleDLA------DRPIGE----LSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 526 AFLRKPQIVLLDDPLSAVDADTENLLCErlIFGAWKD--VTRIVVTHRLEHLAQ-FDQVIYIQHGRV 589
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRRegKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
996-1209 |
1.62e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 153.08 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 996 EISVEGLKVRyaSHLPQVLKG-ITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIeAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:PRK11174 349 TIEAEDLEIL--SPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDRYN-EYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKAR 1153
Cdd:PRK11174 426 SWVGQNPQLPHGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
389-593 |
4.11e-38 |
|
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: 142.34 E-value: 4.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 389 SLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPEMPGRPRMAYVPQEAY 461
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqLDPADLRRNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 462 IVNTSLLENLQFGE-EVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPL 540
Cdd:cd03245 89 LFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 541 SAVDADTENLLCERLifGAW-KDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQG 593
Cdd:cd03245 169 SAMDMNSEERLKERL--RQLlGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
997-1209 |
5.13e-38 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 140.43 E-value: 5.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMGTIRNNLdryneysddevmgalkhasmwdyvqslpdgmnsavsegglnLSQGQRQLLCLARALLTKARVIV 1156
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1157 MDEATASVDVQTDALLQKVI-RTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
86-335 |
1.09e-37 |
|
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: 143.54 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 86 PVFVNRFIGTISAGVTAETLpTALIYGVALGLCGFLSGLCMQHYFFNSLKA-YQV---TTNILnerlFKHSLKLSQKSRQ 161
Cdd:cd18594 17 PLLLGRLVAYFVPDSTVTKT-EAYLYALGLSLCAFLRVLLHHPYFFGLHRYgMQLriaLSSLI----YKKTLKLSSSALS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 162 KNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVAKKFTHLDEEMME 241
Cdd:cd18594 92 KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 242 HRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVLFVALAVHAWRGEKLD 321
Cdd:cd18594 172 LTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLT 251
|
250
....*....|....
gi 499478341 322 AAVIFTCISLFGLL 335
Cdd:cd18594 252 ARKVFTVISLLNAL 265
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
83-332 |
1.41e-37 |
|
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: 143.13 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 83 LLSPVFVNRFIGTISAGVTAETLPTALIYGVALGLCGFLSGLCMQHYFFNSLKA---YQVTTNILnerLFKHSLKLSQKS 159
Cdd:cd18593 14 VVQPIFLGKLIRYFEGNGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIgmrLRVACSSL---IYRKALRLSQAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 160 RQKNQVGDIVNHMSSDsdnVSDFPMVFgdlISASFLIIG------VVAMLFYYIGWSALAALAVLFILAPLTNYVAKKFT 233
Cdd:cd18593 91 LGKTTVGQIVNLLSND---VNRFDQAV---LFLHYLWVAplqliaVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 234 HLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRR--LAKAEVVSSlgYLAVSTLVLFVALA 311
Cdd:cd18593 165 KLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRtsFLRALNMGL--FFVSSKLILFLTFL 242
|
250 260
....*....|....*....|.
gi 499478341 312 VHAWRGEKLDAAVIFTCISLF 332
Cdd:cd18593 243 AYILLGNILTAERVFVTMALY 263
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
997-1226 |
2.01e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 137.85 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPT--LFMGTIRN-------NLDRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARA 1147
Cdd:COG1122 80 VFQNPDdqLFAPTVEEdvafgpeNLGLPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1148 LLTKARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTE-FSQEEIE 1224
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREvFSDYELL 228
|
..
gi 499478341 1225 ES 1226
Cdd:COG1122 229 EE 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1012-1209 |
3.06e-36 |
|
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: 137.22 E-value: 3.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNN 1091
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1092 LDrYN--EYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTD 1169
Cdd:cd03248 108 IA-YGlqSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499478341 1170 ALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:cd03248 187 QQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
400-587 |
4.28e-36 |
|
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: 136.31 E-value: 4.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRPR-----------MAYVPQEAYIVNTSLL 468
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfeatrsrnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 469 ENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTE 548
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499478341 549 NLLCERLIFGAWKDVTR--IVVTHRLEHLAQFDQVIYIQHG 587
Cdd:cd03290 177 DHLMQEGILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
382-598 |
6.50e-36 |
|
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: 138.07 E-value: 6.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 382 GLQMQHFSLRhdgaVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpempgRPRMAYVPQEAY 461
Cdd:cd03291 39 NLFFSNLCLV----GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH------SGRISFSSQFSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 462 IVNTSLLENLQFGeeVSKEELR-RALHNSC-LSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:cd03291 109 IMPGTIKENIIFG--VSYDEYRyKSVVKACqLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 540 LSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:cd03291 187 FGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
997-1209 |
2.77e-35 |
|
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: 134.23 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE-----EGSISIDG--VNTASVPLEK 1069
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGkdIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 LRRSLAIIPQDPTLFMGTIRNNLD--------RYNEYSDDEVMGALKHASMWDYVQSLPDGmnsavseggLNLSQGQRQL 1141
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHA---------LGLSGGQQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1142 LCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADC-DQIVEISAGEV 1209
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRL 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
383-589 |
3.86e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.40 E-value: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG---RPRMAY 455
Cdd:COG4619 1 LELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdgkpLSAMPPpewRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEAYIVNTSLLENLQF-----GEEVSKEELRRALHNSCLSRDLKEWSGGlrteigekgvNLSGGQKQRVALARAFLRK 530
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDILDKPVE----------RLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 531 PQIVLLDDPLSAVDADTENLLcERLI--FGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRV 589
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRV-EELLreYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1014-1162 |
2.43e-34 |
|
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: 128.92 E-value: 2.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1014 LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMG-TIRNNL 1092
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1093 -------DRYNEYSDDEVMGALKHASMWDYvqslpdgMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATA 1162
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
76-339 |
3.04e-34 |
|
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: 132.77 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGVTAETLPTAlIYGVALGLCGFLSGLCMQHYFFNSLKAYQVTTNILNERLFKHSLKL 155
Cdd:pfam00664 9 ILSGAISPAFPLVLGRILDVLLPDGDPETQALN-VYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 156 SQKSRQKNQVGDIVNHMSSDSDNVSDF-PMVFGDLISASFLIIGVVAMLFYYiGWS-ALAALAVLFILAPLTNYVAKKFT 233
Cdd:pfam00664 88 PMSFFDTNSVGELLSRLTNDTSKIRDGlGEKLGLLFQSLATIVGGIIVMFYY-GWKlTLVLLAVLPLYILVSAVFAKILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 234 HLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVLFVALAVH 313
Cdd:pfam00664 167 KLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFG 246
|
250 260
....*....|....*....|....*....
gi 499478341 314 AW---RGEkLDAAVIFTCISLFGLLEGPF 339
Cdd:pfam00664 247 AYlviSGE-LSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
998-1208 |
4.20e-34 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 130.28 E-value: 4.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 998 SVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAII 1077
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1078 PQDPT--LFMGTIR-------NNLDRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARAL 1148
Cdd:cd03225 81 FQNPDdqFFGPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1149 LTKARVIVMDEATASVDVQ-TDALLQKVIRTSFAGVTMLIIAHRLGTIAD-CDQIVEISAGE 1208
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAgRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
997-1227 |
4.79e-34 |
|
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: 131.52 E-value: 4.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYAShlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEkLRRSLAI 1076
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMG-TIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEgglnLSQGQRQLLCLARALLTKARVI 1155
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1156 VMDEATASVDVQTDALLQKVIRtSFA--GVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQEEIEESL 1227
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILR-ALKkeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
997-1209 |
4.89e-34 |
|
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: 128.67 E-value: 4.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPlEKLRRSLAI 1076
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFmgtirnnldryneysddevmgalKHASMWDYvqslpdgmnsavseggLNLSQGQRQLLCLARALLTKARVIV 1156
Cdd:cd03230 78 LPEEPSLY-----------------------ENLTVREN----------------LKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1157 MDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
110-359 |
8.29e-34 |
|
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: 132.74 E-value: 8.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 110 IYGVALGLCGFLSGLCMQHYFF-------NSLKAYQVTtnilnerLFKHSLKLS--QKSRQKNQVGDIVNHMSSDSDNVS 180
Cdd:cd18591 57 VLAVILFLALLLQATFSQASYHiviregiRLKTALQAM-------IYEKALRLSswNLSSGSMTIGQITNHMSEDANNIM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 181 DFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVV 260
Cdd:cd18591 130 FFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 261 KYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVLFVALAVHAWRGEK-LDAAVIFTCISLFGLLEGPF 339
Cdd:cd18591 210 KLYAWENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPL 289
|
250 260
....*....|....*....|
gi 499478341 340 GDLSRLISRATNAKVGARRI 359
Cdd:cd18591 290 FIFPVVIPILINAVVSTRRL 309
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
384-584 |
8.50e-34 |
|
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: 129.58 E-value: 8.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 384 QMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGS--LQFVPEMPGRPRMAYVPQEAY 461
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSirVFGKPLEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 462 I-----------VNTSLLENLQFGEEVSKEELRRALHnsCLSR----DLKEwsgglRTeIGEkgvnLSGGQKQRVALARA 526
Cdd:cd03235 79 IdrdfpisvrdvVLMGLYGHKGLFRRLSKADKAKVDE--ALERvglsELAD-----RQ-IGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 527 FLRKPQIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEH-LAQFDQVIYI 584
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLvLEYFDRVLLL 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
78-610 |
1.05e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 138.23 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 78 SSVLALLSPVFVNRFiGTISAGVTaETLPTALIyGVAL--GLCGFLSGLCMqhyffnSLKAYQVTTNIlNERLFKHSLKL 155
Cdd:PRK11176 42 TFMLSLLKPLLDDGF-GKADRSVL-KWMPLVVI-GLMIlrGITSFISSYCI------SWVSGKVVMTM-RRRLFGHMMGM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 156 SQKSRQKNQVGDIVNHMSSDSDNVSDFPMvfGDLIS-----ASflIIGVVAMLFYYiGWSaLAAlaVLFILAP----LTN 226
Cdd:PRK11176 112 PVSFFDKQSTGTLLSRITYDSEQVASSSS--GALITvvregAS--IIGLFIMMFYY-SWQ-LSL--ILIVIAPivsiAIR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 227 YVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAweksvAKEVTEVREKELTSRRRLAKAEVVSSLG-------YL 299
Cdd:PRK11176 184 VVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFG-----GQEVETKRFDKVSNRMRQQGMKMVSASSisdpiiqLI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 300 AVSTLVLFVALAVHAWRGEKLDA---AVIFTciSLFGLLEgPFGDLSRLIS---RATNAKVGARRILDYLNEDEVEISTE 373
Cdd:PRK11176 259 ASLALAFVLYAASFPSVMDTLTAgtiTVVFS--SMIALMR-PLKSLTNVNAqfqRGMAACQTLFAILDLEQEKDEGKRVI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 374 ERTDGAavgLQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKS---SLLMS---------LLGEVAPREGSL 441
Cdd:PRK11176 336 ERAKGD---IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKStiaNLLTRfydidegeiLLDGHDLRDYTL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 442 QFVpempgRPRMAYVPQEAYIVNTSLLENLQF--GEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQ 519
Cdd:PRK11176 413 ASL-----RNQVALVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 520 RVALARAFLRKPQIVLLDDPLSAVdaDTENllcERLIFGAW----KDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTF 595
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSAL--DTES---ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTH 562
|
570
....*....|....*
gi 499478341 596 SELVKTCAPFAEFYK 610
Cdd:PRK11176 563 AELLAQNGVYAQLHK 577
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
997-1209 |
3.25e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 127.62 E-value: 3.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMGTIRNNLDRYNEYSDDEvmgaLKHASMWDYVQSL---PDGMNSAVSEgglnLSQGQRQLLCLARALLTKAR 1153
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERK----FDRERALELLERLglpPDILDKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
300-629 |
7.25e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 135.86 E-value: 7.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 300 AVSTLVLFVALAVHAWRGEKLDAAV--IFTCISLFGLLegpFGDLSRLISRATNAKVGARRILDYLN-EDEVEiSTEERT 376
Cdd:PRK13657 248 AASTITMLAILVLGAALVQKGQLRVgeVVAFVGFATLL---IGRLDQVVAFINQVFMAAPKLEEFFEvEDAVP-DVRDPP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 377 DGAAVG-----LQMQHFSLRHDGAvSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLmSLLGEV-APREGSLQF------- 443
Cdd:PRK13657 324 GAIDLGrvkgaVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVfDPQSGRILIdgtdirt 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 444 VPEMPGRPRMAYVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVA 522
Cdd:PRK13657 402 VTRASLRRNIAVVFQDAGLFNRSIEDNIRVGrPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLA 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 523 LARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTC 602
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARG 560
|
330 340
....*....|....*....|....*..
gi 499478341 603 APFAEFYKEHGKTQGEGHEVRPAETAQ 629
Cdd:PRK13657 561 GRFAALLRAQGMLQEDERRKQPAAEGA 587
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
383-589 |
8.03e-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: 125.41 E-value: 8.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGS-------LQFVPEMPGRPRMAY 455
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRvrldgadISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEAYIVNTSLLENLqfgeevskeelrralhnsclsrdlkewsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVL 535
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 536 LDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRV 589
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
998-1208 |
1.43e-32 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 123.89 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 998 SVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAII 1077
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1078 PQdptlfmgtirnnldryneysddevmgalkhasmwdyvqslpdgmnsavsegglnLSQGQRQLLCLARALLTKARVIVM 1157
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1158 DEATASVDVQTDALLQKVIRTSFA-GVTMLIIAHRLGTIAD-CDQIVEISAGE 1208
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
995-1209 |
2.52e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 134.18 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMGTIRNNLDRYNEYSDDEVM-GALKHASMWDYVQSlPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKAR 1153
Cdd:PRK11160 417 SVVSQRVHLFSATLRDNLLLAAPNASDEALiEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
997-1225 |
4.87e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.59 E-value: 4.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVntasvPLEKLRRSLAI 1076
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTL---F---------MGTIRNN--LDRYNEYSDDEVMGALKHASMWDYvqslpdgMNSAVSEgglnLSQGQRQLL 1142
Cdd:COG1121 80 VPQRAEVdwdFpitvrdvvlMGRYGRRglFRRPSRADREAVDEALERVGLEDL-------ADRPIGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1143 CLARALLTKARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQ 1220
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHGPPEEVLTP 228
|
....*
gi 499478341 1221 EEIEE 1225
Cdd:COG1121 229 ENLSR 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
383-593 |
5.61e-32 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 123.19 E-value: 5.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPG------RPRMAYV 456
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlekalSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQEAYIVNTSLLENLqfgeevskeelrralhnsclsrdlkewsgglrteigekGVNLSGGQKQRVALARAFLRKPQIVLL 536
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 537 DDPLSAVDADTENLLCErLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQG 593
Cdd:cd03247 123 DEPTVGLDPITERQLLS-LIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
399-598 |
1.15e-31 |
|
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: 132.25 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPEMPGRPRMAYVPQEAYIVNTSLLENL 471
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdgqdirdVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 QFG-EEVSKEELRRALHNSCLS---RDLKEwsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADT 547
Cdd:COG5265 453 AYGrPDASEEEVEAAARAAQIHdfiESLPD---GYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 548 enllcERLIFGAWKDVTR----IVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:COG5265 530 -----ERAIQAALREVARgrttLVIAHRLSTIVDADEILVLEAGRIVERGTHAEL 579
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
86-598 |
2.45e-31 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 131.38 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 86 PVFVNRFIGTIsagVTAETLPTALIYGVA---LGLCGFLSGLcmqHYF----FNSLK---AYQVTTNILNERLFKhslKL 155
Cdd:PRK10790 43 PLLISYFIDNM---VAKGNLPLGLVAGLAaayVGLQLLAAGL---HYAqsllFNRAAvgvVQQLRTDVMDAALRQ---PL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 156 SQKSRQKnqVGDIVNHMSSDSDNVSD-FPMVFGDLISASFLIigvVAML--FYYIGWS-ALAAL----AVLFILA----- 222
Cdd:PRK10790 114 SAFDTQP--VGQLISRVTNDTEVIRDlYVTVVATVLRSAALI---GAMLvaMFSLDWRmALVAImifpAVLVVMViyqry 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 223 --PLTNYVAKKFTHLDEEMMEhrdrrvtlmtqAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEvvsslGYLA 300
Cdd:PRK10790 189 stPIVRRVRAYLADINDGFNE-----------VINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLD-----GFLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 301 VSTLVLFVALAVHAW-------RGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRILDYLNEDEVEISTE 373
Cdd:PRK10790 253 RPLLSLFSALILCGLlmlfgfsASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGND 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 374 ERT-DGAAVGLQMQHFSLRHDgavSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRP- 451
Cdd:PRK10790 333 DRPlQSGRIDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR----LDGRPl 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 452 ----------RMAYVPQEAYIVNTSLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRV 521
Cdd:PRK10790 406 sslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLL 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 522 ALARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAI-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
997-1209 |
6.29e-31 |
|
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: 121.84 E-value: 6.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHL--PQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKLR 1071
Cdd:cd03257 2 LEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLAIIPQDP-----------TLFMGTIRNNLDRYNEYSDDEVMGALKHAsmwdyVQSLPDGMNSAVSEgglnLSQGQRQ 1140
Cdd:cd03257 82 KEIQMVFQDPmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVG-----VGLPEEVLNRYPHE----LSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1141 LLCLARALLTKARVIVMDEATASVDVQTDA----LLQKvIRTSFaGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAqildLLKK-LQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
358-610 |
1.37e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 128.68 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 358 RILDYLNED-EVEISTEERTDGAAVgLQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAP 436
Cdd:PRK10789 289 RIRAMLAEApVVKDGSEPVPEGRGE-LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 437 REGSLQFvPEMP--------GRPRMAYVPQEAYIVNTSLLENLQFGE-EVSKEELRRALHNSCLSRDLKEWSGGLRTEIG 507
Cdd:PRK10789 368 SEGDIRF-HDIPltklqldsWRSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVG 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 508 EKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLifGAW-KDVTRIVVTHRLEHLAQFDQVIYIQH 586
Cdd:PRK10789 447 ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWgEGRTVIISAHRLSALTEASEILVMQH 524
|
250 260
....*....|....*....|....
gi 499478341 587 GRVQGQGTFSELVKTCAPFAEFYK 610
Cdd:PRK10789 525 GHIAQRGNHDQLAQQSGWYRDMYR 548
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
397-589 |
1.53e-30 |
|
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: 120.65 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 397 SDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRPRMAY-----------VPQEAYIVNT 465
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL----LDGKPISQYehkylhskvslVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 SLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:cd03248 103 SLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499478341 545 ADTEnLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRV 589
Cdd:cd03248 183 AESE-QQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
997-1208 |
1.60e-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: 119.88 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYAS---HLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntasvpleklrrS 1073
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPTLFMGTIRNNL---DRYNEYSDDEVMGA--LKHasmwDyVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARAL 1148
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDEERYEKVIKAcaLEP----D-LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1149 LTKARVIVMDEATASVDVQT-DALLQKVIRTSFA-GVTMLIIAHRLGTIADCDQIVEISAGE 1208
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
387-1202 |
1.95e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 130.92 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 387 HFSLRHDgavSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREG--------SLQFVPEMPGRPRMAYVPQ 458
Cdd:PTZ00265 391 HYDTRKD---VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdiiindshNLKDINLKWWRSKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 459 EAYIVNTSLLENLQFG---------------EEVSKEELRRALHNSCLSRDLKEW--------SGGL------------- 502
Cdd:PTZ00265 468 DPLLFSNSIKNNIKYSlyslkdlealsnyynEDGNDSQENKNKRNSCRAKCAGDLndmsnttdSNELiemrknyqtikds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 503 ----------------------RTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERL--IFG 558
Cdd:PTZ00265 548 evvdvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKG 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 559 AWKDVTrIVVTHRLEHLaQFDQVIYIQHGRVQGQGTFSELV--KTCAPFAEFYKEHGKTQGEGHEVRPAETAQEAAS--- 633
Cdd:PTZ00265 628 NENRIT-IIIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIgeDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSyii 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 634 -------------------INTELEAKTTRVTEDEDREvGAVKGSVYWDY------------------------------ 664
Cdd:PTZ00265 706 eqgthdalmknkngiyytmINNQKVSSKKSSNNDNDKD-SDMKSSAYKDSergydpdemngnskhenesasnkksckmsd 784
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 665 --ISSLGGDGKFT--------KP--------------------------LILA-------TLLLGATAATLLPLAQkawL 701
Cdd:PTZ00265 785 enASENNAGGKLPflrnlfkrKPkapnnlrivyreifsykkdvtiialsILVAgglypvfALLYAKYVSTLFDFAN---L 861
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 702 SYYSGHQTEWVALTAIGIYgligvlvlVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDS---TPvGRIIQRFS 778
Cdd:PTZ00265 862 EANSNKYSLYILVIAIAMF--------ISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHIN 932
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 779 RDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLmvfVIAPVMALYYVLQRDYRRPAR-------EVKRF------- 844
Cdd:PTZ00265 933 RDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPI---VAAVLTGTYFIFMRVFAIRARltankdvEKKEInqpgtvf 1009
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 845 -----DSVARSPRYAhFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINrwfssriPLVGGLISMATAVGV 919
Cdd:PTZ00265 1010 aynsdDEIFKDPSFL-IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVN-------SMLWGFSQSAQLFIN 1081
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 920 SLSAYYG--VMDAGTAgLVTLYSLSFWGFLNWG------VRIFADIESRMTSIERLKFFSNLPGEVSVLKPLPEPLRPTW 991
Cdd:PTZ00265 1082 SFAYWFGsfLIRRGTI-LVDDFMKSLFTFLFTGsyagklMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKN 1160
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 992 PEFGEISVEGLKVRYASHlPQV--LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE------------------ 1051
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYISR-PNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtne 1239
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1052 ------------------------------------EGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNLDRY 1095
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG 1319
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1096 NEYSDDE-VMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQK 1174
Cdd:PTZ00265 1320 KEDATREdVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
1050 1060 1070
....*....|....*....|....*....|
gi 499478341 1175 VIR--TSFAGVTMLIIAHRLGTIADCDQIV 1202
Cdd:PTZ00265 1400 TIVdiKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
383-589 |
3.55e-30 |
|
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: 119.05 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPEMPGRPRMAY 455
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdgidistIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEAYIVNTSLLENLQFGEEVSKEELRRALhnsclsrdlkewsgglrtEIGEKGVNLSGGQKQRVALARAFLRKPQIVL 535
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 536 LDDPLSAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRV 589
Cdd:cd03369 149 LDEATASIDYATDALI-QKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
997-1209 |
3.72e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 126.56 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLP---QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKL 1070
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1071 RRSLAIIPQDPT--LF-MGTIRNN----LDRYNEYSDDEVMGALkhASMWDYVQSLPDGMNSAVSEgglnLSQGQRQLLC 1143
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIiaepLRLHGLLSRAERRERV--AELLERVGLPPDLADRYPHE----LSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1144 LARALLTKARVIVMDEATASVDVQTDA----LLQKvIRTSFaGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAqilnLLRD-LQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
399-598 |
1.38e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 118.24 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG--RPRMAYVPQEAYIVNT-SLLENL 471
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedVARDPAevRRRIGYVPQEPALYPDlTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 QF-GE--EVSKEELRRALHnsclsrDLKEWSGgLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTE 548
Cdd:COG1131 95 RFfARlyGLPRKEARERID------ELLELFG-LTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 549 NLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:COG1131 168 RELWELLRELAAEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
75-359 |
2.15e-29 |
|
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: 119.20 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 75 YLASSVLALLSPVFVNRFIgtISagvTAETLPTALIYGVALGLCGFLSGLCmQHYFFNSLKAYQVTTNIlneRL------ 148
Cdd:cd18592 6 LLISLIFGFIGPTILIRKL--LE---YLEDSDSSVWYGILLVLGLFLTELL-RSLFFSLTWAISYRTGI---RLrgavlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 149 --FKHSLKLsqKSRQKNQVGDIVNHMSSDS----DNVSDFPMVFGDLISasfLIIGVVAMLfYYIGWSALAALAVLFILA 222
Cdd:cd18592 77 llYKKILRL--RSLGDKSVGELINIFSNDGqrlfDAAVFGPLVIGGPVV---LILGIVYST-YLLGPWALLGMLVFLLFY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 223 PLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKEltsRRRLAKAEVVSSLGyLAVS 302
Cdd:cd18592 151 PLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEE---RKILEKAGYLQSIS-ISLA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 303 TLVLFVA----LAVHAWRGEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18592 227 PIVPVIAsvvtFLAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
997-1209 |
2.40e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.86 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE---EGSISIDGVNTASVPLEKLRRS 1073
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPT--LFMGTIRNNLdryneysdDEVM--GALKHASMWDYVQSLPD--GMNSAVSEGGLNLSQGQRQLLCLARA 1147
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQI--------AEALenLGLSRAEARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1148 LLTKARVIVMDEATASVDVQTDALLQKVIR--TSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRI 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
383-599 |
2.42e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 118.22 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRP---RMAY 455
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdLASLSRRElarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEAYIV-NTSLLENLQFG--------EEVSKEELR---RALHnsclsrdlkewsgglRTEIG---EKGVN-LSGGQKQ 519
Cdd:COG1120 80 VPQEPPAPfGLTVRELVALGryphlglfGRPSAEDREaveEALE---------------RTGLEhlaDRPVDeLSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 520 RVALARAFLRKPQIVLLDDPLSAVD----ADTENLLcERLIfgAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGT 594
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELL-RRLA--RERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGP 221
|
....*
gi 499478341 595 FSELV 599
Cdd:COG1120 222 PEEVL 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
997-1210 |
2.47e-29 |
|
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: 115.49 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASvpLEKLRRSL-A 1075
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD--LEKALSSLiS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDPTLFMGTIRNNLdryneysddevmgalkhasmwdyvqslpdgmnsavsegGLNLSQGQRQLLCLARALLTKARVI 1155
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1156 VMDEATASVDVQTDallQKVIRTSFA---GVTMLIIAHRLGTIADCDQIVEISAGEVK 1210
Cdd:cd03247 121 LLDEPTVGLDPITE---RQLLSLIFEvlkDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
383-600 |
2.66e-29 |
|
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: 117.05 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF---------VPEMpgRPRM 453
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditkknLREL--RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 454 AYVPQ--EAYIVNTSLLENLQFGEE---VSKEELRRALHNSCLSRDLKEWsggLRTEIGEkgvnLSGGQKQRVALARAFL 528
Cdd:COG1122 78 GLVFQnpDDQLFAPTVEEDVAFGPEnlgLPREEIRERVEEALELVGLEHL---ADRPPHE----LSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 529 RKPQIVLLDDPLSAVDADTENLLcERLIFG-AWKDVTRIVVTHRLEHLAQ-FDQVIYIQHGRVQGQGTFSELVK 600
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRREL-LELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFS 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
981-1209 |
3.02e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 124.44 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 981 KPLPEplrptwpEFGEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGV 1060
Cdd:PRK10789 305 EPVPE-------GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1061 NTASVPLEKLRRSLAIIPQDPTLFMGTIRNN--LDRYNEySDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQ 1138
Cdd:PRK10789 378 PLTKLQLDSWRSRLAVVSQTPFLFSDTVANNiaLGRPDA-TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQ 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1139 RQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
384-593 |
5.44e-29 |
|
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: 114.45 E-value: 5.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 384 QMQHFSLRHDGavSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGR---PRMAYV 456
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdgkdLASLSPKelaRKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQeayivntsLLENLqfgeevskeelrralhnsclsrdlkewsgGLrTEIGEKGVN-LSGGQKQRVALARAFLRKPQIVL 535
Cdd:cd03214 79 PQ--------ALELL-----------------------------GL-AHLADRPFNeLSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 536 LDDPLSAVDADTENLLCERLI-FGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRrLARERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
384-588 |
8.60e-29 |
|
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: 115.26 E-value: 8.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 384 QMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPEMPGRPRMAYV 456
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdgkdltkLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQ--EAYIVNTSL-------LENLQFGEEVSKEELRRALhNSCLSRDLKEWSggLRTeigekgvnLSGGQKQRVALARAF 527
Cdd:cd03225 81 FQnpDDQFFGPTVeeevafgLENLGLPEEEIEERVEEAL-ELVGLEGLRDRS--PFT--------LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 528 LRKPQIVLLDDPLSAVDADTENLLCERLIfgAWKD--VTRIVVTHRLEHLAQF-DQVIYIQHGR 588
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLK--KLKAegKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
399-598 |
1.40e-28 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 115.73 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPR--MAYVPQEAYIV-NTSLLENL 471
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgedVRKEPREARrqIGVLPDERGLYdRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 Q-FGE--EVSKEELRRALHNscLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTE 548
Cdd:COG4555 96 RyFAElyGLFDEELKKRIEE--LIELL-----GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 549 NLLceRLIFGAWKDVTRIVV--THRLEHLAQ-FDQVIYIQHGRVQGQGTFSEL 598
Cdd:COG4555 169 RLL--REILRALKKEGKTVLfsSHIMQEVEAlCDRVVILHKGKVVAQGSLDEL 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
144-594 |
1.87e-28 |
|
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: 121.78 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 144 LNERLFKHSLKLSQKSRQKNQVGDIvnhmsSDSDNVSDF-----PMVFGDLISAsFLIIGVVAMLFYYIGWSALAALAVL 218
Cdd:COG4618 95 LGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLRQFltgpgLFALFDLPWA-PIFLAVLFLFHPLLGLLALVGALVL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 219 FILAPLTNYVAKKFThldEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAevvsSLGY 298
Cdd:COG4618 169 VALALLNERLTRKPL---KEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDR----AGGF 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 299 LAVS-TLVLFV---ALAVHAW---RGEkLDAAVIFTCISLFGLLEGPFgDLS----RLISRATNAkvgARRILDYLNEDE 367
Cdd:COG4618 242 SALSkFLRLLLqsaVLGLGAYlviQGE-ITPGAMIAASILMGRALAPI-EQAiggwKQFVSARQA---YRRLNELLAAVP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 368 VEistEERTD-----GAavgLQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL- 441
Cdd:COG4618 317 AE---PERMPlprpkGR---LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVr 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 442 -------QFVPEMPGrPRMAYVPQEAYIVNTSLLENL-QFGEeVSKEEL----RRA-LHNSCLSrdLKEwsgGLRTEIGE 508
Cdd:COG4618 391 ldgadlsQWDREELG-RHIGYLPQDVELFDGTIAENIaRFGD-ADPEKVvaaaKLAgVHEMILR--LPD---GYDTRIGE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 509 KGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFGAWKD-VTRIVVTHRLEHLAQFDQVIYIQHG 587
Cdd:COG4618 464 GGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL-AAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDG 542
|
....*..
gi 499478341 588 RVQGQGT 594
Cdd:COG4618 543 RVQAFGP 549
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
399-573 |
2.42e-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: 114.11 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VPEMPGRPRMAYVPQEAYIVN-TSLLENLQFGE 475
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgEPVTGPGPDRGYVFQQDALLPwLTVLDNVALGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 476 E---VSKEELR-RALHnsCLSR-DLKEWSGGLRTEigekgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENL 550
Cdd:cd03293 99 ElqgVPKAEAReRAEE--LLELvGLSGFENAYPHQ-------LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ 169
|
170 180
....*....|....*....|....*
gi 499478341 551 LcERLIFGAWKD--VTRIVVTHRLE 573
Cdd:cd03293 170 L-QEELLDIWREtgKTVLLVTHDID 193
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
399-601 |
3.21e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 114.52 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRP---RMAYVPQEAY-------IVN 464
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpVTRRRRKAfrrRVQMVFQDPYaslhprhTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 TSLLENLQ-FGEEVSKEELRRALHNSCLSRDLKEwsgglRTeIGEkgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAV 543
Cdd:COG1124 100 RILAEPLRiHGLPDREERIAELLEQVGLPPSFLD-----RY-PHQ----LSGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 544 DADTE----NLLcERLIfgAWKDVTRIVVTHRL---EHLAqfDQVIYIQHGRVQGQGTFSELVKT 601
Cdd:COG1124 170 DVSVQaeilNLL-KDLR--EERGLTYLFVSHDLavvAHLC--DRVAVMQNGRIVEELTVADLLAG 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
339-582 |
3.37e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 121.07 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 339 FGDLSRLisRATNAKVGA-RRILDYLNEDEVEISTEERTDGAAvgLQMQHFSLRH-DGAVsdVLHDVNVHVPAGSSLAIV 416
Cdd:COG4178 322 YQSLAEW--RATVDRLAGfEEALEAADALPEAASRIETSEDGA--LALEDLTLRTpDGRP--LLEDLSLSLKPGERLLIT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 417 GPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRPRMAYVPQEAYIVNTSLLENL---QFGEEVSKEELRRALHNSCLSR 493
Cdd:COG4178 396 GPSGSGKSTLLRAIAGLWPYGSGRIA----RPAGARVLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGH 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 494 ------DLKEWSgglrteigekgVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIfGAWKDVTRIV 567
Cdd:COG4178 472 laerldEEADWD-----------QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR-EELPGTTVIS 539
|
250
....*....|....*
gi 499478341 568 VTHRLEHLAQFDQVI 582
Cdd:COG4178 540 VGHRSTLAAFHDRVL 554
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
997-1165 |
3.76e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.75 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE-----EGSISIDGVN--TASVPLEK 1069
Cdd:COG1117 12 IEVRNLNVYYGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDiyDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 LRRSLAIIPQDPTLFMGTIRNNLD---RYNEYSD----DE-VMGALKHASMWDYVQslpDGMNSAvsegGLNLSQGQRQL 1141
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAyglRLHGIKSkselDEiVEESLRKAALWDEVK---DRLKKS----ALGLSGGQQQR 162
|
170 180
....*....|....*....|....
gi 499478341 1142 LCLARALLTKARVIVMDEATASVD 1165
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALD 186
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
383-609 |
5.76e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 114.00 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG------RPR 452
Cdd:COG3638 3 LELRNLSKRYPGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVdgqdVTALRGralrrlRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 MAYVPQEAYIV-NTSLLENLQFG------------EEVSKEELRRALHnsCLSR-DL--KEWSgglRTEigekgvNLSGG 516
Cdd:COG3638 82 IGMIFQQFNLVpRLSVLTNVLAGrlgrtstwrsllGLFPPEDRERALE--ALERvGLadKAYQ---RAD------QLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 517 QKQRVALARAFLRKPQIVLLDDPLSAVDADT-----ENL--LCERLifgawkDVTRIVVTHRLEhLAQ--FDQVIYIQHG 587
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTarqvmDLLrrIARED------GITVVVNLHQVD-LARryADRIIGLRDG 223
|
250 260
....*....|....*....|..
gi 499478341 588 RVQGQGTFSELvkTCAPFAEFY 609
Cdd:COG3638 224 RVVFDGPPAEL--TDAVLREIY 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
384-588 |
6.43e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.80 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 384 QMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPEMPGRPRMAYV 456
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIdgkdiakLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQeayivntsllenlqfgeevskeelrralhnsclsrdlkewsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVLL 536
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 537 DDPLSAVDADTENLLcERLIFGAWKD-VTRIVVTHRLEHLAQF-DQVIYIQHGR 588
Cdd:cd00267 105 DEPTSGLDPASRERL-LELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
383-598 |
8.27e-28 |
|
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: 112.66 E-value: 8.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGavSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLL-----MSLLGEVAPREGSLQF---------VPEMP 448
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLdgkdiydldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 449 GRPRMAYVPQEAYIVNTSLLENLQFGEEVSKEELRRALHnsclsrDLKEWS---GGLRTEIGEK--GVNLSGGQKQRVAL 523
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELD------ERVEEAlrkAALWDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 524 ARAFLRKPQIVLLDDPLSAVD-ADTENLlcERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDpISTAKI--EELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
383-609 |
9.68e-28 |
|
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: 112.96 E-value: 9.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREG-------SLQFVPEMPGRPRMAY 455
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEAYIVNTSLLENLQFGEE-VSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIV 534
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 535 LLDDPLSAVDADTenllcERLIFGAWKDV----TRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPFAEFY 609
Cdd:cd03252 161 IFDEATSALDYES-----EHAIMRNMHDIcagrTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
997-1209 |
1.08e-27 |
|
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: 112.97 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRY--ASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:COG1124 2 LEVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPtlfMGTI--RNNLDRyneySDDEVMGALKHASMWDYVQSLPD--GMNSAVseggLN-----LSQGQRQLLCLA 1145
Cdd:COG1124 82 QMVFQDP---YASLhpRHTVDR----ILAEPLRIHGLPDREERIAELLEqvGLPPSF----LDryphqLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1146 RALLTKARVIVMDEATASVDVQTDA----LLQKVIRTSfaGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAeilnLLKDLREER--GLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
383-588 |
1.29e-27 |
|
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: 111.42 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF------VPEMPGRPRMAYV 456
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 -PQEAYIVNTSLLENLQF-----GEEVSKEELRRALHnsclsrdlkEWsgGLRTEIGEKGVNLSGGQKQRVALARAFLRK 530
Cdd:COG4133 81 gHADGLKPELTVRENLRFwaalyGLRADREAIDEALE---------AV--GLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 531 PQIVLLDDPLSAVDADTENLLCERLifGAWKDVTRIVV--THRLEHLAqFDQVIYIQHGR 588
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELI--AAHLARGGAVLltTHQPLELA-AARVLDLGDFK 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
998-1204 |
1.38e-27 |
|
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: 111.86 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 998 SVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntasVPLEKLRRSLAII 1077
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1078 PQ----DPT--------LFMGTIR--NNLDRYNEYSDDEVMGALKHASMWDYVqslpdgmNSAVSEgglnLSQGQRQLLC 1143
Cdd:cd03235 74 PQrrsiDRDfpisvrdvVLMGLYGhkGLFRRLSKADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1144 LARALLTKARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTIAD-CDQIVEI 1204
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
997-1208 |
1.51e-27 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 110.35 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASVPLEKLRRSL 1074
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMG-TIRNNLdryneysddevmgalkhasmwdyvqslpdgmnsavsegGLNLSQGQRQLLCLARALLTKAR 1153
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI--------------------------------------ALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIAHRLG-TIADCDQIVEISAGE 1208
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
399-589 |
1.89e-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: 111.43 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPR-------MAYVPQEAYIVNT-S 466
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdgtdISKLSEKELaafrrrhIGFVFQSFNLLPDlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLEN----LQFGEEVSKEELRRALHnsCLSRdlkewsGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSA 542
Cdd:cd03255 99 ALENvelpLLLAGVPKKERRERAEE--LLER------VGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 543 VDADTE----NLLCErliFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRV 589
Cdd:cd03255 171 LDSETGkevmELLRE---LNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
383-593 |
4.17e-27 |
|
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: 110.30 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPemPGRPRMAY 455
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgVP--PERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEaYIV--NTSLLENLQFG---EEVSKEELRRALHNSclsrdlkEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRK 530
Cdd:cd03259 77 VFQD-YALfpHLTVAENIAFGlklRGVPKAEIRARVREL-------LELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 531 PQIVLLDDPLSAVDADT-ENLLceRLIFGAWK--DVTRIVVTHRL-EHLAQFDQVIYIQHGRVQGQG 593
Cdd:cd03259 149 PSLLLLDEPLSALDAKLrEELR--EELKELQRelGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
378-570 |
6.23e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 111.33 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 378 GAAVGLQMQHFSLRHDGAVSD--VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VPEMPGRPRM 453
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 454 AYVPQEAyivntSLL------ENLQFGEE---VSKEELR-RALHNscLSR-DLKEWSGGLRTEigekgvnLSGGQKQRVA 522
Cdd:COG1116 83 GVVFQEP-----ALLpwltvlDNVALGLElrgVPKAERReRAREL--LELvGLAGFEDAYPHQ-------LSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 523 LARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFGAWKD--VTRIVVTH 570
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERL-QDELLRLWQEtgKTVLFVTH 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
997-1225 |
8.02e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 110.90 E-value: 8.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTL-F---------MGTI--RNNLDRYNEYSDDEVMGALKHASMWDYVqslpdgmNSAVSEgglnLSQGQRQLLCL 1144
Cdd:COG1120 80 VPQEPPApFgltvrelvaLGRYphLGLFGRPSAEDREAVEEALERTGLEHLA-------DRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1145 ARALLTKARVIVMDEATASVDV--QTD--ALLQKVIRTsfAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTE-F 1218
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLahQLEvlELLRRLARE--RGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEvL 226
|
....*..
gi 499478341 1219 SQEEIEE 1225
Cdd:COG1120 227 TPELLEE 233
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
76-359 |
1.28e-26 |
|
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: 111.49 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFI-GTISAGVTAETLPTALIYGVALGLCGFLSGLcmQHYFFNSLkAYQVTTNILNeRLFKHSLK 154
Cdd:cd07346 9 LLATALGLALPLLTKLLIdDVIPAGDLSLLLWIALLLLLLALLRALLSYL--RRYLAARL-GQRVVFDLRR-DLFRHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 155 LSQKSRQKNQVGDIVNHMSSDSDNVSDF-PMVFGDLISASFLIIGVVAMLFYyIGWS-ALAALAVLFILAPLTNYVAKKF 232
Cdd:cd07346 85 LSLSFFDRNRTGDLMSRLTSDVDAVQNLvSSGLLQLLSDVLTLIGALVILFY-LNWKlTLVALLLLPLYVLILRYFRRRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 233 THLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVLFVALAV 312
Cdd:cd07346 164 RKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499478341 313 HAWR--GEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd07346 244 GGYLvlQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
389-593 |
1.75e-26 |
|
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: 109.13 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 389 SLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG------RPRMAYVPQ 458
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkdLLKLSRrlrkirRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 459 EAY-------IVNTSLLENLQFGEEVSKEELRRALHNSCLSRdlkewsGGLRTEIGEKGVN-LSGGQKQRVALARAFLRK 530
Cdd:cd03257 90 DPMsslnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVG------VGLPEEVLNRYPHeLSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 531 PQIVLLDDPLSAVDADTE----NLL---CERLifgawkDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03257 164 PKLLIADEPTSALDVSVQaqilDLLkklQEEL------GLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
400-541 |
1.77e-26 |
|
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: 106.19 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF------VPEMPG-RPRMAYVPQEAYIVN-TSLLENL 471
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltDDERKSlRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 472 QFG-------EEVSKEELRRALHNscLSRDLKewsggLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLS 541
Cdd:pfam00005 81 RLGlllkglsKREKDARAEEALEK--LGLGDL-----ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
399-586 |
3.21e-26 |
|
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: 106.08 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLmSLLGEVAP-REGSLqfvpEMPGRPRMAYVPQEAYIVNTSLLENLqfgeev 477
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLWPwGSGRI----GMPEGEDLLFLPQRPYLPLGTLREQL------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 478 skeelrralhnsclsrdLKEWSGglrteigekgvNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLif 557
Cdd:cd03223 85 -----------------IYPWDD-----------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL-- 134
|
170 180 190
....*....|....*....|....*....|.
gi 499478341 558 gawKD--VTRIVVTHRLEHLAQFDQVIYIQH 586
Cdd:cd03223 135 ---KElgITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
998-1209 |
4.08e-26 |
|
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: 106.37 E-value: 4.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 998 SVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAII 1077
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1078 PQdptlfmgtirnNLDRYNeysddevMGALKHASMWDyvqslpdgmnsavsegglnLSQGQRQLLCLARALLTKARVIVM 1157
Cdd:cd03214 79 PQ-----------ALELLG-------LAHLADRPFNE-------------------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1158 DEATASVDV-QTDALLQKVIR-TSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03214 122 DEPTSHLDIaHQIELLELLRRlARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
143-613 |
7.14e-26 |
|
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: 116.20 E-value: 7.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 143 ILNERLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNV-SDFPMVFGDLISASFLIIG--VVAMLFYYIGWSALAALAVLF 219
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVdSMIPPVIKMFMGSLFNVIGalIVILLATPIAAVIIPPLGLLY 1118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 220 ILapLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYF-AWEKSVAKEVTEVREKE------LTSRRRLA-KAE 291
Cdd:TIGR00957 1119 FF--VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFeEQERFIHQSDLKVDENQkayypsIVANRWLAvRLE 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 292 VVSSlgylavsTLVLFVALAVHAWRgEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRILDYlNEDEVEI- 370
Cdd:TIGR00957 1197 CVGN-------CIVLFAALFAVISR-HSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEY-SETEKEAp 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 371 ----STEERTDGAAVG-LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-- 443
Cdd:TIGR00957 1268 wqiqETAPPSGWPPRGrVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdg 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 444 -----VPEMPGRPRMAYVPQEAYIVNTSLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQK 518
Cdd:TIGR00957 1348 lniakIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQR 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 519 QRVALARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVDLETDNLI-QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
490
....*....|....*
gi 499478341 599 VKTCAPFAEFYKEHG 613
Cdd:TIGR00957 1507 LQQRGIFYSMAKDAG 1521
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
383-598 |
1.13e-25 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 107.27 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG------RPR 452
Cdd:cd03256 1 IEVENLSKTYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdINKLKGkalrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 MAYVPQEAYIVN-TSLLENLQFG------------EEVSKEELRRALHnsCLSRDlkewsgGLRTEIGEKGVNLSGGQKQ 519
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGrlgrrstwrslfGLFPKEEKQRALA--ALERV------GLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 520 RVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLI-FGAWKDVTRIVVTHRLEhLAQ--FDQVIYIQHGRVQGQGTFS 596
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrINREEGITVIVSLHQVD-LAReyADRIVGLKDGRIVFDGPPA 230
|
..
gi 499478341 597 EL 598
Cdd:cd03256 231 EL 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
399-608 |
1.18e-25 |
|
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: 107.04 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-----VPEMPGRPRMAYVPQEAYIV-NTSLLENLQ 472
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkdiTNLPPEKRDISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 473 FG---EEVSKEELRRALHNscLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADT-E 548
Cdd:cd03299 94 YGlkkRKVDKKEIERKVLE--IAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 549 NLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVKTCAP--FAEF 608
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKKPKNefVAEF 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
371-601 |
1.48e-25 |
|
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: 107.30 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 371 STEERTDGAAVGL----QMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--- 443
Cdd:cd03288 4 SISGSSNSGLVGLggeiKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIdgi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 444 ----VPEMPGRPRMAYVPQEAYIVNTSLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQ 519
Cdd:cd03288 84 diskLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 520 RVALARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRV---------- 589
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATENIL-QKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILvecdtpenll 242
|
250
....*....|...
gi 499478341 590 -QGQGTFSELVKT 601
Cdd:cd03288 243 aQEDGVFASLVRT 255
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
743-969 |
1.61e-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: 109.12 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 743 IRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAP 822
Cdd:cd18600 99 ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 823 VMALYYVLQRDYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSS 902
Cdd:cd18600 179 VIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQM 258
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 903 RIPLVGGL-ISMATAVGVSLSAYygvmDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIER-LKF 969
Cdd:cd18600 259 RIEMIFVIfFTAVTFISIGTTGD----GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRiFKF 323
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
399-605 |
2.00e-25 |
|
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: 106.05 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEM------PGRPRMAYVPQEAYIVNT-SL 467
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedISGLseaelyRLRRRMGMLFQSGALFDSlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFG-EEVSK--EELRRALHNSCLSRdlkewsGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:cd03261 95 FENVAFPlREHTRlsEEEIREIVLEKLEA------VGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 545 ADTENLLcERLI--FGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVKTCAPF 605
Cdd:cd03261 169 PIASGVI-DDLIrsLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
379-598 |
2.31e-25 |
|
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: 109.03 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 379 AAVGLQMQHFSLrhdgavsdvlhDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQ-------------FVP 445
Cdd:COG4148 5 VDFRLRRGGFTL-----------DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiFLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 446 emPGRPRMAYVPQEAyivntSLL------ENLQFGEEVSKEELRRALHNsclsrDLKEWSGglrteIG---EKGV-NLSG 515
Cdd:COG4148 74 --PHRRRIGYVFQEA-----RLFphlsvrGNLLYGRKRAPRAERRISFD-----EVVELLG-----IGhllDRRPaTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 516 GQKQRVALARAFLRKPQIVLLDDPLSAVDADTEN----LLcERLifgawKDVTRI---VVTHRLE---HLAqfDQVIYIQ 585
Cdd:COG4148 137 GERQRVAIGRALLSSPRLLLMDEPLAALDLARKAeilpYL-ERL-----RDELDIpilYVSHSLDevaRLA--DHVVLLE 208
|
250
....*....|...
gi 499478341 586 HGRVQGQGTFSEL 598
Cdd:COG4148 209 QGRVVASGPLAEV 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
997-1209 |
9.10e-25 |
|
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: 101.74 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASvPLEKLRRSL 1074
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFAS-PRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQdptlfmgtirnnldryneysddevmgalkhasmwdyvqslpdgmnsavsegglnLSQGQRQLLCLARALLTKARV 1154
Cdd:cd03216 78 AMVYQ------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1155 IVMDEATASVDVQ-TDALLQKVIRTSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03216 104 LILDEPTAALTPAeVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
399-592 |
9.55e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.97 E-value: 9.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPR-------MAYVPQEAYIVNT-S 466
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdgqdISSLSERELarlrrrhIGFVFQFFNLLPElT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLEN----LQFGEEVSKEELRRALHnscLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSA 542
Cdd:COG1136 103 ALENvalpLLLAGVSRKERRERARE---LLERV-----GLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGN 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 543 VDADT-ENLLceRLIFGAWKD--VTRIVVTHRLEHLAQFDQVIYIQHGRVQGQ 592
Cdd:COG1136 175 LDSKTgEEVL--ELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
678-943 |
1.04e-24 |
|
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: 105.42 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILATLLLGATAATLLPLAQKAWLSYYSGH-QTEWVALTAIGI-YGLIGVLVLVGSLLnHLFWLDR-GIRAGKNMHDKML 754
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRILDVLLPDgDPETQALNVYSLaLLLLGLAQFILSFL-QSYLLNHtGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 755 KSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDY 834
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 835 RRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVG-GLISM 913
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGyLSYAL 241
|
250 260 270
....*....|....*....|....*....|
gi 499478341 914 ATAVGVSLSAyYGVMDAGTAGLVTLYSLSF 943
Cdd:pfam00664 242 ALWFGAYLVI-SGELSVGDLVAFLSLFAQL 270
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
997-1209 |
1.28e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 102.98 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEklRRSLAI 1076
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLF--MgTIRNNLD---RYNEYSDDE----VMGALKHASMWDYVQSLPDGmnsavsegglnLSQGQRQLLCLARA 1147
Cdd:cd03259 77 VFQDYALFphL-TVAENIAfglKLRGVPKAEirarVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1148 LLTKARVIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIAHRLG---TIAdcDQIVEISAGEV 1209
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEealALA--DRIAVMNEGRI 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
383-590 |
2.31e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.82 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF------------VPEMpgR 450
Cdd:COG2884 2 IRFENVSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlkrreIPYL--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 451 PRMAYVPQEAYIVNT-SLLENLQFGEEV---SKEELRRALhnsclsRDLKEWSGglrteIGEKG----VNLSGGQKQRVA 522
Cdd:COG2884 79 RRIGVVFQDFRLLPDrTVYENVALPLRVtgkSRKEIRRRV------REVLDLVG-----LSDKAkalpHELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 523 LARAFLRKPQIVLLDDPLSAVDADT-ENLLceRLIF-----GawkdVTRIVVTHRLEHLAQFDQ-VIYIQHGRVQ 590
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsWEIM--ELLEeinrrG----TTVLIATHDLELVDRMPKrVLELEDGRLV 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
399-589 |
2.96e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.60 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqfvpeMPGRP---------RMAYvpQEAYIVN-TSLL 468
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-----LAGTAplaearedtRLMF--QDARLLPwKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 469 ENLQFGEEVS-KEELRRALHNSCLSRDLKEWSGGLrteigekgvnlSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADT 547
Cdd:PRK11247 100 DNVGLGLKGQwRDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499478341 548 EnLLCERLIFGAWKD--VTRIVVTHRL-EHLAQFDQVIYIQHGRV 589
Cdd:PRK11247 169 R-IEMQDLIESLWQQhgFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
103-359 |
3.25e-24 |
|
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: 104.22 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 103 ETLPTALIYGVALGLCGFLSGLCMQHYFFN-SLKAYQVTTNILNErLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSD 181
Cdd:cd18559 32 GPQEHGQVYLSVLGALAILQGITVFQYSMAvSIGGIFASRAVHLD-LYHKALRSPISFFERTPSGELVNLFSKDLDRVDS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 182 FPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVK 261
Cdd:cd18559 111 MAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 262 YFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVLFVALAVHAWRGEK--LDAAVIFTCISLFGLLEGPF 339
Cdd:cd18559 191 AFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLagLVALKVFYSLALTTYLNWPL 270
|
250 260
....*....|....*....|
gi 499478341 340 GDLSRLISRATNAKVGARRI 359
Cdd:cd18559 271 NMSPEVITNIVAAEVSLERS 290
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
379-594 |
4.25e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 105.18 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 379 AAVGLQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPemPGRP 451
Cdd:COG3842 2 AMPALELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtgLP--PEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 452 RMAYVPQE-AYIVNTSLLENLQFG---EEVSKEELRR----ALHnsclsrdlkewsgglRTEIGEKG----VNLSGGQKQ 519
Cdd:COG3842 78 NVGMVFQDyALFPHLTVAENVAFGlrmRGVPKAEIRArvaeLLE---------------LVGLEGLAdrypHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 520 RVALARAFLRKPQIVLLDDPLSAVDADT-ENL------LCERLifgawkDVTRIVVTH-RLEHLAQFDQVIYIQHGRVQG 591
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLrEEMreelrrLQREL------GITFIYVTHdQEEALALADRIAVMNDGRIEQ 216
|
...
gi 499478341 592 QGT 594
Cdd:COG3842 217 VGT 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
383-588 |
5.05e-24 |
|
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: 100.34 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF---------VPEMPGRPRM 453
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdleDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 454 AYVPQEAYIVNT-SLLENLQFGeevskeelrralhnsclsrdlkewsgglrteigekgvnLSGGQKQRVALARAFLRKPQ 532
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 533 IVLLDDPLSAVDADTENLLcERLIFGAWKD--VTRIVVTHRLEHLAQF-DQVIYIQHGR 588
Cdd:cd03229 121 VLLLDEPTSALDPITRREV-RALLKSLQAQlgITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
997-1225 |
5.84e-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: 5.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYaSHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKLRRS 1073
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPTLF--MGTIRNNLdryneysddevMGALKHASMWdyvQSLPdGMNS---------AVSEGGL---------N 1133
Cdd:cd03256 80 IGMIFQQFNLIerLSVLENVL-----------SGRLGRRSTW---RSLF-GLFPkeekqralaALERVGLldkayqradQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1134 LSQGQRQLLCLARALLTKARVIVMDEATASVDVQT-----DALLQkvIRTSFaGVTMLIIAHRLGTIAD-CDQIVEISAG 1207
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASsrqvmDLLKR--INREE-GITVIVSLHQVDLAREyADRIVGLKDG 221
|
250
....*....|....*...
gi 499478341 1208 EVKSIRRPTEFSQEEIEE 1225
Cdd:cd03256 222 RIVFDGPPAELTDEVLDE 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
997-1214 |
6.36e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.66 E-value: 6.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYAS--HLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKLR 1071
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 R-SLAIIPQD----PTLfmgTIRNNLD---RYNEYSDDE----VMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQR 1139
Cdd:COG1136 85 RrHIGFVFQFfnllPEL---TALENVAlplLLAGVSRKErrerARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1140 QLLCLARALLTKARVIVMDEATASVDVQTD----ALLQKVIRTSfaGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRR 1214
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
387-594 |
1.15e-23 |
|
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: 106.53 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 387 HFSLRHDGAVsDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG------RPRMAYV 456
Cdd:COG1123 269 RYPVRGKGGV-RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdgkdLTKLSRrslrelRRRVQMV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQEAY-------IVNTSLLENLQFGEEVSKEELRR----ALHNSCLSRDLKEWSgglrteIGEkgvnLSGGQKQRVALAR 525
Cdd:COG1123 348 FQDPYsslnprmTVGDIIAEPLRLHGLLSRAERRErvaeLLERVGLPPDLADRY------PHE----LSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 526 AFLRKPQIVLLDDPLSAVD----ADTENL---LCERLifgawkDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGT 594
Cdd:COG1123 418 ALALEPKLLILDEPTSALDvsvqAQILNLlrdLQREL------GLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGP 488
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
997-1215 |
1.33e-23 |
|
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: 103.21 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQV--LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEA---EEGSISIDGVNTASVPLEKLR 1071
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 ----RSLAIIPQDPtlfMG------TIRNNLdryneysdDEVM---GALKHASMWDYVQSLPD--GMNSAVSEggLN--- 1133
Cdd:COG0444 82 kirgREIQMIFQDP---MTslnpvmTVGDQI--------AEPLrihGGLSKAEARERAIELLErvGLPDPERR--LDryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1134 --LSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDA----LLQKvIRTSFaGVTMLIIAHRLGTIAD-CD------- 1199
Cdd:COG0444 149 heLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAqilnLLKD-LQREL-GLAILFITHDLGVVAEiADrvavmya 226
|
250
....*....|....*...
gi 499478341 1200 -QIVEIsaGEVKSI-RRP 1215
Cdd:COG0444 227 gRIVEE--GPVEELfENP 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
383-598 |
1.66e-23 |
|
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: 106.14 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPR---EGSLQF-------VPEMPGRPR 452
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLdgrdlleLSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 MAYVPQE--AYIVNTSLLENLQFGEE---VSKEELRRAlhnsclSRDLKEwSGGLRTEIGEKGVNLSGGQKQRVALARAF 527
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALEnlgLSRAEARAR------VLELLE-AVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 528 LRKPQIVLLDDPLSAVDADTenllcERLIFGAWKDVTR------IVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTT-----QAEILDLLRELQRergttvLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEI 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
399-601 |
1.88e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 100.44 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG------RPRMAYVPQEA--YivnTS 466
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqdITGLSEkelyelRRRIGMLFQGGalF---DS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 L--LENLQFG-EEVSK--EELRRALHNSCLSRdlkewsGGLRteigekGVN------LSGGQKQRVALARAFLRKPQIVL 535
Cdd:COG1127 97 LtvFENVAFPlREHTDlsEAEIRELVLEKLEL------VGLP------GAAdkmpseLSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 536 LD------DPLSAvdADTENL---LCERLifgawkDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVKT 601
Cdd:COG1127 165 YDeptaglDPITS--AVIDELireLRDEL------GLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLAS 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
391-582 |
2.18e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 391 RHDGAvsDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqfvpEMPGRPRMAYVPQEAYIVNT----- 465
Cdd:NF040873 1 GYGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----RRAGGARVAYVPQRSEVPDSlpltv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 -SLLENLQFGEEVSKEELRRALH---NSCLSR-DLKEWSGglrTEIGEkgvnLSGGQKQRVALARAFLRKPQIVLLDDPL 540
Cdd:NF040873 75 rDLVAMGRWARRGLWRRLTRDDRaavDDALERvGLADLAG---RQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499478341 541 SAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVI 582
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
397-598 |
2.44e-23 |
|
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: 99.82 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 397 SDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMP--GRPRM--AYVPQEAYI-VNTSL 467
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrdITGLPphERARAgiGYVPEGRRIfPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEEVSKEELRRALHNSCLSR--DLKEwsggLRteiGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPlsavda 545
Cdd:cd03224 93 EENLLLGAYARRRAKRKARLERVYELfpRLKE----RR---KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP------ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 546 dTENL---LCERlIFGAWKD-----VTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:cd03224 160 -SEGLapkIVEE-IFEAIRElrdegVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
997-1201 |
3.02e-23 |
|
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: 99.09 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPlEKLRRSLAI 1076
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMG-TIRNNLD-----RYNEYSDDEVMGALKHASMWDYvqslpdgMNSAVSegglNLSQGQRQLLCLARALLT 1150
Cdd:COG4133 80 LGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1151 KARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIA-HRLGTIADCDQI 1201
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
997-1193 |
3.07e-23 |
|
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: 99.14 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASVPLEKLRRSL 1074
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLF--MgTIRNNL--------DRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCL 1144
Cdd:cd03262 79 GMVFQQFNLFphL-TVLENItlapikvkGMSKAEAEERALELLEKVGLADKADAYPA-----------QLSGGQQQRVAI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1145 ARALLTKARVIVMDEATASVDVQTDALLQKVIRtSFA--GVTMLIIAHRLG 1193
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMK-DLAeeGMTMVVVTHEMG 196
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
399-598 |
4.09e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 102.46 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPemPGRPRMAYVPQEaYIV--NTSLLE 469
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIggrdvtdLP--PKDRNIAMVFQS-YALypHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFG---EEVSKEELRRAlhnsclsrdLKEWSGGLrtEIGE----KGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSA 542
Cdd:COG3839 95 NIAFPlklRKVPKAEIDRR---------VREAAELL--GLEDlldrKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 543 VDAD------TEnL--LCERLifgawkDVTRIVVTH-RLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:COG3839 164 LDAKlrvemrAE-IkrLHRRL------GTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
997-1223 |
4.85e-23 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 100.20 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP-LEKLRRSLA 1075
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDP-TLFMGTIrnnldryneYSDD-----EVMG------------ALKHASMWDYVQSLPdgmnsavseggLNLSQG 1137
Cdd:TIGR04520 81 MVFQNPdNQFVGAT---------VEDDvafglENLGvpreemrkrvdeALKLVGMEDFRDREP-----------HLLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1138 QRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRT--SFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRP 1215
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTP 220
|
....*....
gi 499478341 1216 TE-FSQEEI 1223
Cdd:TIGR04520 221 REiFSQVEL 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
399-589 |
1.18e-22 |
|
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: 96.31 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG--RPRMAYVPQEAYIVNT-SLLENL 471
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgkdIKKEPEevKRRIGYLPEEPSLYENlTVRENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 QfgeevskeelrralhnsclsrdlkewsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLL 551
Cdd:cd03230 95 K----------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 499478341 552 CERLIFGAWKDVTRIVVTHRLEHLAQ-FDQVIYIQHGRV 589
Cdd:cd03230 135 WELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
997-1209 |
1.28e-22 |
|
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: 97.89 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKL-RRSLA 1075
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDPTLFMG-TIRNNLD----RYNEYSDDEVMGALKHASMWDYVQS------LPDGMNSAVSegglNLSQGQRQLLCL 1144
Cdd:cd03219 79 RTFQIPRLFPElTVLENVMvaaqARTGSGLLLARARREEREARERAEEllervgLADLADRPAG----ELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1145 ARALLTKARVIVMDEATASV-DVQTDALLQKVIRTSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
383-590 |
2.48e-22 |
|
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: 96.55 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPR-MAYVP 457
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggrdVTDLPPKDRdIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 458 QE-AYIVNTSLLENLQFG---EEVSKEELRRALHNscLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQI 533
Cdd:cd03301 79 QNyALYPHMTVYDNIAFGlklRKVPKDEIDERVRE--VAELL-----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 534 VLLDDPLSAVDAD------TE-NLLCERLifgawkDVTRIVVTH-RLEHLAQFDQVIYIQHGRVQ 590
Cdd:cd03301 152 FLMDEPLSNLDAKlrvqmrAElKRLQQRL------GTTTIYVTHdQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
706-968 |
4.94e-22 |
|
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: 97.67 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 706 GHQTEWVALTAIGIYGLIGVLvlvGSLLNHLFWLD---RGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVE 782
Cdd:cd18559 30 VNGPQEHGQVYLSVLGALAIL---QGITVFQYSMAvsiGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 783 SVDVYLQwSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRDYRRPAREVKRFDSVARSPRYAHFKESLQG 862
Cdd:cd18559 107 RVDSMAP-QVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 863 LVVIRSFNKGPWFMQNFYAKLSHSnRMFYSHVMINRWFSSRIPLVGGLIsmataVGVSLSAYYGVMD--AGTAGLVTLYS 940
Cdd:cd18559 186 ISVIKAFEWEEAFIRQVDAKRDNE-LAYLPSIVYLRALAVRLWCVGPCI-----VLFASFFAYVSRHslAGLVALKVFYS 259
|
250 260
....*....|....*....|....*...
gi 499478341 941 LSFWGFLNWGVRIFADIESRMTSIERLK 968
Cdd:cd18559 260 LALTTYLNWPLNMSPEVITNIVAAEVSL 287
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
997-1218 |
5.85e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.03 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE-----EGSISIDGVNTAS--VPLEK 1069
Cdd:PRK14258 8 IKVNNLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 LRRSLAIIPQDPTLFMGTIRNNLD--------RYNEYSDDEVMGALKHASMWDYVQSlpdgmnsAVSEGGLNLSQGQRQL 1141
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAygvkivgwRPKLEIDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1142 LCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSF--AGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTEF 1218
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEF 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
747-1208 |
7.58e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 102.80 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 747 KNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFdsavhcaLQVIVSIVLILGLMPLMVF-------V 819
Cdd:PTZ00265 130 KTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKF-------ITIFTYASAFLGLYIWSLFknarltlC 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 820 IAPVMALYYVLQRDYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFyaKLSHSnrmFYSHVMINRW 899
Cdd:PTZ00265 203 ITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKF--NLSEK---LYSKYILKAN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 900 F--SSRIPLVGGLISMATAVGV---------SLSAYYGVMDAGTAG--------LVTLYSLSFwgflnwgvrIFADIESR 960
Cdd:PTZ00265 278 FmeSLHIGMINGFILASYAFGFwygtriiisDLSNQQPNNDFHGGSvisillgvLISMFMLTI---------ILPNITEY 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 961 MTSIERlkffSNLPGEVSVLKPLPEPLR--PTWPEFGEISVEGLKVRYASHLP-QVLKGITFKVEAGSRVGIIGRTGSGK 1037
Cdd:PTZ00265 349 MKSLEA----TNSLYEIINRKPLVENNDdgKKLKDIKKIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGK 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1038 STFFQSLFRFIEAEEGSISI-DGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNL--------------DRYNE----- 1097
Cdd:PTZ00265 425 STILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsNYYNEdgnds 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1098 ---------------------------------------YSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQ 1138
Cdd:PTZ00265 505 qenknkrnscrakcagdlndmsnttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQ 584
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1139 RQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRT--SFAGVTMLIIAHRLGTIADCDQIVEISAGE 1208
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
947-1215 |
1.27e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.65 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 947 LNWGVRIFADIESRMTSIERLKFFSNLPGEVSVLKPLPEPLRPtwPEFGEISVEGLKVRyashLPQ---VLKGITFKVEA 1023
Cdd:COG4178 315 LSWFVDNYQSLAEWRATVDRLAGFEEALEAADALPEAASRIET--SEDGALALEDLTLR----TPDgrpLLEDLSLSLKP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1024 GSRVGIIGRTGSGKSTFFQSLfrfieA-----EEGSISidgvntasVPleKLRRSLaIIPQDPTLFMGTIRNNL---DRY 1095
Cdd:COG4178 389 GERLLITGPSGSGKSTLLRAI-----AglwpyGSGRIA--------RP--AGARVL-FLPQRPYLPLGTLREALlypATA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1096 NEYSDDEVMGALKHASMWDYVQSLPDGMN-SAVsegglnLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQK 1174
Cdd:COG4178 453 EAFSDAELREALEAVGLGHLAERLDEEADwDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499478341 1175 VIRTSFAGVTMLIIAHRLGTIADCDQIVEISA---GEVKSIRRP 1215
Cdd:COG4178 527 LLREELPGTTVISVGHRSTLAAFHDRVLELTGdgsWQLLPAEAP 570
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
997-1209 |
2.12e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.96 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKLRRS 1073
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPTLFMG-TIRNNLD---RYNEYSDDE----VMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLA 1145
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVAlplRVTGKSRKEirrrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1146 RALLTKARVIVMDEATASVDVQTDA----LLQKVIRTsfaGVTMLIIAHRLGTIADCDQ-IVEISAGEV 1209
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWeimeLLEEINRR---GTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
997-1190 |
2.53e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.77 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHL--PQVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFR----FIEAEEGSISIDGVntasvPLEKL 1070
Cdd:COG1116 8 LELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRliagLEKPTSGEVLVDGK-----PVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1071 RRSLAIIPQDPTLF--MgTIRNNL-------DRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQL 1141
Cdd:COG1116 79 GPDRGVVFQEPALLpwL-TVLDNValglelrGVPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1142 LCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIAH 1190
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
398-594 |
2.61e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 96.75 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--------VPemPGRPRMAYVPQE-AYIVNTSLL 468
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngrdlftnLP--PRERRVGFVFQHyALFPHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 469 ENLQFGEEV---SKEELRRalhnsclsrDLKEWsggLRtEIGEKGV------NLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:COG1118 94 ENIAFGLRVrppSKAEIRA---------RVEEL---LE-LVQLEGLadrypsQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 540 LSAVDADTENLLcERLIFGAWKD--VTRIVVTHRLE---HLAqfDQVIYIQHGRVQGQGT 594
Cdd:COG1118 161 FGALDAKVRKEL-RRWLRRLHDElgGTTVFVTHDQEealELA--DRVVVMNQGRIEQVGT 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
387-589 |
2.90e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 93.09 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 387 HFSLRHDgavSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPRMAYVPQEAyi 462
Cdd:cd03226 6 SFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpIKAKERRKSIGYVMQDV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 vntslleNLQFGEEVSKEELRRALHNscLSRDLKEWSGGLRT-EI-GEKGVN---LSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:cd03226 81 -------DYQLFTDSVREELLLGLKE--LDAGNEQAETVLKDlDLyALKERHplsLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 538 DPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRV 589
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
997-1212 |
3.07e-21 |
|
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: 93.69 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLP--QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntasVPLEKLRRSL 1074
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLF--MgTIRNNL---DRYNEYSDDE----VMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLA 1145
Cdd:cd03293 76 GYVFQQDALLpwL-TVLDNValgLELQGVPKAEarerAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1146 RALLTKARVIVMDEATASVDVQTDALLQ----KVIRTSfaGVTMLIIAHRLG-TIADCDQIVEISA--GEVKSI 1212
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQeellDIWRET--GKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
997-1209 |
3.80e-21 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 93.80 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQV--LKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFIEAEE----GSISIDGVNTASVP---L 1067
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINGLErptsGSVLVDGTDLTLLSgkeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1068 EKLRRSLAIIPQDPTLFMG-TIRNNldryneysddeVMGALKHASMWDYVQslpdgmNSAVSE----GGL---------N 1133
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSSrTVFEN-----------VALPLEIAGVPKAEI------EERVLEllelVGLedkadaypaQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1134 LSQGQRQLLCLARALLTKARVIVMDEATASVDVQTD----ALLQKVIRTsfAGVTMLIIAHRLGTIAD-CDQIVEISAGE 1208
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTqsilALLRDINRE--LGLTIVLITHEMEVVKRiCDRVAVMEKGE 218
|
.
gi 499478341 1209 V 1209
Cdd:cd03258 219 V 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
997-1192 |
4.27e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 93.27 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRY-ASHlpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEK-LRRSL 1074
Cdd:cd03224 1 LEVENLNAGYgKSQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFMG-TIRNNLdryneysddeVMGALKH---------ASMWDYVQSLPDGMNSAVSegglNLSQGQRQLLCL 1144
Cdd:cd03224 78 GYVPEGRRIFPElTVEENL----------LLGAYARrrakrkarlERVYELFPRLKERRKQLAG----TLSGGEQQMLAI 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1145 ARALLTKARVIVMDEAT---ASVDVQTdaLLQKVIRTSFAGVTMLIIAHRL 1192
Cdd:cd03224 144 ARALMSRPKLLLLDEPSeglAPKIVEE--IFEAIRELRDEGVTILLVEQNA 192
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
399-598 |
5.56e-21 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 93.52 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG------RPRMAYVPQEAYIV-NTSL 467
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLegtdITKLRGkklrklRRRIGMIFQHYNLIeRLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGE------------EVSKEELRRALhnSCLSRdlkewsGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVL 535
Cdd:TIGR02315 97 LENVLHGRlgykptwrsllgRFSEEDKERAL--SALER------VGLADKAYQRADQLSGGQQQRVAIARALAQQPDLIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 536 LDDPLSAVDADTENLLCERLIFGAWKD-VTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:TIGR02315 169 ADEPIASLDPKTSKQVMDYLKRINKEDgITVIINLHQVDLAKKYaDRIVGLKAGEIVFDGAPSEL 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
997-1226 |
6.44e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDP-TLFMG-TIRnnldryneysDDEVMG----ALKHASMWDYVQSLPD--GMNSAVSEGGLNLSQGQRQLLCLARAL 1148
Cdd:PRK13632 88 IFQNPdNQFIGaTVE----------DDIAFGlenkKVPPKKMKDIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1149 LTKARVIVMDEATASVDVQTDALLQKVIRT--SFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE-FSQEEIEE 1225
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEiLNNKEILE 237
|
.
gi 499478341 1226 S 1226
Cdd:PRK13632 238 K 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
997-1209 |
8.20e-21 |
|
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: 92.43 E-value: 8.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRY--ASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRsl 1074
Cdd:cd03266 2 ITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 aiipqdptlfMGTIRNNLDRYNEYSDDEVMG------ALKHASMWDYVQSLPD--GMNSAVSEGGLNLSQGQRQLLCLAR 1146
Cdd:cd03266 80 ----------LGFVSDSTGLYDRLTARENLEyfaglyGLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1147 ALLTKARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
997-1209 |
9.29e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 92.17 E-value: 9.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLP--QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKL---- 1070
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1071 RRSLAIIPQD----PTLfmgTIRNNLD---RYNEYSDDEVMGALKHasMWDYVQsLPDGMNSAVSEgglnLSQGQRQLLC 1143
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVElplLLAGVPKKERRERAEE--LLERVG-LGDRLNHYPSE----LSGGQQQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1144 LARALLTKARVIVMDEATASVDVQTD----ALLQKVirTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGkevmELLREL--NKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
450-599 |
1.73e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.56 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 450 RPRMAYVPQEAYIVNTSLLENLQFG-EEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFL 528
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALL 1374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 529 RKPQIVLLDDPLSAVDADTENLLCERLIFGAWK-DVTRIVVTHRLEHLAQFDQVIYIQH-----GRVQGQGTFSELV 599
Cdd:PTZ00265 1375 REPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELL 1451
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
395-608 |
1.97e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 395 AVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLL--MSLLgEVaPREGSL-----QF-VPEMPGRPRMAYVPQEAYIV--- 463
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvLNLL-ET-PDSGQLniaghQFdFSQKPSEKAIRLLRQKVGMVfqq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 -----NTSLLENLQfgeE-------VSKEELR-RAlhNSCLSRdlkewsggLRteIGEKG----VNLSGGQKQRVALARA 526
Cdd:COG4161 91 ynlwpHLTVMENLI---EapckvlgLSKEQAReKA--MKLLAR--------LR--LTDKAdrfpLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 527 FLRKPQIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEhLAQ--FDQVIYIQHGRVQGQGTFSELV--KTC 602
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVE-FARkvASQVVYMEKGRIIEQGDASHFTqpQTE 234
|
....*.
gi 499478341 603 ApFAEF 608
Cdd:COG4161 235 A-FAHY 239
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
997-1190 |
2.08e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.21 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE-----EGSISIDGVNTASV---PLE 1068
Cdd:PRK14267 5 IETVNLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPdvdPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1069 kLRRSLAIIPQDPTLF----------MGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQslpDGMNSAVSegglNLSQGQ 1138
Cdd:PRK14267 83 -VRREVGMVFQYPNPFphltiydnvaIGVKLNGLVKSKKELDERVEWALKKAALWDEVK---DRLNDYPS----NLSGGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1139 RQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAH 1190
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
383-573 |
2.22e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.07 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAvsDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VP-EMPGRPRMAYVPQE 459
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgKPvEGPGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 460 AYIVNTSLLENLQFGEE---VSKEElRRALHNSCLSR-DLKEWsgglrteiGEKGV-NLSGGQKQRVALARAFLRKPQIV 534
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQlagVEKMQ-RLEIAHQMLKKvGLEGA--------EKRYIwQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499478341 535 LLDDPLSAVDADTENLLCErLIFGAWKDVTRIV--VTHRLE 573
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQT-LLLKLWQETGKQVllITHDIE 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
383-598 |
2.34e-20 |
|
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: 91.53 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpemPGRPrMAYVPQEAYI 462
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL----DGKD-ITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 VNT-----------SLLENLQFG---EEVSKEELRRALHNSClsrDLKEWSGGLRTEIGEkgvnLSGGQKQRVALARAFL 528
Cdd:cd03300 74 VNTvfqnyalfphlTVFENIAFGlrlKKLPKAEIKERVAEAL---DLVQLEGYANRKPSQ----LSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 529 RKPQIVLLDDPLSAVDAD-TENLLCE--RLifgaWKDV--TRIVVTH-RLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKlRKDMQLElkRL----QKELgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
997-1217 |
4.54e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTL-FMGTIRNNLDryneysddevMGALKHASMWDYVQSLPD-GMNSAVSEGGL---------NLSQGQRQLLCLA 1145
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVE----------MGRTPHRSRFDTWTETDRaAVERAMERTGVaqfadrpvtSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1146 RALLTKARVIVMDEATASVD----VQTDALLQKVI---RTSFAGVTMLIIAHRLgtiadCDQIVEISAGEVKSIRRPTE 1217
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDinhqVRTLELVRRLVddgKTAVAAIHDLDLAARY-----CDELVLLADGRVRAAGPPAD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
997-1209 |
4.61e-20 |
|
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: 90.81 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKLRRS 1073
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPTLF--MgTIRNN----LDRYNEYSDDE----VMGALKHASMWDYVQSLPdgmnsavSEgglnLSQGQRQLLC 1143
Cdd:COG1127 84 IGMLFQGGALFdsL-TVFENvafpLREHTDLSEAEirelVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1144 LARALLTKARVIVMDEATASVDVQTDALLQKVIRT---SFaGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdEL-GLTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1012-1223 |
7.88e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASvPLEKLRRSLAIIPQDPTLFMG-TI 1088
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRS-PRDAQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1089 RNNLdryneYSDDEVM--GALKHASMWDYVQSLPDGMNSAVSEGGL--NLSQGQRQLLCLARALLTKARVIVMDEATASV 1164
Cdd:COG1129 97 AENI-----FLGREPRrgGLIDWRAMRRRARELLARLGLDIDPDTPvgDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1165 DVQ-TDALLqKVIRT-SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:COG1129 172 TEReVERLF-RIIRRlKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTEDEL 232
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
678-967 |
8.02e-20 |
|
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: 91.46 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILATLLLGATAATLLPLAQKAWLSYYSGHQTEWVALTAIGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSV 757
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 758 LSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGL---MPLMVFVIAPVMALYYVLQRDY 834
Cdd:cd07346 83 QRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLnwkLTLVALLLLPLYVLILRYFRRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 835 RRPA-REVKRfdSVARSprYAHFKESLQGLVVIRSFNKGPWFMQNFyakLSHSNRMFYSHVMINRWFSSRIPLVGGLISM 913
Cdd:cd07346 163 IRKAsREVRE--SLAEL--SAFLQESLSGIRVVKAFAAEEREIERF---REANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 914 ATAVGVSLSAYY---GVMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIERL 967
Cdd:cd07346 236 GTALVLLYGGYLvlqGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
997-1190 |
9.18e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.36 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYAShlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE-----EGSISIDGVNTASVPLEKLR 1071
Cdd:PRK14247 4 IEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLAIIPQDP------TLF----MGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQslpDGMNSAVSEgglnLSQGQRQL 1141
Cdd:PRK14247 82 RRVQMVFQIPnpipnlSIFenvaLGLKLNRLVKSKKELQERVRWALEKAQLWDEVK---DRLDAPAGK----LSGGQQQR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499478341 1142 LCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAH 1190
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
382-547 |
1.17e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.69 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 382 GLQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPR---EGSLQF----VPEMPGRPR-M 453
Cdd:COG4136 1 MLSLENLTITLGGRP--LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLngrrLTALPAEQRrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 454 AYVPQEAYIV-NTSLLENLQFG--EEVSKEElRRALHNSCLSrdlkewSGGLrTEIGEKGVN-LSGGQKQRVALARAFLR 529
Cdd:COG4136 79 GILFQDDLLFpHLSVGENLAFAlpPTIGRAQ-RRARVEQALE------EAGL-AGFADRDPAtLSGGQRARVALLRALLA 150
|
170
....*....|....*...
gi 499478341 530 KPQIVLLDDPLSAVDADT 547
Cdd:COG4136 151 EPRALLLDEPFSKLDAAL 168
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
381-598 |
1.30e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.04 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 381 VGLQMQHFSLRHDgavsdvlhdvnVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMP--GRPrMA 454
Cdd:COG3840 7 LTYRYGDFPLRFD-----------LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdLTALPpaERP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 455 YVPQEayivNT-----SLLENLQFG-------EEVSKEELRRALHnsclsrdlkewsgglRTEIGEKG----VNLSGGQK 518
Cdd:COG3840 75 MLFQE----NNlfphlTVAQNIGLGlrpglklTAEQRAQVEQALE---------------RVGLAGLLdrlpGQLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 519 QRVALARAFLRKPQIVLLDDPLSAVD----ADTENL---LCERLifgawkDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQ 590
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLvdeLCRER------GLTVLMVTHDPEDAARIaDRVLLVADGRIA 209
|
....*...
gi 499478341 591 GQGTFSEL 598
Cdd:COG3840 210 ADGPTAAL 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
998-1209 |
1.33e-19 |
|
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: 89.71 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 998 SVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKL-RRSLAI 1076
Cdd:COG0411 6 EVRGLTKRFGGL--VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMG-TIRNNL-------DRYNEYSD---------------DEVMGALKHASMWDYVQSLPDgmnsavsegglN 1133
Cdd:COG0411 84 TFQNPRLFPElTVLENVlvaaharLGRGLLAAllrlprarreerearERAEELLERVGLADRADEPAG-----------N 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1134 LSQGQRQLLCLARALLTKARVIVMDEATASVDVQ-TDALLQKV--IRTSFaGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAELIrrLRDER-GITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
396-596 |
1.52e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 396 VSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSL-LGEVaPREGSL-----QF-VPEMPGRPRMAYVPQEAYIV----- 463
Cdd:PRK11124 14 AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEM-PRSGTLniagnHFdFSKTPSDKAIRELRRNVGMVfqqyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 ---NTSLLENLQfgE------EVSKEELR-RALhnSCLSRdlkewsggLR-TEIGEK-GVNLSGGQKQRVALARAFLRKP 531
Cdd:PRK11124 93 lwpHLTVQQNLI--EapcrvlGLSKDQALaRAE--KLLER--------LRlKPYADRfPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 532 QIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEhLAQ--FDQVIYIQHGRVQGQGTFS 596
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVE-VARktASRVVYMENGHIVEQGDAS 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
399-598 |
2.64e-19 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 88.41 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEMPG------RPRMAYVPQEAYIVNT-SL 467
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgTDLTLLSGkelrkaRRRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEE---VSKEELRRAlhnsclSRDLKEWSGgLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:cd03258 100 FENVALPLEiagVPKAEIEER------VLELLELVG-LEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 545 ADTENLLCERLifgawKDVTR------IVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:cd03258 173 PETTQSILALL-----RDINRelgltiVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEV 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
383-594 |
2.69e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpempGRP----------- 451
Cdd:PRK13548 3 LEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN----GRPladwspaelar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 452 RMAYVPQEAyivntslleNLQFG---EEV----------SKEELRRALHNSCLSRDLKEWSGGLRTEigekgvnLSGGQK 518
Cdd:PRK13548 77 RRAVLPQHS---------SLSFPftvEEVvamgraphglSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 519 QRVALARAFLR------KPQIVLLDDPLSAVD-ADTENLLceRLIfgawKDVTR------IVVTHRLEHLAQF-DQVIYI 584
Cdd:PRK13548 141 QRVQLARVLAQlwepdgPPRWLLLDEPTSALDlAHQHHVL--RLA----RQLAHerglavIVVLHDLNLAARYaDRIVLL 214
|
250
....*....|
gi 499478341 585 QHGRVQGQGT 594
Cdd:PRK13548 215 HQGRLVADGT 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
399-579 |
3.24e-19 |
|
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: 93.66 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLmSLLGEVAPREGSLQFVPEmpgRPRMAYVPQEAYIVNTSLLENL------- 471
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLF-RILGELWPVYGGRLTKPA---KGKLFYVPQRPYMTLGTLRDQIiypdsse 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 -QFGEEVSKEELRRALHNSCLSRDLKEwSGGLRTEIGEKGVnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENl 550
Cdd:TIGR00954 543 dMKRRGLSDKDLEQILDNVQLTHILER-EGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG- 619
|
170 180 190
....*....|....*....|....*....|....*..
gi 499478341 551 lcerLIFGAWKD--VTRIVVTHRL------EHLAQFD 579
Cdd:TIGR00954 620 ----YMYRLCREfgITLFSVSHRKslwkyhEYLLYMD 652
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
997-1209 |
4.72e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.14 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQV--LKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFI----EAEEGSISIDGVNTASVP---L 1067
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKST----LIRCInlleRPTSGSVLVDGVDLTALSereL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1068 EKLRRSLAIIPQDPTLFMG-TIRNNldryneysddeVMGALKHAsmwdyvqslpdGMNSA-----VSE----GGL----- 1132
Cdd:COG1135 78 RAARRKIGMIFQHFNLLSSrTVAEN-----------VALPLEIA-----------GVPKAeirkrVAEllelVGLsdkad 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1133 ----NLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTD----ALLQKvIRTSFaGVTMLIIAHRLGTIAD-CDQIVE 1203
Cdd:COG1135 136 aypsQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAV 213
|
....*.
gi 499478341 1204 ISAGEV 1209
Cdd:COG1135 214 LENGRI 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1013-1217 |
4.78e-19 |
|
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: 87.78 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKlrRSLAIIPQDPTLF--MgTIRN 1090
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFphM-TVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1091 NLdrynEYS--DDEVMGALKHASMWDYVQSLpdGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQT 1168
Cdd:cd03299 91 NI----AYGlkKRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1169 DALLQ---KVIRTSFaGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTE 1217
Cdd:cd03299 165 KEKLReelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
996-1192 |
6.51e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 996 EISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTF---FQSLFRFIEA--EEGSISIDGVN--TASVPLE 1068
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNRLNDLIPGfrVEGKVTFHGKNlyAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1069 KLRRSLAIIPQDPTLFMGTIRNNLD---RYNEYS---DDEVMGALKHASMWDYVQslpDGMNsavsEGGLNLSQGQRQLL 1142
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAygaRINGYKgdmDELVERSLRQAALWDEVK---DKLK----QSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 1143 CLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRL 1192
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
382-598 |
6.64e-19 |
|
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: 87.39 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 382 GLQMQHFSLRHDGAVSdvLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPR-MAYV 456
Cdd:cd03296 2 SIEVRNVSKRFGDFVA--LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedATDVPVQERnVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQE-AYIVNTSLLENLQFGEEV-------SKEELRRALHNSClsrDLKEWSGglrteIGEKGVN-LSGGQKQRVALARAF 527
Cdd:cd03296 80 FQHyALFRHMTVFDNVAFGLRVkprserpPEAEIRAKVHELL---KLVQLDW-----LADRYPAqLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 528 LRKPQIVLLDDPLSAVDADTENLLcerlifGAW-------KDVTRIVVTH-RLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKEL------RRWlrrlhdeLHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
385-590 |
7.36e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 7.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 385 MQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRPRMAYVPQEAYIV- 463
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS----IPKGLRIGYLPQEPPLDd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 NTSLLENLQFG-EEVSK--EELRRALHN-SCLSRDLKE-------------WSG-----------GLRTEIGEKGV-NLS 514
Cdd:COG0488 75 DLTVLDTVLDGdAELRAleAELEELEAKlAEPDEDLERlaelqeefealggWEAearaeeilsglGFPEEDLDRPVsELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 515 GGQKQRVALARAFLRKPQIVLLDDP---LsavDADT----ENLLCERlifgawkDVTRIVVTH-R--LEHLAqfDQVIYI 584
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPtnhL---DLESiewlEEFLKNY-------PGTVLVVSHdRyfLDRVA--TRILEL 222
|
....*.
gi 499478341 585 QHGRVQ 590
Cdd:COG0488 223 DRGKLT 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
397-539 |
9.26e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 86.96 E-value: 9.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 397 SDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMP--GRPRM--AYVPQEAYI-VNTSL 467
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdgedITGLPphRIARLgiGYVPEGRRIfPSLTV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 468 LENLQFGEEV--SKEELRRALHnSCLSR--DLKEwsgglRteIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:COG0410 96 EENLLLGAYArrDRAEVRADLE-RVYELfpRLKE-----R--RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
997-1227 |
1.05e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.73 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYashlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKlrRSLAI 1076
Cdd:COG3840 2 LRLDDLTYRY----GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMG-TIRNNLD-------RYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARAL 1148
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGlglrpglKLTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1149 LTKARVIVMDEATASVD----VQTDALLQKVIRTsfAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEP 222
|
....
gi 499478341 1224 EESL 1227
Cdd:COG3840 223 PPAL 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
997-1209 |
1.57e-18 |
|
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: 86.02 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASV---PLEKLRRS 1073
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPTLF--MgTIRNN----LDRYNEYSDDE----VMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLC 1143
Cdd:cd03261 79 MGMLFQSGALFdsL-TVFENvafpLREHTRLSEEEireiVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1144 LARALLTKARVIVMDEATASVD-VQTDALLQKVIRTSFA-GVTMLIIAHRLGTI-ADCDQIVEISAGEV 1209
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSLKKElGLTSIMVTHDLDTAfAIADRIAVLYDGKI 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
383-617 |
1.65e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 87.38 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfVPEMP--------GRPRMA 454
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT-VGGMVlseetvwdVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 455 YVPQ--EAYIVNTSLLENLQFGEE---VSKEELRRALHNSclsrdLKEWsgGLRTEIGEKGVNLSGGQKQRVALARAFLR 529
Cdd:PRK13635 85 MVFQnpDNQFVGATVQDDVAFGLEnigVPREEMVERVDQA-----LRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 530 KPQIVLLDDPLSAVDA-------DTENLLCERlifgawKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTC 602
Cdd:PRK13635 158 QPDIIILDEATSMLDPrgrrevlETVRQLKEQ------KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
250 260
....*....|....*....|....
gi 499478341 603 A---------PFAEFYKEHGKTQG 617
Cdd:PRK13635 232 HmlqeigldvPFSVKLKELLKRNG 255
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
399-592 |
2.14e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 83.63 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpempgrprmayvpqeayivntsllenlqFGEEVS 478
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-----------------------------DGKEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 479 KEELRRALhnsclsrdlkewsgglrteigEKGVN----LSGGQKQRVALARAFLRKPQIVLLDDPLSAV-DADTENLLC- 552
Cdd:cd03216 66 FASPRDAR---------------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALtPAEVERLFKv 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499478341 553 -ERLifgAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQ 592
Cdd:cd03216 125 iRRL---RAQGVAVIFISHRLDEVFEIaDRVTVLRDGRVVGT 163
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
398-589 |
2.63e-18 |
|
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: 85.56 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqfvpEMPGRP---------------RMAYVPQEAYI 462
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV----RLAGQDlfaldedararlrarHVGFVFQSFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 VNT-SLLENLQ-----FGEEVSKEELRRALHNSCLSRDLKEWSGGLrteigekgvnlSGGQKQRVALARAFLRKPQIVLL 536
Cdd:COG4181 102 LPTlTALENVMlplelAGRRDARARARALLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 537 DDPLSAVDADTENLLCErLIFGAWKD--VTRIVVTHRLEHLAQFDQVIYIQHGRV 589
Cdd:COG4181 171 DEPTGNLDAATGEQIID-LLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
402-598 |
3.22e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 87.86 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQ-------------FVPemPGRPRMAYVPQEAYIV-NTSL 467
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgiFLP--PEKRRIGYVFQEARLFpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEEVSKEELRRALHNScLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADT 547
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFER-VIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 548 ENLL---CERLifGAWKDVTRIVVTHRL---EHLAqfDQVIYIQHGRVQGQGTFSEL 598
Cdd:TIGR02142 167 KYEIlpyLERL--HAEFGIPILYVSHSLqevLRLA--DRVVVLEDGRVAAAGPIAEV 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
397-601 |
3.66e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.14 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 397 SDVLHDVNVHVPAGSSLAIVGPVGAGKSSLL--MSLLGEVAprEGSLqFVPEMPGRPRMAYV---PQEAYIV-------- 463
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcINKLEEIT--SGDL-IVDGLKVNDPKVDErliRQEAGMVfqqfylfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 NTSLLENLQFG----EEVSKEELRRalhnscLSRDLKEwSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK09493 91 HLTALENVMFGplrvRGASKEEAEK------QARELLA-KVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 540 LSAVDADT--ENLLCERLIfgAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVKT 601
Cdd:PRK09493 164 TSALDPELrhEVLKVMQDL--AEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
383-593 |
3.69e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 84.25 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHdGAVSdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VPEMP-GRPRMAYVPQE 459
Cdd:cd03269 1 LEVENVTKRF-GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgKPLDIaARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 460 AYIV-NTSLLENLQFGEE---VSKEELRRALHNSCLSRDLKEWSgglrteigEKGVN-LSGGQKQRVALARAFLRKPQIV 534
Cdd:cd03269 79 RGLYpKMKVIDQLVYLAQlkgLKKEEARRRIDEWLERLELSEYA--------NKRVEeLSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 535 LLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
400-589 |
4.14e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 84.38 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEMPGRpRMAYVPQEAYIV--------NTSL 467
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngQDVSDLRGR-AIPYLRRKIGVVfqdfrllpDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEEVSKEELRRALHNSCLSRDLKewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADT 547
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELV----GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499478341 548 ENLLCERLIFGAWKDVTRIVVTHRLEHLAQFD-QVIYIQHGRV 589
Cdd:cd03292 172 TWEIMNLLKKINKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
997-1227 |
4.42e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.70 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYAS-HlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTAsvplEKLRRSL- 1074
Cdd:PRK15056 7 IVVNDVTVTWRNgH--TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQD-------PTLF-----------MGTIRnnldRYNEYSDDEVMGALKHASMWDYvqslpdgMNSAVSEgglnLSQ 1136
Cdd:PRK15056 81 AYVPQSeevdwsfPVLVedvvmmgryghMGWLR----RAKKRDRQIVTAALARVDMVEF-------RHRQIGE----LSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1137 GQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFA-GVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRR 1214
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEfCDYTVMVKGTVLASGPT 225
|
250
....*....|...
gi 499478341 1215 PTEFSQEEIEESL 1227
Cdd:PRK15056 226 ETTFTAENLELAF 238
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
997-1209 |
4.74e-18 |
|
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: 84.52 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPL-EKLRRSLA 1075
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDPTLFMG-TIRNNLD---RYNEYSDDEVMGALKHasMWDY--VQSLPDGMnsavsegGLNLSQGQRQLLCLARALL 1149
Cdd:cd03218 79 YLPQEASIFRKlTVEENILavlEIRGLSKKEREEKLEE--LLEEfhITHLRKSK-------ASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1150 TKARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRL-GTIADCDQIVEISAGEV 1209
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVrETLSITDRAYIIYEGKV 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
383-573 |
4.83e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.30 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSD--VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VP-EMPGRPRmAYVP 457
Cdd:COG4525 4 LTVRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgVPvTGPGADR-GVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 458 Q-EAYIVNTSLLENLQFG---EEVSK-EELRRALHNSCLSrdlkewsgGLRtEIGEKGV-NLSGGQKQRVALARAFLRKP 531
Cdd:COG4525 83 QkDALLPWLNVLDNVAFGlrlRGVPKaERRARAEELLALV--------GLA-DFARRRIwQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499478341 532 QIVLLDDPLSAVDADTENLLCErLIFGAWKDVTRIV--VTHRLE 573
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQE-LLLDVWQRTGKGVflITHSVE 196
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
400-598 |
4.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.23 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEM-----------PGRPRMAYVPQ--EAYIVNTS 466
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkPLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENLQFGEE---VSKEE-LRRAlhnsclsrdlKEWSG--GLRTEIGEKG-VNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK13634 103 VEKDICFGPMnfgVSEEDaKQKA----------REMIElvGLPEELLARSpFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 540 LSAVDADTENLLCErlIFGAW---KDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK13634 173 TAGLDPKGRKEMME--MFYKLhkeKGLTTVLVTHSMEDAARYaDQIVVMHKGTVFLQGTPREI 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
383-609 |
5.19e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 85.14 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREG-SLQFVPEMPG-------RPRMA 454
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGgedvwelRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 455 YV-P--QEAYIVNTSLLE--------NLQFGEEVSKEELRRALhnsclsRDLKEWsgGLRTEIGEKGVNLSGGQKQRVAL 523
Cdd:COG1119 82 LVsPalQLRFPRDETVLDvvlsgffdSIGLYREPTDEQRERAR------ELLELL--GLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 524 ARAFLRKPQIVLLDDPLSAVD-ADTENLLceRLI--FGAWKDVTRIVVTHRLE-HLAQFDQVIYIQHGRVQGQGTFSElV 599
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDlGARELLL--ALLdkLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEE-V 230
|
250
....*....|
gi 499478341 600 KTCAPFAEFY 609
Cdd:COG1119 231 LTSENLSEAF 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
399-618 |
5.68e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPR-MAYVPQE-AYIVNTSLLENLQ 472
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdVSRLHARDRkVGFVFQHyALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 473 FGEEV--SKEELRRALHNSCLSRDLKEWSggLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTEN- 549
Cdd:PRK10851 97 FGLTVlpRRERPNAAAIKAKVTQLLEMVQ--LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKe 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 550 ------LLCERLIFgawkdvTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVKTCAP-FA-EFYKEHGKTQGE 618
Cdd:PRK10851 175 lrrwlrQLHEELKF------TSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQVWREPATrFVlEFMGEVNRLQGT 246
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
997-1217 |
7.69e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.07 E-value: 7.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDP-TLFMG-TIRNN----LDRyNEYSDDE----VMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLAR 1146
Cdd:PRK13635 86 VFQNPdNQFVGaTVQDDvafgLEN-IGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1147 ALLTKARVIVMDEATASVDVQTDALLQKVIRT--SFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE 1217
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
410-593 |
7.95e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 83.50 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 410 GSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------------VPemPGRPRMAYVPQEAYIV-NTSLLENLQFGE 475
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrkkinLP--PQQRKIGLVFQQYALFpHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 476 EVSKEELRRALHNSCLsrDLKEWSGGLRTEIGEkgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERL 555
Cdd:cd03297 101 KRKRNREDRISVDELL--DLLGLDHLLNRYPAQ----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499478341 556 -----IFGawkdVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03297 175 kqikkNLN----IPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
997-1217 |
1.85e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 82.55 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASvPLEKLRRSLAI 1076
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMG-TIRNNLdryneysddEVMGALKHASMWDY---------VQSLPDGMNSAVSegglNLSQGQRQLLCLAR 1146
Cdd:cd03263 80 CPQFDALFDElTVREHL---------RFYARLKGLPKSEIkeevelllrVLGLTDKANKRAR----TLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1147 ALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTI-ADCDQIVEISAGEVKSIRRPTE 1217
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
997-1207 |
2.42e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 81.88 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTaSVPLEKLRRSLAI 1076
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IpQDPTLFMG-TIRNNL---DRYNEYSDDEVMGALkhasmwDYVqslpdGMNSAVSEGGLNLSQGQRQLLCLARALLTKA 1152
Cdd:cd03268 78 I-EAPGFYPNlTARENLrllARLLGIRKKRIDEVL------DVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1153 RVIVMDEATASVDVQTDALLQKVIRtSFA--GVTMLIIAHRLGTIAD-CDQIVEISAG 1207
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELIL-SLRdqGITVLISSHLLSEIQKvADRIGIINKG 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
997-1218 |
2.85e-17 |
|
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: 82.73 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVlKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLF--MgTIRNN---LDRYNEYSD-------DEVMgALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCL 1144
Cdd:cd03295 80 VIQQIGLFphM-TVEENialVPKLLKWPKekireraDELL-ALVGLDPAEFADRYPH-----------ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1145 ARALLTKARVIVMDEATASVDVQTDALLQKVIRT--SFAGVTMLIIAH------RLGtiadcDQIVEISAGEVKSIRRPT 1216
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHdideafRLA-----DRIAIMKNGEIVQVGTPD 221
|
..
gi 499478341 1217 EF 1218
Cdd:cd03295 222 EI 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
400-589 |
3.86e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLL----------------MSLLGEVAPREGSLQfVPEMPGRPRMAYVPQEAYIV 463
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgdksagshIELLGRTVQREGRLA-RDIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 NT-SLLENLQFGEEVSKEELRRALhnSCLSRDLKEWSGGLRTEIG------EKGVNLSGGQKQRVALARAFLRKPQIVLL 536
Cdd:PRK09984 99 NRlSVLENVLIGALGSTPFWRTCF--SWFTREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 537 DDPLSAVDADTENLLCERLIFGAWKDVTRIVVT-HRLEHLAQF-DQVIYIQHGRV 589
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYALRYcERIVALRQGHV 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
396-593 |
5.29e-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: 81.00 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 396 VSDVLHDVNVH----VPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEMP--GRPrMAYVPQEAYI-VN 464
Cdd:cd03298 6 IRFSYGEQPMHfdltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingVDVTAAPpaDRP-VSMLFQENNLfAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 TSLLENLQFGEEVS---KEELRRALHnSCLSRdlkewsGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLS 541
Cdd:cd03298 85 LTVEQNVGLGLSPGlklTAEDRQAIE-VALAR------VGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 542 AVD-ADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQ-FDQVIYIQHGRVQGQG 593
Cdd:cd03298 158 ALDpALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
997-1222 |
5.60e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDP-TLFMGTI---------RNNLDRYNEYSdDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLAR 1146
Cdd:PRK13648 88 VFQNPdNQFVGSIvkydvafglENHAVPYDEMH-RRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1147 ALLTKARVIVMDEATASVDVQTDALLQKVIR--TSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE-FSQEE 1222
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEiFDHAE 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
399-593 |
6.29e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 80.72 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRprmayvPQEAYIVNTSLLENLQFGEEVS 478
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK------NIEALRRIGALIEAPGFYPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 479 KEE----------LRRALHNSCLSRdlkewsGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADte 548
Cdd:cd03268 89 AREnlrllarllgIRKKRIDEVLDV------VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD-- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499478341 549 NLLCERLIFGAWKD--VTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03268 161 GIKELRELILSLRDqgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
383-585 |
7.22e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpemPGRPRMAYVP----- 457
Cdd:PRK10247 8 LQLQNVGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF----EGEDISTLKPeiyrq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 458 QEAYIVNTSLLenlqFGEEVSKE-----ELRR-ALHNSCLSRDLKEWsgGLRTEIGEKGVN-LSGGQKQRVALARAFLRK 530
Cdd:PRK10247 82 QVSYCAQTPTL----FGDTVYDNlifpwQIRNqQPDPAIFLDDLERF--ALPDTILTKNIAeLSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 531 PQIVLLDDPLSAVDADTE---NLLCERLIfgAWKDVTRIVVTHRLEHLAQFDQVIYIQ 585
Cdd:PRK10247 156 PKVLLLDEITSALDESNKhnvNEIIHRYV--REQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
997-1204 |
7.27e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYA------SHLPQVLK---GITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP- 1066
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1067 --LEKLRRSLAIIPQDPtlfMG------TIRNNLDryneysddEVM---GALKHASMWDYVQSLPDgmnsAVsegGLN-- 1133
Cdd:COG4608 88 reLRPLRRRMQMVFQDP---YAslnprmTVGDIIA--------EPLrihGLASKAERRERVAELLE----LV---GLRpe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1134 --------LSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDA----LLQKvIRTSFaGVTMLIIAHRLGT---IAD- 1197
Cdd:COG4608 150 hadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAqvlnLLED-LQDEL-GLTYLFISHDLSVvrhISDr 227
|
250
....*....|..
gi 499478341 1198 -----CDQIVEI 1204
Cdd:COG4608 228 vavmyLGKIVEI 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
399-589 |
7.52e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 80.65 E-value: 7.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-----------VPEMpgRPRMAYVPQEAYIV-NTS 466
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdglkltddkknINEL--RQKVGMVFQQFNLFpHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENLQFG------------EEVSKEELRRAlhnsclsrdlkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIV 534
Cdd:cd03262 93 VLENITLApikvkgmskaeaEERALELLEKV---------------GLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 535 LLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLehlaQF-----DQVIYIQHGRV 589
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEM----GFarevaDRVIFMDDGRI 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
383-597 |
8.25e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF---VpempgrpRMAYVPQ- 458
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgetV-------KIGYFDQh 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 459 -EAYIVNTSLLENL-QFGEEVSKEELRRALHNSCLSRDLkewsggLRTEIGekgvNLSGGQKQRVALARAFLRKPQIVLL 536
Cdd:COG0488 387 qEELDPDKTVLDELrDGAPGGTEQEVRGYLGRFLFSGDD------AFKPVG----VLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 537 DDPLSAVDADTENLLCERLI-F-GawkdvTRIVVTH-R--LEHLAqfDQVIYIQHGRVQG-QGTFSE 597
Cdd:COG0488 457 DEPTNHLDIETLEALEEALDdFpG-----TVLLVSHdRyfLDRVA--TRILEFEDGGVREyPGGYDD 516
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
400-577 |
9.42e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 9.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLL-----MSLLGEVAPREGSLQF---------VPEMPGRPRMAYVPQEAYIVNT 465
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFhgknlyapdVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 SLLENLQFGEEVS------KEELRRALHNSCLSRDLKEwsgglrtEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK14243 106 SIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 499478341 540 LSAVDAdTENLLCERLIFGAWKDVTRIVVTHRLEHLAQ 577
Cdd:PRK14243 179 CSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQQAAR 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1006-1207 |
1.16e-16 |
|
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: 80.45 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1006 YASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKL----RRSLAIIPQDP 1081
Cdd:cd03290 10 WGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1082 TLFMGTIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEAT 1161
Cdd:cd03290 89 WLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499478341 1162 ASVDVQ-TDALLQKVIRTSFAG--VTMLIIAHRLGTIADCDQIVEISAG 1207
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1013-1190 |
1.29e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGV------NTASVPLEKLRRSLAIIPQDPTLF-- 1084
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1085 ---MGTIRNNLDRYNEYSDDEVMG----ALKHASMWDYVQslpDGMNSAVSEgglnLSQGQRQLLCLARALLTKARVIVM 1157
Cdd:PRK14246 105 lsiYDNIAYPLKSHGIKEKREIKKiveeCLRKVGLWKEVY---DRLNSPASQ----LSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190
....*....|....*....|....*....|...
gi 499478341 1158 DEATASVDVQTDALLQKVIRTSFAGVTMLIIAH 1190
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
999-1211 |
1.37e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 999 VEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntasvpleKLRrsLAIIP 1078
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1079 QDPTLFMG-TIRNN-----------LDRYNE-------YSDD-----EVMGALKHASMWDY---VQSLPDGM-------N 1124
Cdd:COG0488 68 QEPPLDDDlTVLDTvldgdaelralEAELEEleaklaePDEDlerlaELQEEFEALGGWEAearAEEILSGLgfpeedlD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1125 SAVSEgglnLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRtSFAGvTMLIIAHrlgtiaD------- 1197
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK-NYPG-TVLVVSH------Dryfldrv 215
|
250
....*....|....
gi 499478341 1198 CDQIVEISAGEVKS 1211
Cdd:COG0488 216 ATRILELDRGKLTL 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1012-1209 |
1.62e-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: 79.13 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSL--FRFIEAEEGSISIDGVNtasVPLEKLRRSLAIIPQD----PTLfm 1085
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDdilhPTL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1086 gTIRNNLdryneysddevmgalkhasmwdyvqslpdgMNSAVSEGglnLSQGQRQLLCLARALLTKARVIVMDEATASVD 1165
Cdd:cd03213 98 -TVRETL------------------------------MFAAKLRG---LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499478341 1166 VQTDALLQKVIRT-SFAGVTMLIIAHRLGT--IADCDQIVEISAGEV 1209
Cdd:cd03213 144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
399-544 |
1.94e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqfvpEMPGRPRMAYVPQEAYIVNTSLLENLQFgeevs 478
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLRIGYVPQKLYLDTTLPLTVNRF----- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 479 kEELRRALHNSCLSRDLKEWSGG-LRTEIGEKgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:PRK09544 90 -LRLRPGTKKEDILPALKRVQAGhLIDAPMQK---LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
399-594 |
2.07e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.54 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpemPGRP-----------RMAYVPQEAyivntsl 467
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL----NGRPlaawspwelarRRAVLPQHS------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 leNLQFG---EEV-----------SKEELRRALHnsCLSR-DLKEWSGGLRTEigekgvnLSGGQKQRVALARAFL---- 528
Cdd:COG4559 85 --SLAFPftvEEVvalgraphgssAAQDRQIVRE--ALALvGLAHLAGRSYQT-------LSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 529 ---RKPQIVLLDDPLSAVDadtenLLCERLIFGAWKDVTR-----IVVTHRLEHLAQF-DQVIYIQHGRVQGQGT 594
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALD-----LAHQHAVLRLARQLARrgggvVAVLHDLNLAAQYaDRILLLHQGRLVAQGT 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
997-1223 |
2.11e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.59 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:PRK13548 3 LEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTL-FMGTIRnnldryneysddEV--MGALKHASMWDYVQSLPDGMNSAVSEGGL------NLSQGQRQLLCLARA 1147
Cdd:PRK13548 81 LPQHSSLsFPFTVE------------EVvaMGRAPHGLSRAEDDALVAAALAQVDLAHLagrdypQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1148 L--LTKA----RVIVMDEATASVDV--QtdallQKVIRT--SFA---GVTMLIIAHRLG-TIADCDQIVEISAGEVKSIR 1213
Cdd:PRK13548 149 LaqLWEPdgppRWLLLDEPTSALDLahQ-----HHVLRLarQLAherGLAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
250
....*....|
gi 499478341 1214 RPTEFSQEEI 1223
Cdd:PRK13548 224 TPAEVLTPET 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
383-588 |
2.12e-16 |
|
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: 77.10 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGavSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpemPGRPRMAYVPQeayi 462
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----GSTVKIGYFEQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 vntsllenlqfgeevskeelrralhnsclsrdlkewsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSA 542
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499478341 543 VDADTENLLCERLIfgAWKDvTRIVVTHRLEHLAQF-DQVIYIQHGR 588
Cdd:cd03221 101 LDLESIEALEEALK--EYPG-TVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
76-308 |
2.43e-16 |
|
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: 80.92 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAG-VTAETLPTALIYGVALGLCGFLSGLCMQHYFFNSlkAYQVTTNILNeRLFKHSLK 154
Cdd:cd18541 9 ILVDLLQLLIPRIIGRAIDALTAGtLTASQLLRYALLILLLALLIGIFRFLWRYLIFGA--SRRIEYDLRN-DLFAHLLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 155 LSQKSRQKNQVGDIVNHMSSDSDNVSdfpMVFGD----LISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLTNYVA 229
Cdd:cd18541 86 LSPSFYQKNRTGDLMARATNDLNAVR---MALGPgilyLVDALFLGVLVLVMMF-TISPKlTLIALLPLPLLALLVYRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 230 KKFTHLDEEMMEHRDrRVTLMTQ-AMNAIRVVKYFAWEKSV----AKEVTEVREKELtsrrRLAKAE--------VVSSL 296
Cdd:cd18541 162 KKIHKRFRKVQEAFS-DLSDRVQeSFSGIRVIKAFVQEEAEierfDKLNEEYVEKNL----RLARVDalffpligLLIGL 236
|
250
....*....|..
gi 499478341 297 GYLavstLVLFV 308
Cdd:cd18541 237 SFL----IVLWY 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
399-594 |
2.64e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRpRMAYVPQEAYIVNT-----------SL 467
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM----LDGQ-DITHVPAENRHVNTvfqsyalfphmTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFG---EEVSKEELRRALHNSCLSRDLKEWSGglrteigEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:PRK09452 104 FENVAFGlrmQKTPAAEITPRVMEALRMVQLEEFAQ-------RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 545 ADTENLLCERLifgawKDVTR------IVVTH-RLEHLAQFDQVIYIQHGRVQGQGT 594
Cdd:PRK09452 177 YKLRKQMQNEL-----KALQRklgitfVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
383-600 |
3.00e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 79.40 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpempGRPRMAYVPQE--- 459
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD----GEDITGLPPHEiar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 460 AYIVNT----------SLLENLQFGEEVSKEELRRALHNSCLSRDLKEWSG------GLRTEIGEKGVNLSGGQKQRVAL 523
Cdd:cd03219 75 LGIGRTfqiprlfpelTVLENVMVAAQARTGSGLLLARARREEREARERAEellervGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 524 ARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVK 600
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
399-601 |
4.00e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.62 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE-MPGRPRMA-----YVPQ-EAYIVNTSLLENL 471
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpVPSRARHArqrvgVVPQfDNLDPDFTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 Q-----FGeeVSKEELRRALHNsclsrdLKEWSGgLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDAD 546
Cdd:PRK13537 102 LvfgryFG--LSAAAARALVPP------LLEFAK-LENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 547 TENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVKT 601
Cdd:PRK13537 173 ARHLMWERLRSLLARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
399-599 |
4.09e-16 |
|
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: 79.90 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLL------GEVAPREGSLQFVPEMPGRPRMAYVPQEAYIVNTSLLENLQ 472
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 473 FGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLc 552
Cdd:cd03289 99 PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVI- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499478341 553 ERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELV 599
Cdd:cd03289 178 RKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
981-1209 |
5.57e-16 |
|
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: 82.42 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 981 KPLPEPLRPTWPEFgeISVEGLKVRY----------ASHLPQVlKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEA 1050
Cdd:COG4172 262 RGDPRPVPPDAPPL--LEARDLKVWFpikrglfrrtVGHVKAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1051 eEGSISIDGVNTASVP---LEKLRRSLAIIPQDPtlF----------------MGTIRNNLDRynEYSDDEVMGALKHas 1111
Cdd:COG4172 339 -EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FgslsprmtvgqiiaegLRVHGPGLSA--AERRARVAEALEE-- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1112 mwdyVQSLPDGMNSAVSEgglnLSQGQRQLLCLARALLTKARVIVMDEATASVDV----QTDALLQKVIRTsfAGVTMLI 1187
Cdd:COG4172 412 ----VGLDPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVsvqaQILDLLRDLQRE--HGLAYLF 481
|
250 260
....*....|....*....|...
gi 499478341 1188 IAHRLGTI-ADCDQIVEISAGEV 1209
Cdd:COG4172 482 ISHDLAVVrALAHRVMVMKDGKV 504
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
997-1209 |
6.13e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAI 1076
Cdd:PRK13647 5 IEVEDLHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDP--TLFMGTIRN-------NLDRYNEYSDDEVMGALKHASMWDYVQSLPdgmnsavseggLNLSQGQRQLLCLARA 1147
Cdd:PRK13647 84 VFQDPddQVFSSTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1148 LLTKARVIVMDEATASVDVQTDALLQKVI-RTSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRV 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
398-589 |
7.05e-16 |
|
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: 78.08 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVapREGSLQ----FVPEMPGRP-----RMAYVPQEAYIVNT-SL 467
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTsgqiLFNGQPRKPdqfqkCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQF-----GEEVSKEELRRALHNSCLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSA 542
Cdd:cd03234 99 RETLTYtailrLPRKSSDAIRKKRVEDVLLRDL-----ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499478341 543 VDADTENLLCERLIFGAWKDVTRIVVTH--RLEHLAQFDQVIYIQHGRV 589
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
400-587 |
7.27e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 78.28 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEmPGRPRMAyVPQeayivNTSLLENLQFGE 475
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVilegKQITE-PGPDRMV-VFQ-----NYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 476 EVskeelrrALHNSCLSRDLKEWSG-----------GLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:TIGR01184 74 NI-------ALAVDRVLPDLSKSERraiveehialvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499478341 545 ADTENLLCERLIfGAWKD--VTRIVVTHRL-EHLAQFDQVIYIQHG 587
Cdd:TIGR01184 147 ALTRGNLQEELM-QIWEEhrVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
398-593 |
7.34e-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: 77.21 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG--EVAPREGSLQF----VPEMPGRPRMAYVPQEayivnTSLLENL 471
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLIngrpLDKRSFRKIIGYVPQD-----DILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 QfgeevskeeLRRALHNSCLSRdlkewsgglrteigekgvNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLL 551
Cdd:cd03213 98 T---------VRETLMFAAKLR------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499478341 552 CERLIFGAWKDVTRIVVTHRL--EHLAQFDQVIYIQHGRVQGQG 593
Cdd:cd03213 151 MSLLRRLADTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
383-598 |
8.29e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpemPGRP-------RMAY 455
Cdd:COG4152 2 LELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW----DGEPldpedrrRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQEA--YiVNTSLLENLQF-----GeeVSKEELRRAlhnsclsrdLKEWsggL-RTEIGE---KGV-NLSGGQKQRVAL 523
Cdd:COG4152 76 LPEERglY-PKMKVGEQLVYlarlkG--LSKAEAKRR---------ADEW---LeRLGLGDranKKVeELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 524 ARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFG-AWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELL-KDVIRElAAKGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
997-1222 |
9.06e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQ-VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLA 1075
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDP-TLFMGTIrnnldryneYSDDEVMG----ALKHASMWDYVQSLPD--GMNSAVSEGGLNLSQGQRQLLCLARAL 1148
Cdd:PRK13650 85 MVFQNPdNQFVGAT---------VEDDVAFGlenkGIPHEEMKERVNEALElvGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1149 LTKARVIVMDEATASVDVQTD-ALLQKV--IRTSFaGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE-FSQEE 1222
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRlELIKTIkgIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSRGN 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
997-1191 |
9.26e-16 |
|
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: 76.04 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntasvpleklRRSLAI 1076
Cdd:cd03223 1 IELENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMGTIRnnldryneysddevmGALKHAsmWDYVqslpdgmnsavsegglnLSQGQRQLLCLARALLTKARVIV 1156
Cdd:cd03223 69 LPQRPYLPLGTLR---------------EQLIYP--WDDV-----------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 499478341 1157 MDEATASVDVQTDALLQKVIRTsfAGVTMLIIAHR 1191
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
399-594 |
1.30e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 77.73 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-----------VPEMpgRPRMAYVPQeayivNTSL 467
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdgedltdskkdINKL--RRKVGMVFQ-----QFNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 ------LENLQFGEE----VSKEELR-RALHNsclsrdLKewsgglRTEIGEKG----VNLSGGQKQRVALARAFLRKPQ 532
Cdd:COG1126 89 fphltvLENVTLAPIkvkkMSKAEAEeRAMEL------LE------RVGLADKAdaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 533 IVLLDDPLSAVD----ADTENLLcERLifgAWKDVTRIVVTHRLehlaQF-----DQVIYIQHGRVQGQGT 594
Cdd:COG1126 157 VMLFDEPTSALDpelvGEVLDVM-RDL---AKEGMTMVVVTHEM----GFarevaDRVVFMDGGRIVEEGP 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-598 |
1.50e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSL--LGEVAPR---------EGSLQF---VPEMPGRPRMAY-VPQEayI 462
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvsgevylDGQDIFkmdVIELRRRVQMVFqIPNP--I 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 VNTSLLENLQFGEEV-----SKEEL----RRALHNSCLSRDLKEwsgglrtEIGEKGVNLSGGQKQRVALARAFLRKPQI 533
Cdd:PRK14247 95 PNLSIFENVALGLKLnrlvkSKKELqervRWALEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 534 VLLDDPLSAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK14247 168 LLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
404-606 |
1.69e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.31 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 404 NVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE-----MPGRPRMAYVPQEAYIVN-TSLLENLQFG--- 474
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSRRPVSMLFQENNLFShLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 475 ----EEVSKEELRRALHN----SCLSRdlkewsggLRTEigekgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD-- 544
Cdd:PRK10771 99 glklNAAQREKLHAIARQmgieDLLAR--------LPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 545 --ADTENLL---CERlifgawKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVKTCAPFA 606
Cdd:PRK10771 164 lrQEMLTLVsqvCQE------RQLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLSGKASAS 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1012-1223 |
1.90e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.20 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASVPLEKLRRSLAIIPQDP--TLFMGT 1087
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1088 IRN-------NLDRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEA 1160
Cdd:PRK13639 96 VEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1161 TASVDVQ-TDALLQKVIRTSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTE-FSQEEI 1223
Cdd:PRK13639 165 TSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEvFSDIET 230
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
76-359 |
2.11e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 78.32 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSP----VFVNRFIGTISAGVtaetlPTALIYGVALGLCG---FLSGLCMQHYFFNSLKAYQVTTNILNeRL 148
Cdd:cd18563 9 LLGTALGLVPPyltkILIDDVLIQLGPGG-----NTSLLLLLVLGLAGayvLSALLGILRGRLLARLGERITADLRR-DL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 149 FKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFpMVFG--DLISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLT 225
Cdd:cd18563 83 YEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDF-LSDGlpDFLTNILMIIGIGVVLF-SLNWKlALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 226 NYVAKKFTHldeemMEHR-DRRVTLMTQAMN----AIRVVKYFAWEKsvaKEVTEVREKELTSRRRLAKAEVVSSLGYLA 300
Cdd:cd18563 161 YFFWKKIRR-----LFHRqWRRWSRLNSVLNdtlpGIRVVKAFGQEK---REIKRFDEANQELLDANIRAEKLWATFFPL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 301 VSTLV---LFVALAVHAWR--GEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18563 233 LTFLTslgTLIVWYFGGRQvlSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
997-1192 |
2.20e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE-----EGSISIDGVNTASVPLE--K 1069
Cdd:PRK14239 6 LQVSDLSVYYNKK--KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDtvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 LRRSLAIIPQDPTLFMGTIRNNLD---RYNEYSDDEVMGA-----LKHASMWDYVQSlpdgmnsAVSEGGLNLSQGQRQL 1141
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVyglRLKGIKDKQVLDEaveksLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1142 LCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRL 1192
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1014-1190 |
2.28e-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: 76.29 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1014 LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKLRRSLAIIPQDPTLFMG-TIR 1089
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQDFRLLPDrNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1090 NNLDRYNEYSD-------DEVMGALKHASMWDYVQSLPDGmnsavsegglnLSQGQRQLLCLARALLTKARVIVMDEATA 1162
Cdd:cd03292 97 ENVAFALEVTGvppreirKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190
....*....|....*....|....*....|..
gi 499478341 1163 SVDVQTDA----LLQKVirtSFAGVTMLIIAH 1190
Cdd:cd03292 166 NLDPDTTWeimnLLKKI---NKAGTTVVVATH 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
997-1227 |
2.56e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.78 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLP---QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTA--SVPLEKLR 1071
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLAIIPQDP--TLFMGTIRN-------NLDryneYSDDEVMGALKHA------SMWDYVQSLPdgmnsavseggLNLSQ 1136
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKdiafgpiNLG----LSEEEIENRVKRAmnivglDYEDYKDKSP-----------FELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1137 GQRQLLCLARALLTKARVIVMDEATASVDVQT-DALLQKV--IRTSFaGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSI 1212
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrDEILNKIkeLHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQ 226
|
250
....*....|....*.
gi 499478341 1213 RRPTE-FSQEEIEESL 1227
Cdd:PRK13637 227 GTPREvFKEVETLESI 242
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
76-359 |
2.88e-15 |
|
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: 77.85 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGVTAETL---PTALIyGVAL--GLCGFLSGLCMQHyffnslkayqVTTNILN---ER 147
Cdd:cd18552 9 ILVAATTAALAWLLKPLLDDIFVEKDLEALllvPLAII-GLFLlrGLASYLQTYLMAY----------VGQRVVRdlrND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 148 LFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSD-FPMVFGDLISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLT 225
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGLLGVLF-YLDWKlTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 226 NYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSS-----LGYLA 300
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSplmelLGAIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 301 VSTLVLFVALAVHAwrgEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18552 237 IALVLWYGGYQVIS---GELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
997-1210 |
3.00e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIdGVNTasvpleklrrSLAI 1076
Cdd:COG0488 316 LELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQ-----DPTLfmgTIRNNLDRYNEYSDDevmgalKHASmwDYVQSL---PDGMNSAVSegglNLSQGQRQLLCLARAL 1148
Cdd:COG0488 383 FDQhqeelDPDK---TVLDELRDGAPGGTE------QEVR--GYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1149 LTKARVIVMDEAT-----ASVDVQTDALLqkvirtSFAGvTMLIIAH-R--LGTIadCDQIVEISAGEVK 1210
Cdd:COG0488 448 LSPPNVLLLDEPTnhldiETLEALEEALD------DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
996-1193 |
3.08e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.93 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 996 EISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASV---------- 1065
Cdd:PRK10619 5 KLNVIDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1066 ---PLEKLRRSLAIIPQDPTL--FMGTIRNNLDryneySDDEVMGALKHASMWDYVQSLPD-GMN-SAVSEGGLNLSQGQ 1138
Cdd:PRK10619 83 dknQLRLLRTRLTMVFQHFNLwsHMTVLENVME-----APIQVLGLSKQEARERAVKYLAKvGIDeRAQGKYPVHLSGGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1139 RQLLCLARALLTKARVIVMDEATASVDVQtdaLLQKVIRT----SFAGVTMLIIAHRLG 1193
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRImqqlAEEGKTMVVVTHEMG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
383-589 |
3.16e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.00 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSL--LGEVAPR---EGSLQF-----------VPE 446
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLdgediydpdvdVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 447 MpgRPRMAYVPQEAyivN---TSLLENLQFG----EEVSKEEL----RRALHNSCLSRDLKEwsgglrtEIGEKGVNLSG 515
Cdd:COG1117 90 L--RRRVGMVFQKP---NpfpKSIYDNVAYGlrlhGIKSKSELdeivEESLRKAALWDEVKD-------RLKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 516 GQKQRVALARAFLRKPQIVLLDDPLSAVD----ADTENLLCE-RlifgawKDVTRIVVTHRLEHLAQF-DQVIYIQHGRV 589
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILElK------KDYTIVIVTHNMQQAARVsDYTAFFYLGEL 231
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
76-359 |
3.17e-15 |
|
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: 77.47 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGvtaETLPTALIYGVALGLCG-FLSGLcmQHYFFNSLKAYQVTTniLNERLFKHSLK 154
Cdd:cd18551 9 LLGTAASLAQPLLVKNLIDALSAG---GSSGGLLALLVALFLLQaVLSAL--SSYLLGRTGERVVLD--LRRRLWRRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 155 LSQKSRQKNQVGDIVNHMSSDSDNVSDFP-MVFGDLISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLTNYVAKKF 232
Cdd:cd18551 82 LPVSFFDRRRSGDLVSRVTNDTTLLRELItSGLPQLVTGVLTVVGAVVLMF-LLDWVlTLVTLAVVPLAFLIILPLGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 233 THLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAE-VVSSLGYLAVsTLVLFVALA 311
Cdd:cd18551 161 RKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEaLIGPLMGLAV-QLALLVVLG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 312 VHAWR---GEkLDAA--VIFtCISLFGLLeGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18551 240 VGGARvasGA-LTVGtlVAF-LLYLFQLI-TPLSQLSSFFTQLQKALGALERI 289
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
997-1192 |
3.54e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.05 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLP---QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRS 1073
Cdd:COG1101 2 LELKNLSKTFNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPTlfMGT-----IRNNL------------------DRYNEYSDdevmgALKHASMwdyvqSLPDGMNSAVseg 1130
Cdd:COG1101 82 IGRVFQDPM--MGTapsmtIEENLalayrrgkrrglrrgltkKRRELFRE-----LLATLGL-----GLENRLDTKV--- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1131 GLnLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALL----QKVIRTSfaGVTMLIIAHRL 1192
Cdd:COG1101 147 GL-LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN--NLTTLMVTHNM 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
387-547 |
3.65e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 76.32 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 387 HFSLRH-DGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqFVPEMPGR-------PR------ 452
Cdd:COG4778 13 TFTLHLqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-LVRHDGGWvdlaqasPReilalr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 ---MAYVPQ--------EAY-IVNTSLLEnLQFGEEVSKEELRRALHNSCLSRDLkeWSGGLRTeigekgvnLSGGQKQR 520
Cdd:COG4778 92 rrtIGYVSQflrviprvSALdVVAEPLLE-RGVDREEARARARELLARLNLPERL--WDLPPAT--------FSGGEQQR 160
|
170 180
....*....|....*....|....*..
gi 499478341 521 VALARAFLRKPQIVLLDDPLSAVDADT 547
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAAN 187
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
399-608 |
3.82e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEMPGRPR-MAYVPQE-AYIVNTSLLENLQ 472
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgEDVTHRSIQQRdICMVFQSyALFPHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 473 FG---EEVSKEELRRALHNSCLSRDLkewsGGLrteiGEKGVN-LSGGQKQRVALARAFLRKPQIVLLDDPLSAVDAdte 548
Cdd:PRK11432 101 YGlkmLGVPKEERKQRVKEALELVDL----AGF----EDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDA--- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 549 NL----------LCERLifgawkDVTRIVVTH-RLEHLAQFDQVIYIQHGRVQGQGTFSELVKTcaPFAEF 608
Cdd:PRK11432 170 NLrrsmrekireLQQQF------NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ--PASRF 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
997-1210 |
6.08e-15 |
|
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: 74.92 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSrVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPlEKLRRSLAI 1076
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMG-TIRNNLDrY--------NEYSDDEVMGALKHASMWDYVqslpdgmNSAVSEgglnLSQGQRQLLCLARA 1147
Cdd:cd03264 77 LPQEFGVYPNfTVREFLD-YiawlkgipSKEVKARVDEVLELVNLGDRA-------KKKIGS----LSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1148 LLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVK 1210
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLV 208
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
678-966 |
7.06e-15 |
|
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: 76.66 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILA-TLLLGATAATLLP--LAQKAWLSYYSGHQTEWVALTAIGIygLIGVLVLVGSLLNHL--FWLDR-GIRAGKNMHD 751
Cdd:cd18544 1 FILAlLLLLLATALELLGplLIKRAIDDYIVPGQGDLQGLLLLAL--LYLGLLLLSFLLQYLqtYLLQKlGQRIIYDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 752 KMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESV-DVYlqwsfdSAVhcALQVIVSIVLILGL----------MPLMVFVI 820
Cdd:cd18544 79 DLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALnELF------TSG--LVTLIGDLLLLIGIliamfllnwrLALISLLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 821 APVMALY-YVLQRDYRRPAREVKRfdSVARSprYAHFKESLQGLVVIRSFNKGPWFMQNFYAklsHSNRMFYSHVMINRW 899
Cdd:cd18544 151 LPLLLLAtYLFRKKSRKAYREVRE--KLSRL--NAFLQESISGMSVIQLFNREKREFEEFDE---INQEYRKANLKSIKL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 900 FSSRIPLVGGLISMATAVGVSLSAYYGVMDAGTAGlvTLYSlsfwgFLNWGVRIF------AD----IESRMTSIER 966
Cdd:cd18544 224 FALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG--VLYA-----FIQYIQRFFrpirdlAEkfniLQSAMASAER 293
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
383-593 |
7.14e-15 |
|
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: 74.92 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSsLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG--RPRMAYV 456
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdVLKQPQklRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQE-AYIVNTSLLENLQFG---EEVS----KEELRRALHNSCLSRDLKEwsgglrtEIGEkgvnLSGGQKQRVALARAFL 528
Cdd:cd03264 78 PQEfGVYPNFTVREFLDYIawlKGIPskevKARVDEVLELVNLGDRAKK-------KIGS----LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 529 RKPQIVLLDDPLSAVDADtENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03264 147 GDPSILIVDEPTAGLDPE-ERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
397-612 |
8.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 397 SDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfVPEM------------PGRPRMAYVPQ--EAYI 462
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVT-VGDIvvsstskqkeikPVRKKVGVVFQfpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 VNTSLLENLQFGEE---VSKEELRRalhnscLSRDLKEWSGgLRTEIGEKG-VNLSGGQKQRVALARAFLRKPQIVLLDD 538
Cdd:PRK13643 98 FEETVLKDVAFGPQnfgIPKEKAEK------IAAEKLEMVG-LADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 539 PLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVIY-IQHGRVQGQGTFSELVKTcapfAEFYKEH 612
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYlLEKGHIISCGTPSDVFQE----VDFLKAH 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
400-593 |
1.01e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfVPEMPGRPRM-----AYVPQEAYiVNTS---LLENL 471
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS-ILGQPTRQALqknlvAYVPQSEE-VDWSfpvLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 ----QFGE----EVSKEELRRALHNSCLSRDLKEWSgglRTEIGEkgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAV 543
Cdd:PRK15056 101 vmmgRYGHmgwlRRAKKRDRQIVTAALARVDMVEFR---HRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 544 DADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQG 593
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1011-1192 |
1.12e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.67 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1011 PQVLK---GITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG---VNTASVPLEKLRRSLAIIPQDP--- 1081
Cdd:PRK15079 31 PKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDPlas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1082 ---TLFMGTIRNNLDR--YNEYSDDEVMGALKhaSMWDYVQSLPDGMNSAVSEgglnLSQGQRQLLCLARALLTKARVIV 1156
Cdd:PRK15079 111 lnpRMTIGEIIAEPLRtyHPKLSRQEVKDRVK--AMMLKVGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499478341 1157 MDEATASVDVQTDA----LLQKVIRTsfAGVTMLIIAHRL 1192
Cdd:PRK15079 185 CDEPVSALDVSIQAqvvnLLQQLQRE--MGLSLIFIAHDL 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
400-599 |
1.14e-14 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 75.76 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEMPG-------RPRMAYVPQE-AYIVNTSL 467
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgQDIAAMSRkelrelrRKKISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEEVS----KEELRRALHnsCLSR-DLKEWSGGLRTEigekgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSA 542
Cdd:cd03294 120 LENVAFGLEVQgvprAEREERAAE--ALELvGLEGWEHKYPDE-------LSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 543 VD----ADTENLLcerLIFGAWKDVTRIVVTHRL-EHLAQFDQVIYIQHGRVQGQGTFSELV 599
Cdd:cd03294 191 LDplirREMQDEL---LRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
399-598 |
1.31e-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: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----------VPEMPG-----RPRMAYVPQEAYIV 463
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKGlirqlRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 -NTSLLENLQFGEEVSKEELRRALhnSCLSRDL--------KEWSGGLRteigekgvnLSGGQKQRVALARAFLRKPQIV 534
Cdd:PRK11264 98 pHRTVLENIIEGPVIVKGEPKEEA--TARARELlakvglagKETSYPRR---------LSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 535 LLDDPLSAVDADT--ENLLCERLIfgAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK11264 167 LFDEPTSALDPELvgEVLNTIRQL--AQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKAL 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1009-1208 |
1.40e-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: 75.66 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1009 HLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntasvpleklrrSLAIIPQDPTLFMGTI 1088
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1089 RNNLD---RYNEYSDDEVMGALKhasMWDYVQSLPDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVD 1165
Cdd:cd03291 115 KENIIfgvSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499478341 1166 VQTDA-LLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGE 1208
Cdd:cd03291 192 VFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
997-1223 |
1.40e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKST---FFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRS 1073
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDP-TLFMGTIrnnldryneYSDDEVMG-----------------ALKHASMWDYVQSLPDgmnsavsegglNLS 1135
Cdd:PRK13640 86 VGIVFQNPdNQFVGAT---------VGDDVAFGlenravprpemikivrdVLADVGMLDYIDSEPA-----------NLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1136 QGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIR--TSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIR 1213
Cdd:PRK13640 146 GGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
250
....*....|.
gi 499478341 1214 RPTE-FSQEEI 1223
Cdd:PRK13640 226 SPVEiFSKVEM 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1021-1202 |
1.41e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 74.07 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1021 VEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEklRRSLAIIPQDPTLFMG-TIRNNLD------ 1093
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGlglspg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1094 -RYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALL 1172
Cdd:cd03298 99 lKLTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190
....*....|....*....|....*....|..
gi 499478341 1173 QKVIRTSFA--GVTMLIIAHRLGTIADCDQIV 1202
Cdd:cd03298 168 LDLVLDLHAetKMTVLMVTHQPEDAKRLAQRV 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
998-1209 |
1.52e-14 |
|
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: 73.24 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 998 SVEGLKVRYAshlpqvLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVN-TASVPLEKLRRSLAI 1076
Cdd:cd03215 6 EVRGLSVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPT---LFMG-TIRNNLdryneysddeVMGALkhasmwdyvqslpdgmnsavsegglnLSQGQRQLLCLARALLTKA 1152
Cdd:cd03215 80 VPEDRKregLVLDlSVAENI----------ALSSL--------------------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1153 RVIVMDEATASVDVQTDALLQKVIR-TSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIReLADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
399-600 |
1.98e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.02 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE-MPGRPRMA-----YVPQ-EAYIVNTSLLENL 471
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpVPARARLArarigVVPQfDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 -QFGE--EVSKEELRRALHNsclsrdLKEWSGgLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTE 548
Cdd:PRK13536 136 lVFGRyfGMSTREIEAVIPS------LLEFAR-LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 549 NLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVK 600
Cdd:PRK13536 209 HLIWERLRSLLARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
997-1217 |
1.99e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 73.94 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPlEKLRRSLAI 1076
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMG-TIRNNLdryneysddEVMGAL----------KHASMWDYVQsLPDGMNSAVSegglNLSQGQRQLLCLA 1145
Cdd:cd03265 78 VFQDLSVDDElTGWENL---------YIHARLygvpgaerreRIDELLDFVG-LLEAADRLVK----TYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1146 RALLTKARVIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIAHRLGTiAD--CDQIVEISAGEVKSIRRPTE 1217
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEE-AEqlCDRVAIIDHGRIIAEGTPEE 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
402-597 |
2.14e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQ-------------FVPemPGRPRMAYVPQEA-----YIV 463
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlfdaekgiCLP--PEKRRIGYVFQDArlfphYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 NTslleNLQFG-EEVSKEELRRALhnSCLSRD--LKEWSGglrteigekgvNLSGGQKQRVALARAFLRKPQIVLLDDPL 540
Cdd:PRK11144 94 RG----NLRYGmAKSMVAQFDKIV--ALLGIEplLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 541 SAVDADTENLL---CERLIfgawKDV-TRIV-VTHRLE---HLAqfDQVIYIQHGRVQGQGTFSE 597
Cdd:PRK11144 157 ASLDLPRKRELlpyLERLA----REInIPILyVSHSLDeilRLA--DRVVVLEQGKVKAFGPLEE 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-589 |
2.65e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.11 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSL-----LGEVAPREGSLQ------FVPEMPG---RPRMAYVPQEAY-IV 463
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRlfgrniYSPDVDPievRREVGMVFQYPNpFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 NTSLLENLQFGEEV-----SKEEL----RRALHNSCLSRDLKEwsgglrtEIGEKGVNLSGGQKQRVALARAFLRKPQIV 534
Cdd:PRK14267 99 HLTIYDNVAIGVKLnglvkSKKELdervEWALKKAALWDEVKD-------RLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 535 LLDDPLSAVD-ADTENLlcERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRV 589
Cdd:PRK14267 172 LMDEPTANIDpVGTAKI--EELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKL 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
398-598 |
3.13e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 74.10 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpemPGRP-------------RMAYvpQEAyivN 464
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILI----NGHKleygdykyrckhiRMIF--QDP---N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 TSLLENLQFGEEVSkEELRRalhNSCLS---RDLKEWSG----GLRTEIGEKGVN-LSGGQKQRVALARAFLRKPQIVLL 536
Cdd:COG4167 98 TSLNPRLNIGQILE-EPLRL---NTDLTaeeREERIFATlrlvGLLPEHANFYPHmLSSGQKQRVALARALILQPKIIIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 537 DDPLSAVDADTE----NLLCE---RLifgawkDVTRIVVTHRL---EHLAqfDQVIYIQHGRVQGQGTFSEL 598
Cdd:COG4167 174 DEALAALDMSVRsqiiNLMLElqeKL------GISYIYVSQHLgivKHIS--DKVLVMHQGEVVEYGKTAEV 237
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
997-1227 |
4.29e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.97 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYA--SHLPQvLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSL 1074
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDP-TLFMG-TIRN-------NLDRYNEYSDDEVMGALKHASMWDYVQSLPdgmnsavseggLNLSQGQRQLLCLA 1145
Cdd:PRK13642 84 GMVFQNPdNQFVGaTVEDdvafgmeNQGIPREEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1146 RALLTKARVIVMDEATASVDVQTDALLQKVIR--TSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTEF---SQ 1220
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELfatSE 232
|
....*..
gi 499478341 1221 EEIEESL 1227
Cdd:PRK13642 233 DMVEIGL 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1013-1222 |
5.50e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP-LEKLRRSLAIIPQDP-TLFMGTI-- 1088
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdNQIVATIve 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1089 ------RNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEATA 1162
Cdd:PRK13633 105 edvafgPENLGIPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1163 SVDVQTDALLQKVIR--TSFAGVTMLIIAHRLGTIADCDQIVEISAGEVKSIRRPTE-FSQEE 1222
Cdd:PRK13633 174 MLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEiFKEVE 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
995-1217 |
5.78e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.72 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFI----EAEEGSISIDGVNTASVPLEKl 1070
Cdd:COG3839 2 ASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIagleDPTSGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1071 rRSLAIIPQDPTLF--MgTIRNNLD---RYNEYSDDEVMGALKHAS----MWDYVQSLPDgmnsavsegglNLSQGQRQL 1141
Cdd:COG3839 75 -RNIAMVFQSYALYphM-TVYENIAfplKLRKVPKAEIDRRVREAAellgLEDLLDRKPK-----------QLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1142 LCLARALLTKARVIVMDEATASVD----VQTDALLQKVIRTSfaGVTMLIIAH------RLGtiadcDQIVEISAGEVKS 1211
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL--GTTTIYVTHdqveamTLA-----DRIAVMNDGRIQQ 214
|
....*.
gi 499478341 1212 IRRPTE 1217
Cdd:COG3839 215 VGTPEE 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
997-1223 |
5.98e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntASVP--LEKLRRSL 1074
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG---EPVPsrARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQ----DPTLfmgTIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEgglnLSQGQRQLLCLARALLT 1150
Cdd:PRK13537 83 GVVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1151 KARVIVMDEATASVDVQTDALLQKVIRTSFA-GVTMLIIAH------RLgtiadCDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
383-598 |
6.12e-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: 72.54 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-----VPEMPG-RPRMAYV 456
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngysiRTDRKAaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQEAYIVNT-SLLENLQF-----GeeVSKEELRRALHNSCLSRDLKEWsggLRTEIGekgvNLSGGQKQRVALARAFLRK 530
Cdd:cd03263 81 PQFDALFDElTVREHLRFyarlkG--LPKSEIKEEVELLLRVLGLTDK---ANKRAR----TLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 531 PQIVLLDDPLSAVDADTENLLCeRLIFGAWKDVTRIVVTHRL---EHLAqfDQVIYIQHGRVQGQGTFSEL 598
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIW-DLILEVRKGRSIILTTHSMdeaEALC--DRIAIMSDGKLRCIGSPQEL 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
399-599 |
6.98e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 76.74 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRPRMAY-----------VPQEAYIVNTSL 467
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR----VNGREIGAYglrelrrqfsmIPQDPVLFDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQ-IVLLDDPLSAVDAD 546
Cdd:PTZ00243 1401 RQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPA 1480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 547 TENLLcERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELV 599
Cdd:PTZ00243 1481 LDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1012-1222 |
7.14e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.62 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPL-EKLRRSLAIIPQDPTLFMG-TIR 1089
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1090 NNLDRYNEYSDDevMGALKHASMWD------YVQSLPDGMnsavsegGLNLSQGQRQLLCLARALLTKARVIVMDEATAS 1163
Cdd:PRK10895 97 DNLMAVLQIRDD--LSAEQREDRANelmeefHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1164 VDVQTDALLQKVI---RTSFAGVtmLIIAHRL-GTIADCDQIVEISAGEVKSIRRPTEFSQEE 1222
Cdd:PRK10895 168 VDPISVIDIKRIIehlRDSGLGV--LITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1012-1193 |
7.68e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASVPLEKLRRSLAIIPQDPTLF--MGT 1087
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEAGMVFQQFYLFphLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1088 IRNNLdryneYSDDEVMGALKHAS------MWDYVqSLPDGMNSAVSEgglnLSQGQRQLLCLARALLTKARVIVMDEAT 1161
Cdd:PRK09493 95 LENVM-----FGPLRVRGASKEEAekqareLLAKV-GLAERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 499478341 1162 ASVDVQtdaLLQKVIRT--SFA--GVTMLIIAHRLG 1193
Cdd:PRK09493 165 SALDPE---LRHEVLKVmqDLAeeGMTMVIVTHEIG 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
394-611 |
8.29e-14 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 72.33 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 394 GAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPEMPGRPRMAYVPQEAYIV--- 463
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdgedireQDPVELRRKIGYVIQQIGLFphm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 ----NTSLLENLQ-FGEEVSKEELRRALHnsCLSRDLKEWSGGLRTEigekgvnLSGGQKQRVALARAFLRKPQIVLLDD 538
Cdd:cd03295 91 tveeNIALVPKLLkWPKEKIRERADELLA--LVGLDPAEFADRYPHE-------LSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 539 PLSAVDADTENLLCERLI-----FGAwkdvTRIVVTHRLEH---LAqfDQVIYIQHGRVQGQGTFSELVKTCAP--FAEF 608
Cdd:cd03295 162 PFGALDPITRDQLQEEFKrlqqeLGK----TIVFVTHDIDEafrLA--DRIAIMKNGEIVQVGTPDEILRSPANdfVAEF 235
|
...
gi 499478341 609 YKE 611
Cdd:cd03295 236 VGA 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
399-555 |
8.39e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.24 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRPRMAYVPQEAYIVNT-------SLLENL 471
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLpglkpelSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 QFGEEVSKEElRRALHNSCLSRDLkewsgglrTEIGEKGVN-LSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENL 550
Cdd:TIGR01189 95 HFWAAIHGGA-QRTIEDALAAVGL--------TGFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
....*
gi 499478341 551 LCERL 555
Cdd:TIGR01189 166 LAGLL 170
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
997-1209 |
8.67e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.07 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQV--LKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFI----EAEEGSISIDGVNTASVP---L 1067
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKST----LIRCInlleRPTSGRVLVDGQDLTALSekeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1068 EKLRRSLAIIPQDptlFmgtirNNLDRYNEYsdDEVMGALKHAsmwdyvqslpdGMNSA-----VSE----GGL------ 1132
Cdd:PRK11153 78 RKARRQIGMIFQH---F-----NLLSSRTVF--DNVALPLELA-----------GTPKAeikarVTEllelVGLsdkadr 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1133 ---NLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTD----ALLQKVIRTsfAGVTMLIIAHRLGTIAD-CDQIVEI 1204
Cdd:PRK11153 137 ypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTrsilELLKDINRE--LGLTIVLITHEMDVVKRiCDRVAVI 214
|
....*
gi 499478341 1205 SAGEV 1209
Cdd:PRK11153 215 DAGRL 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1013-1223 |
8.83e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVntaSVPLEK--LRRSLAIIPQDPTLFMG-TIR 1089
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---PVPARArlARARIGVVPQFDNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1090 NNL---DRYNEYSDDEVMGALkhASMWDYVQsLPDGMNSAVSEgglnLSQGQRQLLCLARALLTKARVIVMDEATASVDV 1166
Cdd:PRK13536 133 ENLlvfGRYFGMSTREIEAVI--PSLLEFAR-LESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1167 QTDALLQKVIRTSFA-GVTMLIIAH------RLgtiadCDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:PRK13536 206 HARHLIWERLRSLLArGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
399-544 |
9.99e-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: 72.19 E-value: 9.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEMP--GRPR--MAYVPQEAYI-----VNT 465
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgQDITKLPmhKRARlgIGYLPQEASIfrkltVEE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 466 SLLENLQFGEEVSKEELRRALHnscLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:cd03218 95 NILAVLEIRGLSKKEREEKLEE---LLEEF-----HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
399-556 |
1.02e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRP----RMAYV-PQEAYIVNTSLLENLQF 473
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPdvaeACHYLgHRNAMKPALTVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 474 GEEVskeelrRALHNSCLSRDLKEWsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLcE 553
Cdd:PRK13539 97 WAAF------LGGEELDIAAALEAV--GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF-A 167
|
...
gi 499478341 554 RLI 556
Cdd:PRK13539 168 ELI 170
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
383-598 |
1.08e-13 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 72.85 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----------VPEMpgRPR 452
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdgldtldeenLWEI--RKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 MAYVPQ--EAYIVNTSLLENLQFGEE---VSKEELRRALHNSCLSRDLKEWsggLRTEigekGVNLSGGQKQRVALARAF 527
Cdd:TIGR04520 79 VGMVFQnpDNQFVGATVEDDVAFGLEnlgVPREEMRKRVDEALKLVGMEDF---RDRE----PHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 528 LRKPQIVLLDDPLSAVDADT--------ENLLCErlifgawKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGrkevletiRKLNKE-------EGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
400-589 |
1.12e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.94 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL-----QFVPEMPG------RPRMAYVPQ--EAYIVNTS 466
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyHITPETGNknlkklRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENLQFGEE---VSKEELRRALhnsclsrdlKEW--SGGLRTEIGEKG-VNLSGGQKQRVALARAFLRKPQIVLLDDPL 540
Cdd:PRK13641 103 VLKDVEFGPKnfgFSEDEAKEKA---------LKWlkKVGLSEDLISKSpFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499478341 541 SAVDADTENLLCErlIFGAWKDV--TRIVVTHRLEHLAQF-DQVIYIQHGRV 589
Cdd:PRK13641 174 AGLDPEGRKEMMQ--LFKDYQKAghTVILVTHNMDDVAEYaDDVLVLEHGKL 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
387-545 |
1.17e-13 |
|
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: 73.55 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 387 HFSLRhDGAVSdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPR---EGSLQF----VPEMPGR-------PR 452
Cdd:COG0444 10 YFPTR-RGVVK-AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFdgedLLKLSEKelrkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 MAYVPQEAYivnTSL----------LENLQFGEEVSKEELR-RAlhnsclsRDLKEwSGGLRTEigEKGVN-----LSGG 516
Cdd:COG0444 88 IQMIFQDPM---TSLnpvmtvgdqiAEPLRIHGGLSKAEAReRA-------IELLE-RVGLPDP--ERRLDrypheLSGG 154
|
170 180
....*....|....*....|....*....
gi 499478341 517 QKQRVALARAFLRKPQIVLLDDPLSAVDA 545
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDV 183
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
997-1209 |
1.24e-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: 73.98 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFR----FIEAEEGSISIDGVNTASVPLEKlrR 1072
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLDGRDVTGLPPEK--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1073 SLAIIPQDPTLF--MgTIRNN---------LDRynEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQL 1141
Cdd:COG3842 78 NVGMVFQDYALFphL-TVAENvafglrmrgVPK--AEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1142 LCLARALLTKARVIVMDEATASVDVQT--------DALLQKVirtsfaGVTMLIIAHRLG---TIAdcDQIVEISAGEV 1209
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLreemreelRRLQREL------GITFIYVTHDQEealALA--DRIAVMNDGRI 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
992-1223 |
1.39e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 992 PEFGEI--SVEGLKVRyashlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASvPL 1067
Cdd:COG1129 250 AAPGEVvlEVEGLSVG------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRS-PR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1068 EKLRRSLAIIPQDPT---LFMG-TIRNNLdryneysddeVMGALKHASMW-------------DYVQSL---PDGMNSAV 1127
Cdd:COG1129 323 DAIRAGIAYVPEDRKgegLVLDlSIRENI----------TLASLDRLSRGglldrrreralaeEYIKRLrikTPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1128 SegglNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRtSFA--GVTMLII------AHRLgtiadCD 1199
Cdd:COG1129 393 G----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIR-ELAaeGKAVIVIsselpeLLGL-----SD 462
|
250 260
....*....|....*....|....
gi 499478341 1200 QIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:COG1129 463 RILVMREGRIVGELDREEATEEAI 486
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
399-604 |
1.49e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMP------GRPRMAYVPQE-AYIVNTSL 467
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdgenIPAMSrsrlytVRKRMSMLFQSgALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEEVSKEELRRALHNSCLsrdLKEWSGGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADT 547
Cdd:PRK11831 102 FDNVAYPLREHTQLPAPLLHSTVM---MKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 548 ENLLCeRLI--FGAWKDVTRIVVTHRL-EHLAQFDQVIYIQHGRVQGQGTFSELVKTCAP 604
Cdd:PRK11831 179 MGVLV-KLIseLNSALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANPDP 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
997-1209 |
2.14e-13 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 71.27 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFIEAEE-----GSISIDGVNTASVPLEKLR 1071
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGDLpptygNDVRLFGERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLAI--------IPQDPTL-------FMGTIrnnlDRYNEYSDDEVMGALKHASMWDyVQSLPD-GMNSavsegglnLS 1135
Cdd:COG1119 78 KRIGLvspalqlrFPRDETVldvvlsgFFDSI----GLYREPTDEQRERARELLELLG-LAHLADrPFGT--------LS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1136 QGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTsFAG---VTMLIIAHRLGTIADC-DQIVEISAGEV 1209
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDK-LAAegaPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
399-593 |
2.24e-13 |
|
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: 71.21 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRPRMAYVPQEAYIV--------NTSLLEN 470
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgqktqlwwDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 471 LQFGEEVSKEELRRAlhnsclSRDLKEWSGGLR-TEIGEKGV-NLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTE 548
Cdd:cd03267 116 FYLLAAIYDLPPARF------KKRLDELSELLDlEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499478341 549 NLLCERL-IFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03267 190 ENIRNFLkEYNRERGTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
997-1209 |
2.33e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.94 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP-LEKLRRSLA 1075
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDP-TLFMG-------------------TIRNNLDRyneysddevmgALKHASMWDYVQSLPDgmnsavsegglNLS 1135
Cdd:PRK13644 81 IVFQNPeTQFVGrtveedlafgpenlclppiEIRKRVDR-----------ALAEIGLEKYRHRSPK-----------TLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1136 QGQRQLLCLARALLTKARVIVMDEATASVDVQT-DALLQKVIRTSFAGVTMLIIAHRLGTIADCDQIVEISAGEV 1209
Cdd:PRK13644 139 GGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
997-1217 |
2.34e-13 |
|
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: 71.11 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKlrRSLAI 1076
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLF--MGTIRN-----NLDRYNEYS-DDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARAL 1148
Cdd:cd03300 77 VFQNYALFphLTVFENiafglRLKKLPKAEiKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1149 LTKARVIVMDEATASVDVQTDALLQ---KVIRTSFaGVTMLIIAHRLG-TIADCDQIVEISAGEVKSIRRPTE 1217
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKEL-GITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
383-600 |
2.44e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.75 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpEMPG-----------RP 451
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKI-TVDGitltaktvwdiRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 452 RMAYVPQ--EAYIVNTSLLENLQFGEE---VSKEELRRALHNSCLSRDLKEWsgglrteIGEKGVNLSGGQKQRVALARA 526
Cdd:PRK13640 85 KVGIVFQnpDNQFVGATVGDDVAFGLEnraVPRPEMIKIVRDVLADVGMLDY-------IDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 527 FLRKPQIVLLDDPLSAVD-ADTENLLceRLIFGAWKD--VTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVK 600
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDpAGKEQIL--KLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
399-598 |
2.72e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.42 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLL--MSLLgEVaPREGSLqfvpempgrprmayvpqeayIVNtsllenlqfGEE 476
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLL-ER-PTSGSV--------------------LVD---------GVD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 477 V---SKEELRRA------------LHNSCLSRD-----LkEWSGGLRTEIGEKgVN------------------LSGGQK 518
Cdd:COG1135 69 LtalSERELRAArrkigmifqhfnLLSSRTVAEnvalpL-EIAGVPKAEIRKR-VAellelvglsdkadaypsqLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 519 QRVALARAFLRKPQIVLLDDPLSAVDAD-TENLLceRLIfgawKDVTR------IVVTHRLE---HLAqfDQVIYIQHGR 588
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPEtTRSIL--DLL----KDINRelgltiVLITHEMDvvrRIC--DRVAVLENGR 218
|
250
....*....|
gi 499478341 589 VQGQGTFSEL 598
Cdd:COG1135 219 IVEQGPVLDV 228
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
76-359 |
2.94e-13 |
|
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: 71.65 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGVTAET---LPTALIYGVALGLCGFLSGLcmQHYFFNSLkAYQVTTNIlNERLFKHS 152
Cdd:cd18544 9 LLATALELLGPLLIKRAIDDYIVPGQGDLqglLLLALLYLGLLLLSFLLQYL--QTYLLQKL-GQRIIYDL-RRDLFSHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 153 LKLSQKSRQKNQVGDIVNHMSSDSDNVSD-FPMVFGDLISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLTNYVAK 230
Cdd:cd18544 85 QRLPLSFFDRTPVGRLVTRVTNDTEALNElFTSGLVTLIGDLLLLIGILIAMF-LLNWRlALISLLVLPLLLLATYLFRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 231 KFthldeemmehRD--RRVTLMTQAMNA--------IRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAE-----VVSS 295
Cdd:cd18544 164 KS----------RKayREVREKLSRLNAflqesisgMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFalfrpLVEL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 296 LGYLAVSTLVLFVALAVHAwrgEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18544 234 LSSLALALVLWYGGGQVLS---GAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1013-1189 |
3.24e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNtasVPLEKLRRSLAII-PQD---PTLfmgTI 1088
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNamkPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1089 RNNLD---RYNEYSDDEVMGALKHASMWDyVQSLPDGMnsavsegglnLSQGQRQLLCLARALLTKARVIVMDEATASVD 1165
Cdd:PRK13539 91 AENLEfwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....
gi 499478341 1166 VQTDALLQKVIRTSFAGVTMLIIA 1189
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAA 183
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
400-594 |
3.64e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPEMPG-RPRMAYVPQ--EAYIVNTSLLE 469
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtgdFSKLQGiRKLVGIVFQnpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFGEE---VSKEELRRALhnsclSRDLKEWsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDAD 546
Cdd:PRK13644 98 DLAFGPEnlcLPPIEIRKRV-----DRALAEI--GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499478341 547 TENLLCERLIFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGT 594
Cdd:PRK13644 171 SGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
383-600 |
4.38e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.94 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPG-------RPRMAY 455
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddnfeklRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 VPQ--EAYIVNTSLLENLQFGEE---VSKEELRRALHNSCLSRDLKEWSGglrteigEKGVNLSGGQKQRVALARAFLRK 530
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLEnhaVPYDEMHRRVSEALKQVDMLERAD-------YEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 531 PQIVLLDDPLSAVDADT-ENLLceRLI--FGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVK 600
Cdd:PRK13648 161 PSVIILDEATSMLDPDArQNLL--DLVrkVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
399-555 |
4.56e-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: 69.44 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRPRMAYVPQEAYIVNT-------SLLENL 471
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHApgikttlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 QFGEEV-SKEELRRALHNSCLsrdlkewsgglrTEIGEKGVN-LSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTEN 549
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGL------------NGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*.
gi 499478341 550 LLCERL 555
Cdd:cd03231 163 RFAEAM 168
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
76-359 |
4.85e-13 |
|
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: 71.28 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGVTAET---LPTALIYGVALGLCGFLSGLCM--QHYFFNslKAYQVTTNILNERLFK 150
Cdd:cd18547 9 IISTLLSVLGPYLLGKAIDLIIEGLGGGGgvdFSGLLRILLLLLGLYLLSALFSylQNRLMA--RVSQRTVYDLRKDLFE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 151 HSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDF-PMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVA 229
Cdd:cd18547 87 KLQRLPLSYFDTHSHGDIMSRVTNDVDNISQAlSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 230 KK----FthldeemmehRDRRVTL------MTQAMNAIRVVKYFAWEKSVAKEVTEVREkELtsRRRLAKAEVVSS---- 295
Cdd:cd18547 167 KRsqkyF----------RKQQKALgelngyIEEMISGQKVVKAFNREEEAIEEFDEINE-EL--YKASFKAQFYSGllmp 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 296 -------LGYLAV----STLVLFVALAVhawrgekldaAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18547 234 imnfinnLGYVLVavvgGLLVINGALTV----------GVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
383-598 |
4.98e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRH-DGavSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE---------MPGRPR 452
Cdd:PRK13636 6 LKVEELNYNYsDG--THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 MAYVPQEA--YIVNTSLLENLQFGE---EVSKEELRRALHNScLSRDlkewsgGLRTEIGEKGVNLSGGQKQRVALARAF 527
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAvnlKLPEDEVRKRVDNA-LKRT------GIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 528 LRKPQIVLLDDPLSAVDADTENLLCERLIFGAWK-DVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
997-1223 |
5.77e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.65 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASVPLEKLRRSL 1074
Cdd:PRK13636 6 LKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDP--TLFMGTIrnnldrYNEYS---------DDEVMGALKHASMWDYVQSLPDGMNSAvsegglnLSQGQRQLLC 1143
Cdd:PRK13636 85 GMVFQDPdnQLFSASV------YQDVSfgavnlklpEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1144 LARALLTKARVIVMDEATASVD-VQTDALLQKVIRTSFA-GVTMLIIAHRLGTIA-DCDQIVEISAGEVKSIRRPTE-FS 1219
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEvFA 231
|
....
gi 499478341 1220 QEEI 1223
Cdd:PRK13636 232 EKEM 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
402-573 |
6.53e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEMP--GRPRMAYVPQEAYIVNTSLLENLQFG- 474
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgVDLSHVPpyQRPINMMFQSYALFPHMTVEQNIAFGl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 475 --EEVSKEELRRALHNSCLSRDLKEWSGglrteigEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDA---DTEN 549
Cdd:PRK11607 117 kqDKLPKAEIASRVNEMLGLVHMQEFAK-------RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrDRMQ 189
|
170 180
....*....|....*....|....*...
gi 499478341 550 L----LCERLifgawkDVTRIVVTHRLE 573
Cdd:PRK11607 190 LevvdILERV------GVTCVMVTHDQE 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
400-599 |
6.84e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFV-------PEMPGRPRMAYVPQEA--YIVNTSLLEN 470
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMgrevnaeNEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 471 LQFG---EEVSKEELRRALHNSCLSRDLKEWSgglrteigEKG-VNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDAD 546
Cdd:PRK13647 101 VAFGpvnMGLDKDEVERRVEEALKAVRMWDFR--------DKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 547 TENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELV 599
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVATHDVDLAAEWaDQVIVLKEGRVLAEGDKSLLT 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1012-1197 |
9.69e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG----VNTASVPLEKLRRSLAIIPQDP--TLFM 1085
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQFPeaQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1086 GTIRNNLD---RYNEYSDDEvmgALKHASMWDYVQSLPDGMnsaVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATA 1162
Cdd:PRK13641 101 NTVLKDVEfgpKNFGFSEDE---AKEKALKWLKKVGLSEDL---ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 499478341 1163 SVDVQT-DALLQKVIRTSFAGVTMLIIAHRLGTIAD 1197
Cdd:PRK13641 175 GLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAE 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
399-618 |
1.01e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.14 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG--EVAPREGSLQF------------VPEMPGRP------------- 451
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvalcekcgyveRPSKVGEPcpvcggtlepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 452 ---------------RMAYVPQEAYIV--NTSLLENL-----QFGEEvSKEELRRALhnsclsrDLKEWSGgLRTEIGEK 509
Cdd:TIGR03269 95 dfwnlsdklrrrirkRIAIMLQRTFALygDDTVLDNVlealeEIGYE-GKEAVGRAV-------DLIEMVQ-LSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 510 GVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFGAW-KDVTRIVVTHRLEHLAQF-DQVIYIQHG 587
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVIEDLsDKAIWLENG 245
|
250 260 270
....*....|....*....|....*....|..
gi 499478341 588 RVQGQGTFSELV-KTCAPFAEFYKEHGKTQGE 618
Cdd:TIGR03269 246 EIKEEGTPDEVVaVFMEGVSEVEKECEVEVGE 277
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
400-573 |
1.09e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSL--LGEVAPR---EGSLQF---------VPEMPGRPRMAYVPQEAYIVNT 465
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYnghniysprTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 SLLENLQFGEEVS----KEELRRALHNSCLSRDLkeWSGgLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLS 541
Cdd:PRK14239 101 SIYENVVYGLRLKgikdKQVLDEAVEKSLKGASI--WDE-VKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|..
gi 499478341 542 AVDADTENLLcERLIFGAWKDVTRIVVTHRLE 573
Cdd:PRK14239 178 ALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
76-359 |
1.11e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 70.15 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFI-GTISAGVTAETLPTALIY-GVAL--GLCGFLSGlcmqhYFFNSLkAYQVTTNILNeRLFKH 151
Cdd:cd18542 9 LLATALNLLIPLLIRRIIdSVIGGGLRELLWLLALLIlGVALlrGVFRYLQG-----YLAEKA-SQKVAYDLRN-DLYDH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 152 SLKLSQKSRQKNQVGDIVNHMSSDSDNVSDF-PMVFGDLISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLTNYVA 229
Cdd:cd18542 82 LQRLSFSFHDKARTGDLMSRCTSDVDTIRRFlAFGLVELVRAVLLFIGALIIMF-SINWKlTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 230 KKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKS----VAKEVTEVREKELTSRRRLAKaevvsslgYLAVSTLV 305
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYeiekFDKENEEYRDLNIKLAKLLAK--------YWPLMDFL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 306 LFVALAVHAW-------RGE-KLDAAVIFtcISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18542 233 SGLQIVLVLWvggylviNGEiTLGELVAF--ISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
997-1192 |
1.14e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYAsHLPQVLkgiTFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVN-TASVPlekLRRSLA 1075
Cdd:PRK10771 2 LKLTDITWLYH-HLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPP---SRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDPTLFMG-TIRNNLD-------RYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARA 1147
Cdd:PRK10771 75 MLFQENNLFSHlTVAQNIGlglnpglKLNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499478341 1148 LLTKARVIVMDEATASVD----VQTDALLQKVIRTSfaGVTMLIIAHRL 1192
Cdd:PRK10771 144 LVREQPILLLDEPFSALDpalrQEMLTLVSQVCQER--QLTLLMVSHSL 190
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1029-1221 |
1.20e-12 |
|
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: 70.60 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1029 IIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEklRRSLAIIPQDPTLF--MGTIRN--------NLDRynEY 1098
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFphMTVEENvafglkmrKVPR--AE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1099 SDDEVMGALKHASMWDYVQSLPdgmnsavseggLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRT 1178
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499478341 1179 --SFAGVTMLIIAH-RLGTIADCDQIVEISAGEVKSIRRPTEFSQE 1221
Cdd:TIGR01187 146 iqEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1002-1212 |
1.29e-12 |
|
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: 68.48 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1002 LKVRYASHLPQVLKGITFKVEaGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGV----NTASVPLEKLRRSLAII 1077
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1078 PQDPTLF--MgTIRNNLdrynEYsddeVMGALKHASMWDYVQSLPDGMN--SAVSEGGLNLSQGQRQLLCLARALLTKAR 1153
Cdd:cd03297 81 FQQYALFphL-NVRENL----AF----GLKRKRNREDRISVDELLDLLGldHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIR---TSFaGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSI 1212
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKqikKNL-NIPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
399-593 |
1.32e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRP-----------RMAYVPQEayivnTSL 467
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL----VAGDDvealsaraasrRVASVPQD-----TSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEEVskeELRRALHNSCLSRDLKEWSGGLRTEIGEKGV---------NLSGGQKQRVALARAFLRKPQIVLLDD 538
Cdd:PRK09536 89 SFEFDVRQVV---EMGRTPHRSRFDTWTETDRAAVERAMERTGVaqfadrpvtSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 539 PLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
997-1209 |
1.48e-12 |
|
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: 68.08 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPleklRRSLAI 1076
Cdd:cd03269 1 LEVENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFMG-TIRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAVSEgglnLSQGQRQLLCLARALLTKARVI 1155
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1156 VMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
399-544 |
1.48e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE----MP----GRPRMAYVPQEAYI-----VNT 465
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdislLPlharARRGIGYLPQEASIfrrlsVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 SLLENLQFGEEVSKE-------ELRRALHNSCLSRDLkewsgglrteigekGVNLSGGQKQRVALARAFLRKPQIVLLDD 538
Cdd:PRK10895 98 NLMAVLQIRDDLSAEqredranELMEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLDE 163
|
....*.
gi 499478341 539 PLSAVD 544
Cdd:PRK10895 164 PFAGVD 169
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1013-1196 |
1.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEA-----EEGSISIDGVNTASV-PLEKLRRSLAIIPQDPTLFMG 1086
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 TIRNNL----DRYNEYSDDEVMGA----LKHASMWDYVQSlpdgmnsAVSEGGLNLSQGQRQLLCLARALLTKARVIVMD 1158
Cdd:PRK14271 116 SIMDNVlagvRAHKLVPRKEFRGVaqarLTEVGLWDAVKD-------RLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 499478341 1159 EATASVDVQTDALLQKVIRTSFAGVTMLIIAHRLGTIA 1196
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAA 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
400-600 |
1.53e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.69 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGS--------------LQFVpempgRPRMAYVPQ--EAYIV 463
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditdkkvkLSDI-----RKKVGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 NTSLLENLQFG-------EEVSKEELRRALHNSCLSRD-LKEWSGglrteigekgVNLSGGQKQRVALARAFLRKPQIVL 535
Cdd:PRK13637 98 EETIEKDIAFGpinlglsEEEIENRVKRAMNIVGLDYEdYKDKSP----------FELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 536 LDDPLSAVDADT-ENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVK 600
Cdd:PRK13637 168 LDEPTAGLDPKGrDEILNKIKELHKEYNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFK 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
997-1190 |
1.59e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASVPLEK----L 1070
Cdd:PRK11124 3 IQLNGINCFYGAH--QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDKaireL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1071 RRSLAIIPQD----PTLfmgTIRNNLD----RYNEYSDDEV----MGALKHASMWDYVQSLPdgmnsavseggLNLSQGQ 1138
Cdd:PRK11124 81 RRNVGMVFQQynlwPHL---TVQQNLIeapcRVLGLSKDQAlaraEKLLERLRLKPYADRFP-----------LHLSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1139 RQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAH 1190
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTH 199
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
383-594 |
1.77e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRH-DGAVS-DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPRMAYV 456
Cdd:PRK11629 6 LQCDNLCKRYqEGSVQtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngqpMSKLSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 PQEAYIV--------NTSLLEN----LQFGEEVSKEELRRALHNsclsrdLKewSGGLRTEIGEKGVNLSGGQKQRVALA 524
Cdd:PRK11629 86 NQKLGFIyqfhhllpDFTALENvampLLIGKKKPAEINSRALEM------LA--AVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 525 RAFLRKPQIVLLDDPLSAVDADTENLLCERL-IFGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGT 594
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
386-600 |
1.81e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 69.25 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 386 QHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpempgrprmayvpqeayivnt 465
Cdd:PRK13632 11 ENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI---------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 sllenlqFGEEVSKEELRRA---------------------------LHNSCLSR-DLKEWSGGLRTEIGEKGV------ 511
Cdd:PRK13632 69 -------DGITISKENLKEIrkkigiifqnpdnqfigatveddiafgLENKKVPPkKMKDIIDDLAKKVGMEDYldkepq 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 512 NLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLI-FGAWKDVTRIVVTHRLEHLAQFDQVIYIQHGRVQ 590
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
250
....*....|
gi 499478341 591 GQGTFSELVK 600
Cdd:PRK13632 222 AQGKPKEILN 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
399-593 |
1.85e-12 |
|
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: 67.94 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQ--------------FVPEMPGRprmayvpqeayivn 464
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgrvssllglgggFNPELTGR-------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 tsllENLQF-----GeeVSKEELRRALHnsclsrDLKEWSgglrtEIGEKG----VNLSGGQKQRVALARAFLRKPQIVL 535
Cdd:cd03220 103 ----ENIYLngrllG--LSRKEIDEKID------EIIEFS-----ELGDFIdlpvKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 536 LDDPLSAVDADTENlLCERLIFGAWKD-VTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03220 166 IDEVLAVGDAAFQE-KCQRRLRELLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
399-600 |
1.96e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.57 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQ--------------FVPEMPGRprmayvpqeayivn 464
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngrvsallelgagFHPELTGR-------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 tsllENLQF-----GeeVSKEELRRALhnsclsRDLKEWSgglrtEIGE------KgvNLSGGQKQRVALARAFLRKPQI 533
Cdd:COG1134 107 ----ENIYLngrllG--LSRKEIDEKF------DEIVEFA-----ELGDfidqpvK--TYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 534 VLLDDPLSAVDADTENlLCERLIFGAWKDVTRIV-VTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVK 600
Cdd:COG1134 168 LLVDEVLAVGDAAFQK-KCLARIRELRESGRTVIfVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1012-1209 |
2.02e-12 |
|
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: 67.94 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvnTASVPLEKlrrSLAIIPQ----DPTLFMGT 1087
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--RVSSLLGL---GGGFNPEltgrENIYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1088 IRNnldryneYSDDEVmgalkhASMWDYVQS---LPDGMNSAVSegglNLSQGQRQLLCLARALLTKARVIVMDEATASV 1164
Cdd:cd03220 111 LLG-------LSRKEI------DEKIDEIIEfseLGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499478341 1165 DVQTDALLQKVIRTSFAGVTMLIIA-HRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKI 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
997-1208 |
2.14e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.93 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTasvpleklrrsLAI 1076
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-----------IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQdptlfmgtirnnldryneysddevmgalkhasmwdyvqslpdgmnsavsegglnLSQGQRQLLCLARALLTKARVIV 1156
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1157 MDEATASVDVQTDALLQKVIRtSFAGvTMLIIAHrlgtiaD-------CDQIVEISAGE 1208
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALK-EYPG-TVILVSH------DryfldqvATKIIELEDGK 144
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
982-1209 |
2.32e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 982 PLPEPLRPTwpefgeISVEGLKV----------RYASHlPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIeAE 1051
Cdd:PRK15134 267 PLPEPASPL------LDVEQLQVafpirkgilkRTVDH-NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1052 EGSISIDGvntasVPLEKL--------RRSLAIIPQDPTLFMGTIRNNLDRYNEysddevmGALKHASMWDYVQSlPDGM 1123
Cdd:PRK15134 339 QGEIWFDG-----QPLHNLnrrqllpvRHRIQVVFQDPNSSLNPRLNVLQIIEE-------GLRVHQPTLSAAQR-EQQV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1124 NSAVSEGGLN----------LSQGQRQLLCLARALLTKARVIVMDEATASVD--VQTD--ALLQKVIRTSfaGVTMLIIA 1189
Cdd:PRK15134 406 IAVMEEVGLDpetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAQilALLKSLQQKH--QLAYLFIS 483
|
250 260
....*....|....*....|.
gi 499478341 1190 HRLGTI-ADCDQIVEISAGEV 1209
Cdd:PRK15134 484 HDLHVVrALCHQVIVLRQGEV 504
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
401-546 |
3.48e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 401 HDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRPRMAYVPQEAYI-----VNTSL--LENLQF 473
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLghqpgIKTELtaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 474 ----GEEVSKEELRRALhnsclsrdlkewsgglrTEIGEKGV------NLSGGQKQRVALARAFLRKPQIVLLDDPLSAV 543
Cdd:PRK13538 98 yqrlHGPGDDEALWEAL-----------------AQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
...
gi 499478341 544 DAD 546
Cdd:PRK13538 161 DKQ 163
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
400-597 |
4.00e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.06 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSL--LMSLLGEvaPREGSLqfvpempgrprmayvpqeayIVNtsllenlqfGEEV 477
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLirCINLLER--PTSGRV--------------------LVD---------GQDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 478 ---SKEELRRALH-------------------NSCLSRDLKEWSgglRTEIGEK--------GV---------NLSGGQK 518
Cdd:PRK11153 70 talSEKELRKARRqigmifqhfnllssrtvfdNVALPLELAGTP---KAEIKARvtellelvGLsdkadrypaQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 519 QRVALARAFLRKPQIVLLDDPLSAVDADTenllcERLIFGAWKDVTR-----IV-VTHRLEHLAQF-DQVIYIQHGRVQG 591
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPAT-----TRSILELLKDINRelgltIVlITHEMDVVKRIcDRVAVIDAGRLVE 221
|
....*.
gi 499478341 592 QGTFSE 597
Cdd:PRK11153 222 QGTVSE 227
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
76-359 |
4.04e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 68.69 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSP----VFVNRFIGTISAGVTAETL------PTALIYGVALGLCGF--LSGLC--MQHYFFNSLkAYQVTT 141
Cdd:cd18564 9 LLETALRLLEPwplkVVIDDVLGDKPLPGLLGLApllgpdPLALLLLAAAALVGIalLRGLAsyAGTYLTALV-GQRVVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 142 NiLNERLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPM-VFGDLISASFLIIGVVAMLFyYIGWS-ALAALAVLF 219
Cdd:cd18564 88 D-LRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVsGVLPLLTNLLTLVGMLGVMF-WLDWQlALIALAVAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 220 ILAPLTNYVAKKFThldEEMMEHRDRR---VTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSl 296
Cdd:cd18564 166 LLLLAARRFSRRIK---EASREQRRREgalASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLS- 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 297 gyLAVSTLVLFVALAVhAWRG--EKLDAA------VIFtcISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18564 242 --PVVDVLVAVGTALV-LWFGawLVLAGRltpgdlLVF--LAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
399-544 |
4.33e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.36 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF-------VPeMPGRPRM--AYVPQEAYIV-NTSLL 468
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdgedithLP-MHKRARLgiGYLPQEASIFrKLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 469 EN----LQFgEEVSKEELRRALHNscLsrdLKEWS-GGLRTEigeKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAV 543
Cdd:COG1137 97 DNilavLEL-RKLSKKEREERLEE--L---LEEFGiTHLRKS---KAYSLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
.
gi 499478341 544 D 544
Cdd:COG1137 168 D 168
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
71-358 |
4.56e-12 |
|
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: 68.34 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 71 AYIWYLASSVLALLSPVFVNRFIGTISAGVTAETLPTALIY----GVALGLCGFLSGLCMQhyffnslKAYQVTTNILNE 146
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLllllSVLSGLFSGLRGGCFS-------YAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 147 RLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSD-FPMVFGDLISASFLIIGVVAMLFYYiGWSaLAALAvlFILAPLT 225
Cdd:cd18572 74 DLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDpLSTNLNVFLRNLVQLVGGLAFMFSL-SWR-LTLLA--FITVPVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 226 NYVAKKFTH----LDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVtevrEKELTSRRRLAKAEVVSSLGYLAV 301
Cdd:cd18572 150 ALITKVYGRyyrkLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRY----ERALDKALKLSVRQALAYAGYVAV 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 302 STLVLFVALAVHAWRG------EKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAkVGARR 358
Cdd:cd18572 226 NTLLQNGTQVLVLFYGghlvlsGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQA-VGAAE 287
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
385-589 |
4.88e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 385 MQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpempgrprmayVPQEAYIVN 464
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------VPDNQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 TSLLENLqfGEEVSKEELRRALHNSCLSrDLKEWsggLRteigeKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:COG2401 100 ASLIDAI--GRKGDFKDAVELLNAVGLS-DAVLW---LR-----RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499478341 545 ADTENLLcERLIFGAWKD--VTRIVVTHRLEHLA--QFDQVIYIQHGRV 589
Cdd:COG2401 169 RQTAKRV-ARNLQKLARRagITLVVATHHYDVIDdlQPDLLIFVGYGGV 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
997-1225 |
5.31e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASVPLEKLRRSL 1074
Cdd:PRK13638 2 LATSDLWFRYQDE--PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDP--TLFMGTIRNNLD---RYNEYSDDEVmgalkhASMWDYVQSLPDGMNSAvSEGGLNLSQGQRQLLCLARALL 1149
Cdd:PRK13638 80 ATVFQDPeqQIFYTDIDSDIAfslRNLGVPEAEI------TRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1150 TKARVIVMDEATASVDVQTDALLQKVIRTSFA-GVTMLIIAHrlgtiaDCDQIVEIS-------AGEVKSIRRPTE-FSQ 1220
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSH------DIDLIYEISdavyvlrQGQILTHGAPGEvFAC 226
|
....*
gi 499478341 1221 EEIEE 1225
Cdd:PRK13638 227 TEAME 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
399-599 |
5.56e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRPRMAYVPQEAYIVNTSLLENLQFGEEVS 478
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW----LDGEHIQHYASKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 479 KEEL---RRALHNSCLSRDLKE----WSGGLR----TEIGEKGVN-LSGGQKQRVALARAFLRKPQIVLLDDPLSAVDAD 546
Cdd:PRK10253 98 VQELvarGRYPHQPLFTRWRKEdeeaVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 547 TENLLCERLI-FGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELV 599
Cdd:PRK10253 178 HQIDLLELLSeLNREKGYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
76-320 |
6.27e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 67.59 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGVTAETLP-TALIYGVALGLCGFLSGlcMQHYFFNSLkAYQVTTNiLNERLFKHSLK 154
Cdd:cd18557 6 LISSAAQLLLPYLIGRLIDTIIKGGDLDVLNeLALILLAIYLLQSVFTF--VRYYLFNIA-GERIVAR-LRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 155 LSQKSRQKNQVGDIVNHMSSDSDNVSD-FPMVFGDLISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLTNYVAKKF 232
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSaVTDNLSQLLRNILQVIGGLIILF-ILSWKlTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 233 THLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEksvAKEVTEVREKELTSrRRLAKAEVVSSLGYLAVSTLVLFVALAV 312
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAE---EKEIRRYSEALDRS-YRLARKKALANALFQGITSLLIYLSLLL 236
|
....*...
gi 499478341 313 HAWRGEKL 320
Cdd:cd18557 237 VLWYGGYL 244
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-587 |
6.40e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 382 GLQMQHFSLRHDgaVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSL------LGEVAPrEGSLQF---------VPE 446
Cdd:PRK14258 7 AIKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelESEVRV-EGRVEFfnqniyerrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 447 MPGRPRMAYVPQEAYIVNTSLLENLQFGEEV----SKEELRRALHNSCLSRDLkeWSGgLRTEIGEKGVNLSGGQKQRVA 522
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIvgwrPKLEIDDIVESALKDADL--WDE-IKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 523 LARAFLRKPQIVLLDDPLSAVDAdTENLLCERLIFGAW--KDVTRIVVTHRLEHLAQFDQVIYIQHG 587
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDP-IASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
399-597 |
8.72e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.96 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpemPGRPRMAYVPQEaYIVNTSLL-ENLQFGEEV 477
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFL----GDKPISMLSSRQ-LARRLALLpQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 478 SKEEL---RRALHNSC---LSRD---LKEWSGGlRTEI---GEKGV-NLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:PRK11231 92 TVRELvayGRSPWLSLwgrLSAEdnaRVNQAME-QTRInhlADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 545 ----ADTENLLCERLIFGAwkdvTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSE 597
Cdd:PRK11231 171 inhqVELMRLMRELNTQGK----TVVTVLHDLNQASRYcDHLVVLANGHVMAQGTPEE 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1014-1223 |
9.13e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1014 LKGITFKVEAGSRVGIIGRTGSGKSTFFQSL--------FrfieaeEGSISIDG-VNTASVPLEKLRRSLAIIPQDPTL- 1083
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphgtY------EGEIIFEGeELQASNIRDTERAGIAIIHQELALv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1084 ---------FMGtirNNLDRYNEYSDDEVMgaLKHASMWDYVQsLPDGMNSAVSEGGLnlsqGQRQLLCLARALLTKARV 1154
Cdd:PRK13549 95 kelsvleniFLG---NEITPGGIMDYDAMY--LRAQKLLAQLK-LDINPATPVGNLGL----GQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1155 IVMDEATASVDVQTDALLQKVIRTSFA-GVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTEDDI 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
386-553 |
1.03e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 67.83 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 386 QHFSL------RHDGAVSDVlHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG------ 449
Cdd:COG4608 15 KHFPVrgglfgRTVGVVKAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdgqdITGLSGrelrpl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 450 RPRMAYVPQEAY-------IVNTSLLENLQFGEEVSKEELRRALhnsclsRDLKEwSGGLRTEIG-----EkgvnLSGGQ 517
Cdd:COG4608 94 RRRMQMVFQDPYaslnprmTVGDIIAEPLRIHGLASKAERRERV------AELLE-LVGLRPEHAdryphE----FSGGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499478341 518 KQRVALARAFLRKPQIVLLDDPLSAVD----ADTENLLCE 553
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALDvsiqAQVLNLLED 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
398-598 |
1.11e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL-------QFVPEMPG-------------RPRMAYVP 457
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtiNLVRDKDGqlkvadknqlrllRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 458 QEAYI-VNTSLLENLQFGE----EVSKEELR-RALhnsclsRDLKEWSGGLRTEiGEKGVNLSGGQKQRVALARAFLRKP 531
Cdd:PRK10619 99 QHFNLwSHMTVLENVMEAPiqvlGLSKQEAReRAV------KYLAKVGIDERAQ-GKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 532 QIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLE---HLAqfDQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGfarHVS--SHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
399-600 |
1.17e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.65 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqFVPEMPG---------RPRMAYVPQ--EAYIVNTSL 467
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLDTsdeenlwdiRNKAGMVFQnpDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEE---VSKEELRRALHNsCLSR----DLKEWSGGLrteigekgvnLSGGQKQRVALARAFLRKPQIVLLDDPL 540
Cdd:PRK13633 104 EEDVAFGPEnlgIPPEEIRERVDE-SLKKvgmyEYRRHAPHL----------LSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 541 SAVDADTenllcERLIFGAWKDV------TRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVK 600
Cdd:PRK13633 173 AMLDPSG-----RREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1013-1194 |
1.18e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.07 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQD---PTLfmgTIR 1089
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPglkPEL---SAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1090 NNLDRYNEYSDDEvmgalkHASMWDyvqslpdgmnsAVSEGGLN---------LSQGQRQLLCLARALLTKARVIVMDEA 1160
Cdd:TIGR01189 92 ENLHFWAAIHGGA------QRTIED-----------ALAAVGLTgfedlpaaqLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 499478341 1161 TASVDVQTDALLQKVIRTSFA--GVTMLIIAHRLGT 1194
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLArgGIVLLTTHQDLGL 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
399-573 |
1.29e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSlLMSLL-GEVAPREGSLQF--VPEMPGRPRMA------YVPQEAYIVNT-SLL 468
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKST-LMKILsGVYQPDSGEILLdgEPVRFRSPRDAqaagiaIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 469 ENLQFGEE------VSKEELRRAlhnsclSRD-LKEWsgGL----RTEIGEkgvnLSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:COG1129 98 ENIFLGREprrgglIDWRAMRRR------ARElLARL--GLdidpDTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499478341 538 DPLSA-VDADTENL--LCERLifgawKD--VTRIVVTHRLE 573
Cdd:COG1129 166 EPTASlTEREVERLfrIIRRL-----KAqgVAIIYISHRLD 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
402-589 |
1.32e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.75 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpempGRPRMAYVPQ---------EAYIV--NTSLLEN 470
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-----GEKRMNDVPPaergvgmvfQSYALypHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 471 LQFG---EEVSKEELRRALHNSC--------LSRDLKEwsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK11000 96 MSFGlklAGAKKEEINQRVNQVAevlqlahlLDRKPKA---------------LSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 540 LSAVDADTE-------NLLCERLifgawkDVTRIVVTH-RLEHLAQFDQVIYIQHGRV 589
Cdd:PRK11000 161 LSNLDAALRvqmrieiSRLHKRL------GRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
997-1209 |
1.40e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.19 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFI---EAEEGSISIDG--VNTASVPLEKLR 1071
Cdd:PRK09984 5 IRVEKLAKTFNQH--QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrtVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLAiipqdptlFMGTIRNNLDRYNEYS--DDEVMGALKHASMW-------------DYVQSLPD-GMNSAVSEGGLNLS 1135
Cdd:PRK09984 83 KSRA--------NTGYIFQQFNLVNRLSvlENVLIGALGSTPFWrtcfswftreqkqRALQALTRvGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1136 QGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIR--TSFAGVTMLIIAHRLG-TIADCDQIVEISAGEV 1209
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
997-1217 |
1.64e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.53 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYAS--HLPQVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFI----EAEEGSISIDGVNTASV---PL 1067
Cdd:COG4181 9 IELRGLTKTVGTgaGELTILKGISLEVEAGESVAIVGASGSGKST----LLGLLagldRPTSGTVRLAGQDLFALdedAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1068 EKLR-RSLAIIPQD----PTLfmgTIRNNldryneysddeVMGALKHASMwdyvqslPDGMNSAVSE---GGLN------ 1133
Cdd:COG4181 85 ARLRaRHVGFVFQSfqllPTL---TALEN-----------VMLPLELAGR-------RDARARARALlerVGLGhrldhy 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1134 ---LSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDAllqKVIRTSFA-----GVTMLIIAHRLGTIADCDQIVEIS 1205
Cdd:COG4181 144 paqLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGE---QIIDLLFElnrerGTTLVLVTHDPALAARCDRVLRLR 220
|
250
....*....|..
gi 499478341 1206 AGEVKSIRRPTE 1217
Cdd:COG4181 221 AGRLVEDTAATA 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
373-539 |
1.70e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 373 EERTDGAAVgLQMQHFSLRHdgavsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqfvpEMPGRP- 451
Cdd:COG1129 248 RAAAPGEVV-LEVEGLSVGG------VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEI----RLDGKPv 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 452 -----------RMAYVP----QEAYIVNTSLLEN--------------LQFGEEVSK-EELRRALhnsclsrDLKewSGG 501
Cdd:COG1129 317 rirsprdairaGIAYVPedrkGEGLVLDLSIRENitlasldrlsrgglLDRRRERALaEEYIKRL-------RIK--TPS 387
|
170 180 190
....*....|....*....|....*....|....*...
gi 499478341 502 LRTEIGekgvNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:COG1129 388 PEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1013-1223 |
1.93e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASV-PLEKLRRSLAIIPQDPTLFMG-TIRN 1090
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAKAHQLGIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1091 NLdryneysddeVMGALKHAS----MWDYVQSLPDGMNSAVSEGGLNLSqgQRQLLCLARALLTKARVIVMDEATASVD- 1165
Cdd:PRK15439 106 NI----------LFGLPKRQAsmqkMKQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1166 VQTDALLQKVIRTSFAGVTMLIIAHRLGTI-ADCDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-598 |
2.09e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.84 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSL--LGEVAPR----EGSLQF-------VPEMPGRPRMAYVPQEAY-IVN 464
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrLIEIYDSkikvDGKVLYfgkdifqIDAIKLRKEVGMVFQQPNpFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 TSLLENLQFGEEV----SKEELRRALHNSClsRDLKEWSGgLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPL 540
Cdd:PRK14246 105 LSIYDNIAYPLKShgikEKREIKKIVEECL--RKVGLWKE-VYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 541 SAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK14246 182 SMIDIVNSQAI-EKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEI 239
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
399-597 |
2.15e-11 |
|
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: 65.45 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpempGRP--RMAyvPQEAY---IVNT-------- 465
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD----GRDitGLP--PHRIArlgIARTfqnprlfp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 --SLLENLQFGeevskeeLRRALHNSCLSRDLKEWSG------------------GLRTEIGEKGVNLSGGQKQRVALAR 525
Cdd:COG0411 93 elTVLENVLVA-------AHARLGRGLLAALLRLPRArreereareraeellervGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 526 AFLRKPQIVLLDDPLSAV-DADTENLLceRLIFG--AWKDVTRIVVTHRLE---HLAqfDQVIYIQHGRVQGQGTFSE 597
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLnPEETEELA--ELIRRlrDERGITILLIEHDMDlvmGLA--DRIVVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
398-598 |
2.20e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.98 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRPRMAYVPQEAYIV---------NTSLL 468
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVfqnpddqifSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 469 ENLQFG-------EEVSKEELRRALHNSCLSRdlkewsggLRTEIGEkgvNLSGGQKQRVALARAFLRKPQIVLLDDPLS 541
Cdd:PRK13652 98 QDIAFGpinlgldEETVAHRVSSALHMLGLEE--------LRDRVPH---HLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 542 AVDA-------DTENLLCERLIFgawkdvTRIVVTHRLEHLAQFDQVIYI-QHGRVQGQGTFSEL 598
Cdd:PRK13652 167 GLDPqgvkeliDFLNDLPETYGM------TVIFSTHQLDLVPEMADYIYVmDKGRIVAYGTVEEI 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
400-644 |
2.20e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG------EVAPR---EGSLQFVPEMpgRPRMAYVPQEAYIVNT-SLLE 469
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrspkgvKGSGSvllNGMPIDAKEM--RAISAYVQQDDLFIPTlTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQF------GEEVSKEELRRALHNscLSRDLkewsgGLR----TEIGEKGV--NLSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:TIGR00955 119 HLMFqahlrmPRRVTKKEKRERVDE--VLQAL-----GLRkcanTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 538 DPLSAVDADTENLLCERLIFGAWKDVTRIVVTHR--LEHLAQFDQVIYIQHGRVQGQGTFSELVKtcapfaeFYKEHGKT 615
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAVP-------FFSDLGHP 264
|
250 260 270
....*....|....*....|....*....|.
gi 499478341 616 QGEGHEvrPAETAQEAASI--NTELEAKTTR 644
Cdd:TIGR00955 265 CPENYN--PADFYVQVLAVipGSENESRERI 293
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
76-348 |
2.77e-11 |
|
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: 65.97 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGVTAETLPT-ALIYGVALGLCGFLSGLcmQHYFFNslkayQVTTNILNE---RLFKH 151
Cdd:cd18576 6 LLSSAIGLVFPLLAGQLIDAALGGGDTASLNQiALLLLGLFLLQAVFSFF--RIYLFA-----RVGERVVADlrkDLYRH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 152 SLKLSQKSRQKNQVGDIVNHMSSDSDNVSD-FPMVFGDLISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLTNYVA 229
Cdd:cd18576 79 LQRLPLSFFHERRVGELTSRLSNDVTQIQDtLTTTLAEFLRQILTLIGGVVLLF-FISWKlTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 230 KKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVsslgYLAVSTLVLFVA 309
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRAL----FSSFIIFLLFGA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499478341 310 LAVHAWRG------EKLDAAVIFTCISLFGLLEGPFGDLSRLISR 348
Cdd:cd18576 234 IVAVLWYGgrlvlaGELTAGDLVAFLLYTLFIAGSIGSLADLYGQ 278
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1012-1196 |
2.81e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSI-----SIDGVNTASVPLekLRRSLAIIPQDPTLFMG 1086
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLKNREVPF--LRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 -TIRNN----LDRYNEYSDD---EVMGALKHASMWDYVQSLPdgmnsavseggLNLSQGQRQLLCLARALLTKARVIVMD 1158
Cdd:PRK10908 94 rTVYDNvaipLIIAGASGDDirrRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499478341 1159 EATASVDvqtDALLQKVIRT----SFAGVTMLIIAHRLGTIA 1196
Cdd:PRK10908 163 EPTGNLD---DALSEGILRLfeefNRVGVTVLMATHDIGLIS 201
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
377-601 |
2.91e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.50 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 377 DGAAVGLQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSL------------LGEVAPREGSL-QF 443
Cdd:PRK14271 16 DAAAPAMAAVNLTLGFAGKT--VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrySGDVLLGGRSIfNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 444 VPEMPGRPRMAYVPQEAYIVNTSLLENLQFGEEVSKEELRRALHNSCLSR--DLKEWSGgLRTEIGEKGVNLSGGQKQRV 521
Cdd:PRK14271 94 RDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARltEVGLWDA-VKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 522 ALARAFLRKPQIVLLDDPLSAVDADTENLLcERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVK 600
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFS 251
|
.
gi 499478341 601 T 601
Cdd:PRK14271 252 S 252
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
402-598 |
3.26e-11 |
|
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: 64.31 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGS-----LQFVPEMPG-RPRMAYVPQEAyIVNTSL--LENLQ- 472
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvagHDVVREPREvRRRIGIVFQDL-SVDDELtgWENLYi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 473 FGE--EVSKEELRRALHNSCLSRDLkewsgglrTEIGEKGV-NLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTEN 549
Cdd:cd03265 97 HARlyGVPGAERRERIDELLDFVGL--------LEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 550 LLCERL-IFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:cd03265 169 HVWEYIeKLKEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1017-1217 |
3.65e-11 |
|
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: 64.97 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1017 ITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKLRR--------SLAIIPQdptlfm 1085
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkkismvfqSFALLPH------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1086 gtiRNNLDryNEYSDDEVMG------------ALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARALLTKAR 1153
Cdd:cd03294 117 ---RTVLE--NVAFGLEVQGvpraereeraaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1154 VIVMDEATASVD------VQTDAL-LQKVIRTsfagvTMLIIAH------RLGtiadcDQIVEISAGEVKSIRRPTE 1217
Cdd:cd03294 181 ILLMDEAFSALDplirreMQDELLrLQAELQK-----TIVFITHdldealRLG-----DRIAIMKDGRLVQVGTPEE 247
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
67-364 |
3.69e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 65.94 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 67 FTRPAYIWYLASSVLALLS----PVF---VNRFIGTISAGVTAETLPTALIYG---VALGLCGFLSGLCmQHYFFNslka 136
Cdd:cd18578 3 LNKPEWPLLLLGLIGAIIAgavfPVFailFSKLISVFSLPDDDELRSEANFWAlmfLVLAIVAGIAYFL-QGYLFG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 137 yqVTTNILNERLFKHSLK--LSQK----SRQKNQVGDIVNHMSSDSDNVSDFP-MVFGDLISASFLIIGVVAMLFYYiGW 209
Cdd:cd18578 78 --IAGERLTRRLRKLAFRaiLRQDiawfDDPENSTGALTSRLSTDASDVRGLVgDRLGLILQAIVTLVAGLIIAFVY-GW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 210 S-ALAALAVLFILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKE-VTEVREKELTSRRRL 287
Cdd:cd18578 155 KlALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKyEEALEEPLKKGLRRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 288 akaeVVSSLGYlAVSTLVLFVALAVHAWRGEKLDA--------------AVIFTCISLfgllegpfGDLSRLISRATNAK 353
Cdd:cd18578 235 ----LISGLGF-GLSQSLTFFAYALAFWYGGRLVAngeytfeqffivfmALIFGAQSA--------GQAFSFAPDIAKAK 301
|
330
....*....|.
gi 499478341 354 VGARRILDYLN 364
Cdd:cd18578 302 AAAARIFRLLD 312
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1014-1223 |
3.71e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.16 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1014 LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIE--AEEGSISIDGVN-TASVPLEKLRRSLAIIPQDPTL------- 1083
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPlKASNIRDTERAGIVIIHQELTLvpelsva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1084 ---FMGtirNNLDRYNEYSDDEVMGALKHASMWDYvqSLPDGMNS-AVSEGGLnlsqGQRQLLCLARALLTKARVIVMDE 1159
Cdd:TIGR02633 97 eniFLG---NEITLPGGRMAYNAMYLRAKNLLREL--QLDADNVTrPVGDYGG----GQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1160 ATASVDVQTDALLQKVIRTSFA-GVTMLIIAHRLGTI-ADCDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVkAVCDTICVIRDGQHVATKDMSTMSEDDI 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1013-1209 |
3.87e-11 |
|
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: 64.66 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVntasVPLEKLRRSLAIIpqdpTLFMGTiRNNL 1092
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLRRI----GVVFGQ-KTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1093 -------DRYN------EYSDDEVMGALKH-ASMWDyvqsLPDGMNSAVSegglNLSQGQRQLLCLARALLTKARVIVMD 1158
Cdd:cd03267 107 wwdlpviDSFYllaaiyDLPPARFKKRLDElSELLD----LEELLDTPVR----QLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1159 EATASVDVQTDALLQKVIRTSFA--GVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1012-1201 |
3.98e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGV-----NTAsvplEKLRRSLAIIPQD----PT 1082
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaSTT----AALAAGVAIIYQElhlvPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1083 LfmgTIRNNLdryneysddeVMGALKHASMWDYVQSLPDGMNSAVSEGGLN---------LSQGQRQLLCLARALLTKAR 1153
Cdd:PRK11288 94 M---TVAENL----------YLGQLPHKGGIVNRRLLNYEAREQLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRTSFA-GVTMLIIAHRLGTI-ADCDQI 1201
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAeGRVILYVSHRMEEIfALCDAI 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1014-1217 |
4.15e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1014 LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLR-----------RSLAIIPQDPT 1082
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1083 LFMGTIRNNLDRY-NEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEAT 1161
Cdd:PRK10070 124 LDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1162 ASVD--VQTDALLQKVIRTSFAGVTMLIIAHRLG-TIADCDQIVEISAGEVKSIRRPTE 1217
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLDeAMRIGDRIAIMQNGEVVQVGTPDE 251
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
399-589 |
4.30e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.72 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMP--------GR----PRMAYVPqeayi 462
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdgkdVTKLPeykrakyiGRvfqdPMMGTAP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 vNTSLLENL--------QFGeevskeeLRRALHNSClsRD-----LKEWSGGL----RTEIGekgvNLSGGQKQRVALAR 525
Cdd:COG1101 96 -SMTIEENLalayrrgkRRG-------LRRGLTKKR--RElfrelLATLGLGLenrlDTKVG----LLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 526 AFLRKPQIVLLDDPLSAVDADTENL---LCERLIfgAWKDVTRIVVTHRLEH-LAQFDQVIYIQHGRV 589
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALvleLTEKIV--EENNLTTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
399-545 |
4.52e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.02 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL----QFVPEMPGRPR-MAYVPQE-AYIVNTSLLENLQ 472
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIwiggRVVNELEPADRdIAMVFQNyALYPHMSVRENMA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 473 FG---EEVSKEELRRalhnsclsRdLKEWSGGLrtEIGE----KGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDA 545
Cdd:PRK11650 99 YGlkiRGMPKAEIEE--------R-VAEAARIL--ELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1017-1204 |
5.28e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1017 ITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVP---LEKLRRSLAIIPQDPTLfmgtirnNLD 1093
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-------SLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1094 RyNEYSDDEVMGALKhasmwdyVQSLPDGMNSA------VSEGGL----------NLSQGQRQLLCLARALLTKARVIVM 1157
Cdd:PRK10261 416 P-RQTVGDSIMEPLR-------VHGLLPGKAAAarvawlLERVGLlpehawryphEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1158 DEATASVDV----QTDALLQKVIRTsfAGVTMLIIAHRLGTIADCD---------QIVEI 1204
Cdd:PRK10261 488 DEAVSALDVsirgQIINLLLDLQRD--FGIAYLFISHDMAVVERIShrvavmylgQIVEI 545
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1012-1211 |
6.34e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.67 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASV---PLEKLRRS-LAIIPQDPTLFMG- 1086
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 TIRNNLDRYNEYSDDEVMGALKHASMwdYVQSLpdGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDV 1166
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKQRLLRAQE--LLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499478341 1167 QTD----ALLQKVIRTsfaGVTMLIIAHRLGTIADCDQIVEISAGEVKS 1211
Cdd:PRK10535 178 HSGeevmAILHQLRDR---GHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
380-544 |
6.44e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 380 AVGLQMQHFSLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPGRPRMAY 455
Cdd:PRK10419 8 GLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgepLAKLNRAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 ------VPQEA-------YIVNTSLLENLQF-------GEEVSKEELRRALhnsclsrdlkewsgGLRTEIGEK-GVNLS 514
Cdd:PRK10419 88 rrdiqmVFQDSisavnprKTVREIIREPLRHllsldkaERLARASEMLRAV--------------DLDDSVLDKrPPQLS 153
|
170 180 190
....*....|....*....|....*....|
gi 499478341 515 GGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
398-589 |
7.98e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 398 DVLHDVNVHVPAGSSLAIVGPVGAGKSSLlMSLLGEV-APREGSL----QFVPEMPG-------RPRMAYVPQEAYivnt 465
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTL-MNILGCLdKPTSGTYrvagQDVATLDAdalaqlrREHFGFIFQRYH---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 sLLENLQFGEEV--------SKEELRRALHNSCLSRDlkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:PRK10535 97 -LLSHLTAAQNVevpavyagLERKQRLLRAQELLQRL------GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 538 DPLSAVDADTE-------NLLCERlifgawkDVTRIVVTHRLEHLAQFDQVIYIQHGRV 589
Cdd:PRK10535 170 EPTGALDSHSGeevmailHQLRDR-------GHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
997-1212 |
1.05e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLfRFIEAEE------GSISIDG---VNTASVPL 1067
Cdd:PRK11264 4 IEVKNLVKKFHGQ--TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDTarsLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1068 EKLRRSLAIIPQDPTLFmgTIRNNLDRYNEySDDEVMGALKHASMWDYVQSLPD-GMNSAVSEGGLNLSQGQRQLLCLAR 1146
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLF--PHRTVLENIIE-GPVIVKGEPKEEATARARELLAKvGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1147 ALLTKARVIVMDEATASVDVQtdaLLQKVIRT--SFA--GVTMLIIAHRLG---TIAD----CDQIVEISAGEVKSI 1212
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPE---LVGEVLNTirQLAqeKRTMVIVTHEMSfarDVADraifMDQGRIVEQGPAKAL 231
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
399-544 |
1.10e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRPRMAYVPQEAYI-------VNTSLLENL 471
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVghrsginPYLTLRENC 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 472 QFGeevskeelrraLHNSCLSRDLKEWSGGLRTE--IGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:PRK13540 96 LYD-----------IHFSPGAVGITELCRLFSLEhlIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
997-1224 |
1.20e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSL--FRFIEAEEGSI------------------- 1055
Cdd:TIGR03269 1 IEVKNLTKKFDGK--EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1056 --------------SIDGVNTASVPLEKLRRSLAIIPQDPTLFMG---TIRNNLDRYNE--YSDDEVMGalKHASMWDYV 1116
Cdd:TIGR03269 79 gepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddtVLDNVLEALEEigYEGKEAVG--RAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1117 QslpdgMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSF--AGVTMLIIAHRLGT 1194
Cdd:TIGR03269 157 Q-----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEV 231
|
250 260 270
....*....|....*....|....*....|.
gi 499478341 1195 IAD-CDQIVEISAGEVKSIRRPTEFSQEEIE 1224
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGTPDEVVAVFME 262
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
711-934 |
1.23e-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: 63.98 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 711 WVALTAIGIYGLIGVLVLVGS-LLNHLfwldrGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVdvylQ 789
Cdd:cd18552 40 LVPLAIIGLFLLRGLASYLQTyLMAYV-----GQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQV----Q 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 790 WSFDSAVHCALQVIVSIVLILGLM-------PLMVFVIAPVMALY-YVLQRDYRRPAREVkrFDSVARSprYAHFKESLQ 861
Cdd:cd18552 111 NALTSALTVLVRDPLTVIGLLGVLfyldwklTLIALVVLPLAALPiRRIGKRLRKISRRS--QESMGDL--TSVLQETLS 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 862 GLVVIRSFNkgpwfMQNF-YAKLSHSNRMFYSHVM-INRWFSSRIPLVGGLISMATAVGVSLSAYYGVMDAGTAG 934
Cdd:cd18552 187 GIRVVKAFG-----AEDYeIKRFRKANERLRRLSMkIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPG 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
379-544 |
1.24e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 61.68 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 379 AAVGLQMQHFSlrhdgaVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VPEMPGRPR---- 452
Cdd:cd03215 1 GEPVLEVRGLS------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgKPVTRRSPRdair 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 --MAYVP----QEAYIVNTSLLENLqfgeevskeelrrALHNSclsrdlkewsgglrteigekgvnLSGGQKQRVALARA 526
Cdd:cd03215 75 agIAYVPedrkREGLVLDLSVAENI-------------ALSSL-----------------------LSGGNQQKVVLARW 118
|
170
....*....|....*...
gi 499478341 527 FLRKPQIVLLDDPLSAVD 544
Cdd:cd03215 119 LARDPRVLILDEPTRGVD 136
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
399-589 |
1.26e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPR--EGSLQF----VPEMPgrprmayvPQEayIVNTSLLENLQ 472
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFkgedITDLP--------PEE--RARLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 473 FGEEVSkeelrrALHNSCLSRDLkewsgglrteigekGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLC 552
Cdd:cd03217 85 YPPEIP------GVKNADFLRYV--------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499478341 553 ErlIFGAWKDVTR--IVVTHRlEHLAQF---DQVIYIQHGRV 589
Cdd:cd03217 145 E--VINKLREEGKsvLIITHY-QRLLDYikpDRVHVLYDGRI 183
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
998-1165 |
1.33e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.50 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 998 SVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE---EGSISIDGVNTASVPLEklRRSL 1074
Cdd:COG4136 3 SLENLTITLGGRP--LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLF--MgTIRNNL-----------DRyneysDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQL 1141
Cdd:COG4136 79 GILFQDDLLFphL-SVGENLafalpptigraQR-----RARVEQALEEAGLAGFADRDPA-----------TLSGGQRAR 141
|
170 180
....*....|....*....|....
gi 499478341 1142 LCLARALLTKARVIVMDEATASVD 1165
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLD 165
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
997-1212 |
1.57e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 62.27 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKlrRSLAI 1076
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLF--MgTIRNNLD---RYNEYSDDE----VMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARA 1147
Cdd:cd03301 77 VFQNYALYphM-TVYDNIAfglKLRKVPKDEiderVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1148 LLTKARVIVMDEATASVdvqtDALLQKVIRTSFA------GVTMLIIAH---RLGTIAdcDQIVEISAGEVKSI 1212
Cdd:cd03301 145 IVREPKVFLMDEPLSNL----DAKLRVQMRAELKrlqqrlGTTTIYVTHdqvEAMTMA--DRIAVMNDGQIQQI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
997-1192 |
1.61e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASH-------LPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntasVPLEK 1069
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG-----EPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 L--------RRSLAIIPQDPTLFMG---TIRNNLDRYNEY--SDDEVMGALKHASMWDYVQsLPDGMNSAVSEgglNLSQ 1136
Cdd:PRK10419 79 LnraqrkafRRDIQMVFQDSISAVNprkTVREIIREPLRHllSLDKAERLARASEMLRAVD-LDDSVLDKRPP---QLSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1137 GQRQLLCLARALLTKARVIVMDEATASVD--VQTDAL-LQKVIRTSFaGVTMLIIAHRL 1192
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDlvLQAGVIrLLKKLQQQF-GTACLFITHDL 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
400-594 |
1.78e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.83 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSL--LMSLLGEvaPREGSL----QFVPEMPG------RPRMAYVPQEAY------ 461
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarLLTMIET--PTGGELyyqgQDLLKADPeaqkllRQKIQIVFQNPYgslnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 462 -IVNTSLLENLQFGEEVSKEElRRALHNSCLSRDlkewsgGLRTEIGEKGVNL-SGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK11308 109 kKVGQILEEPLLINTSLSAAE-RREKALAMMAKV------GLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 540 LSAVD----ADTENLLCE-RLIFGawkdVTRIVVTHRL---EHLAqfDQVIYIQHGRVQGQGT 594
Cdd:PRK11308 182 VSALDvsvqAQVLNLMMDlQQELG----LSYVFISHDLsvvEHIA--DEVMVMYLGRCVEKGT 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
400-600 |
1.87e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.26 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfVPEM------------PGRPRMAYVPQ--EAYIVNT 465
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT-VDDItithktkdkyirPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 SLLENLQFG--------EEVsKEELRRALHNSCLSRDLKEWSgglrteigekGVNLSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:PRK13646 102 TVEREIIFGpknfkmnlDEV-KNYAHRLLMDLGFSRDVMSQS----------PFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 538 DPLSAVDADTENLLCERLI-FGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVK 600
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKsLQTDENKTIILVSHDMNEVARYaDEVIVMKEGSIVSQTSPKELFK 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
392-597 |
2.15e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.55 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 392 HDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGeVAPREGSLQFvpemPGRPRMAYVPQE-----AYIVNTS 466
Cdd:COG4138 4 NDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILL----NGRPLSDWSAAElarhrAYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LL-------ENLQFG--EEVSKEELRRALhnSCLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLR-------K 530
Cdd:COG4138 79 SPpfampvfQYLALHqpAGASSEAVEQLL--AQLAEAL-----GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 531 PQIVLLDDPLSAVD----ADTENLL---CERLIfgawkdvTRIVVTHRLEH-LAQFDQVIYIQHGRVQGQGTFSE 597
Cdd:COG4138 152 GQLLLLDEPMNSLDvaqqAALDRLLrelCQQGI-------TVVMSSHDLNHtLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
71-322 |
2.24e-10 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 63.01 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 71 AYIWYLASSVLALLSPVFVNRFIGTISAGvTAETLPTALIYGVALGLCGFLSGLC--MQHYFFnsLKAYQVTTNILNERL 148
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLA-KVKDLESAVTLILLYALLRFSSKLLkeLRSLLY--RRVQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 149 FKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYYIG--WSALAALAVLFILAPLTN 226
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFgaWLALIVFLSVLLYGVFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 227 YVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRlakaeVVSSLGYLAVS---- 302
Cdd:cd18560 158 KVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVK-----VQASLSLLNVGqqli 232
|
250 260
....*....|....*....|...
gi 499478341 303 ---TLVLFVALAVHAWRGEKLDA 322
Cdd:cd18560 233 iqlGLTLGLLLAGYRVVDGGLSV 255
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
996-1217 |
2.30e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.12 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 996 EISVEGLKVRYASHLP---QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISI-DGVNTASVP---LE 1068
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKnkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1069 KLRRSLAIIPQDP--TLFMGTIRN-------NLDryneYSDDEvmgALKHASMWDYVQSLPDgmnSAVSEGGLNLSQGQR 1139
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETVEKdicfgpmNFG----VSEED---AKQKAREMIELVGLPE---ELLARSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1140 QLLCLARALLTKARVIVMDEATASVDVQTdallQKVIRTSFA------GVTMLIIAHRLGTIAD-CDQIVEISAGEVKSI 1212
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQ 227
|
....*
gi 499478341 1213 RRPTE 1217
Cdd:PRK13634 228 GTPRE 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1019-1210 |
2.33e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 63.97 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1019 FKVEAGSRVGIIGRTGSGKSTffqsLFRFI----EAEEGSISIDG---VNTAS---VPLEklRRSLAIIPQDPTLF--Mg 1086
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTT----LLRAIagleRPDSGRIRLGGevlQDSARgifLPPH--RRRIGYVFQEARLFphL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 TIRNNLdRYneysddevmgALKHASMwdyvQSLPDGMNSAVSEGGL---------NLSQGQRQLLCLARALLTKARVIVM 1157
Cdd:COG4148 93 SVRGNL-LY----------GRKRAPR----AERRISFDEVVELLGIghlldrrpaTLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1158 DEATASVDVQTDA----LLQKVIRTsfAGVTMLIIAHRLGTIAD-CDQIVEISAGEVK 1210
Cdd:COG4148 158 DEPLAALDLARKAeilpYLERLRDE--LDIPILYVSHSLDEVARlADHVVLLEQGRVV 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
987-1226 |
2.51e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 987 LRPTWPEfgEISVEGLKVRYAS-------HLPQVlKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE-EGSISID 1058
Cdd:TIGR02633 245 LYPHEPH--EIGDVILEARNLTcwdvinpHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFIN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1059 G--VNTASvPLEKLRRSLAIIPQD-------PTLFMG--TIRNNLDRY-------NEYSDDEVMGALKHASMWDYVQSLP 1120
Cdd:TIGR02633 322 GkpVDIRN-PAQAIRAGIAMVPEDrkrhgivPILGVGknITLSVLKSFcfkmridAAAELQIIGSAIQRLKVKTASPFLP 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1121 DGmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFA-GVTMLIIAHRLGTIAD-C 1198
Cdd:TIGR02633 401 IG----------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGlS 470
|
250 260
....*....|....*....|....*...
gi 499478341 1199 DQIVEISAGEVKSIRRPTEFSQEEIEES 1226
Cdd:TIGR02633 471 DRVLVIGEGKLKGDFVNHALTQEQVLAA 498
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
402-601 |
2.62e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.88 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMpgrpRMAYVPQEAY----IVNTSLLENLQFGEEV 477
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV----RMAVFSQHHVdgldLSSNPLLYMMRCFPGV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 478 SKEELRRALHNSCLSRDLKEwsgglrteigEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIF 557
Cdd:PLN03073 603 PEQKLRAHLGSFGVTGNLAL----------QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVL 672
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 558 ---GAwkdvtrIVVTHRlEHL--AQFDQVIYIQHGRVQG-QGTFSELVKT 601
Cdd:PLN03073 673 fqgGV------LMVSHD-EHLisGSVDELWVVSEGKVTPfHGTFHDYKKT 715
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
997-1217 |
2.65e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKL-RRSLA 1075
Cdd:PRK11300 6 LSVSGLMMRFGGLL--AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDPTLF--MGTIRNNLDRYNEYSDDEVMG--------------ALKHASMWDYVQSLPDGMNSavsEGGlNLSQGQR 1139
Cdd:PRK11300 84 RTFQHVRLFreMTVIENLLVAQHQQLKTGLFSgllktpafrraeseALDRAATWLERVGLLEHANR---QAG-NLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1140 QLLCLARALLTKARVIVMDEATASVDVQTDALLQKVI---RTSFaGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRP 1215
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTP 238
|
..
gi 499478341 1216 TE 1217
Cdd:PRK11300 239 EE 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1014-1223 |
2.73e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1014 LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASvPLEKLRRSLAIIPQDPTLF--MgTIR 1089
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS-PRDAIALGIGMVHQHFMLVpnL-TVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1090 NNLdryneysddeVMGA-------LKHASMWDYVQSLPDGMnsavsegGLN---------LSQGQRQLLCLARALLTKAR 1153
Cdd:COG3845 99 ENI----------VLGLeptkggrLDRKAARARIRELSERY-------GLDvdpdakvedLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1154 VIVMDEATAsvdV----QTDALLqKVIRtSFA--GVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:COG3845 162 ILILDEPTA---VltpqEADELF-EILR-RLAaeGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTAETSEEEL 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
400-598 |
3.04e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.44 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL---------QFVPEMPGRPRMAYVPQEAYIVNTSLLEN 470
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteENVWDIRHKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 471 LQFGEE---VSKEELRRALHNScLS----RDLKEwsgglrteigEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAV 543
Cdd:PRK13650 103 VAFGLEnkgIPHEEMKERVNEA-LElvgmQDFKE----------REPARLSGGQKQRVAIAGAVAMRPKIIILDEATSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 544 DADTENLLCeRLIFGAWKD--VTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK13650 172 DPEGRLELI-KTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
59-537 |
3.25e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.05 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 59 SLIRALRdftRPAYIWYLASSVLALLSPVFVNRFIGTISAGVTAETLPTALIYGVALGLCGFlsglcmqhyFFNSLKAYQ 138
Cdd:COG4615 2 NLLRLLL---RESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVL---------LLLSRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 139 VTTNILNER-LFKHSLKLSQKS-----RQKNQVG--DIVNHMSSDSDNVSDFPMVFGDLISASFLIIGVVAMLFYyIGWS 210
Cdd:COG4615 70 LLLTRLGQHaVARLRLRLSRRIlaaplERLERIGaaRLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAW-LSPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 211 ALAALAVLFILAPLTNYVA-KKFTHLDEEMMEHRDR---RVTLMTQ-----AMNAIRVVKYFawEKSVAKEVTEVREKEL 281
Cdd:COG4615 149 LFLLTLVLLGLGVAGYRLLvRRARRHLRRAREAEDRlfkHFRALLEgfkelKLNRRRRRAFF--DEDLQPTAERYRDLRI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 282 TSRRRLAKAEVVSSLGYLAVSTLVLFVALAVHAwrgekLDAAVI--FTCISLFglLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:COG4615 227 RADTIFALANNWGNLLFFALIGLILFLLPALGW-----ADPAVLsgFVLVLLF--LRGPLSQLVGALPTLSRANVALRKI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 360 --LDyLNEDEVEISTEERTDGAAVGlQMQHFSLR--------HDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMS 429
Cdd:COG4615 300 eeLE-LALAAAEPAAADAAAPPAPA-DFQTLELRgvtyrypgEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 430 LLGEVAPREGSLQFvpemPGRPrmayVP---QEAYIVNTS-------LLENL-QFGEEVSKEELRRALHNSCLSRDLKEW 498
Cdd:COG4615 378 LTGLYRPESGEILL----DGQP----VTadnREAYRQLFSavfsdfhLFDRLlGLDGEADPARARELLERLELDHKVSVE 449
|
490 500 510
....*....|....*....|....*....|....*....
gi 499478341 499 SGGLRTeigekgVNLSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:COG4615 450 DGRFST------TDLSQGQRKRLALLVALLEDRPILVFD 482
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
996-1223 |
3.45e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 996 EISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLA 1075
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1076 IIPQDPTLFMGTIRNNLDRYneysddevmGALKHASMWDYVqSLPDGM--NSAVSEGGLN---------LSQGQRQLLCL 1144
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAY---------GRSPWLSLWGRL-SAEDNArvNQAMEQTRINhladrrltdLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1145 ARALLTKARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQEE 1222
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229
|
.
gi 499478341 1223 I 1223
Cdd:PRK11231 230 L 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
997-1221 |
3.56e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLP---QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEK---- 1069
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 LRRSLAIIPQDP--TLFMGTIRNNLDryneySDDEVMGALKHASMWDYVQSLPD-GMNSAVSEGG-LNLSQGQRQLLCLA 1145
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVA-----FGPQNFGIPKEKAEKIAAEKLEMvGLADEFWEKSpFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1146 RALLTKARVIVMDEATASVDVQTDALLQKVIRTSF-AGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQE 1221
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
680-926 |
3.71e-10 |
|
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: 62.58 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 680 LATLLLGATAATLLPLAQkAWL---SYYSGHQTEWV--ALTAIGIYGLIGVLVLVGSLLNHLFWlDRGIRagkNMHDKML 754
Cdd:cd18557 2 LLFLLISSAAQLLLPYLI-GRLidtIIKGGDLDVLNelALILLAIYLLQSVFTFVRYYLFNIAG-ERIVA---RLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 755 KSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMP---LMVFVIAPVMALYYVLQ 831
Cdd:cd18557 77 SSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWkltLVLLLVIPLLLIASKIY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 832 RDYRRPaREVKRFDSVARSPRYAHfkESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRmfyshvmINRWFSSRIPLVGGLI 911
Cdd:cd18557 157 GRYIRK-LSKEVQDALAKAGQVAE--ESLSNIRTVRSFSAEEKEIRRYSEALDRSYR-------LARKKALANALFQGIT 226
|
250
....*....|....*
gi 499478341 912 SMATAVGVSLSAYYG 926
Cdd:cd18557 227 SLLIYLSLLLVLWYG 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
399-593 |
3.75e-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: 61.23 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMP--GRPRMAYVP-QEAYIVNTSLLENL 471
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdgfdVVKEPaeARRRLGFVSdSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 Q-FGeevskeelrrALHNscLSRD-----LKEWSGGLRTE--IGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAV 543
Cdd:cd03266 100 EyFA----------GLYG--LKGDeltarLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 544 DADTENLLCErlIFGAWKDVTRIVV--THRLEHLAQF-DQVIYIQHGRVQGQG 593
Cdd:cd03266 168 DVMATRALRE--FIRQLRALGKCILfsTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1005-1202 |
3.75e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 60.71 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1005 RYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntasvpleklRRSLAIIPQ----D 1080
Cdd:NF040873 1 GYGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrsevP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1081 PTL--------FMGTI--RNNLDRYNEYSDDEVMGALkhasmwDYVQsLPDGMNSAVSEgglnLSQGQRQLLCLARALLT 1150
Cdd:NF040873 68 DSLpltvrdlvAMGRWarRGLWRRLTRDDRAAVDDAL------ERVG-LADLAGRQLGE----LSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1151 KARVIVMDEATASVDVQTDALLQKVIRTSFA-GVTMLIIAHRLGTIADCDQIV 1202
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCV 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
400-544 |
4.11e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.94 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVaPREGSLQFV---------PEM-PGRPRMAYVPQEAYivnTSLLE 469
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDgqdldglsrRALrPLRRRMQVVFQDPF---GSLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFGEEVSkEELRraLHNSCLSRD---------LKEwsgglrteigekgVNL------------SGGQKQRVALARAFL 528
Cdd:COG4172 378 RMTVGQIIA-EGLR--VHGPGLSAAerrarvaeaLEE-------------VGLdpaarhryphefSGGQRQRIAIARALI 441
|
170
....*....|....*.
gi 499478341 529 RKPQIVLLDDPLSAVD 544
Cdd:COG4172 442 LEPKLLVLDEPTSALD 457
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
997-1207 |
4.12e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQV--LKGITFKVEAGSRVGIIGRTGSGKS-TFFqSLFRFIEAE---EGSISIDGVNTASVP---L 1067
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANgriGGSATFNGREILNLPekeL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1068 EKLR-RSLAIIPQDPTlfmgtirNNLDRYNEYSDD--EVMGALKHAS----------MWDYVQsLPDG---MNSAVSEgg 1131
Cdd:PRK09473 92 NKLRaEQISMIFQDPM-------TSLNPYMRVGEQlmEVLMLHKGMSkaeafeesvrMLDAVK-MPEArkrMKMYPHE-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1132 lnLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDA----LLQKVIRtSFaGVTMLIIAHRLGTIAD-CDQIVEISA 1206
Cdd:PRK09473 162 --FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAqimtLLNELKR-EF-NTAIIMITHDLGVVAGiCDKVLVMYA 237
|
.
gi 499478341 1207 G 1207
Cdd:PRK09473 238 G 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
981-1223 |
4.13e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 981 KPLPEPLRPTWPEFGEI--SVEGLKVRYASHLPqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISID 1058
Cdd:COG3845 240 REVLLRVEKAPAEPGEVvlEVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1059 GVN-TASVPLEKLRRSLAIIPQDPtLFMG-----TIRNN--LDRYN--EYSDdevMGALKHASMWDYVQSL-------PD 1121
Cdd:COG3845 319 GEDiTGLSPRERRRLGVAYIPEDR-LGRGlvpdmSVAENliLGRYRrpPFSR---GGFLDRKAIRAFAEELieefdvrTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1122 GMNSAVSegglNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQ-TDALLQKVIRTSFAGVTMLIIAHRLGTI-ADCD 1199
Cdd:COG3845 395 GPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGaIEFIHQRLLELRDAGAAVLLISEDLDEIlALSD 470
|
250 260
....*....|....*....|....
gi 499478341 1200 QIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:COG3845 471 RIAVMYEGRIVGEVPAAEATREEI 494
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
399-590 |
4.16e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE----MPGRPRMA-------YVPQEAYIVNT-S 466
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqMDEEARAKlrakhvgFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENLQF-------GEEVSKEELRRALHNSCLSRDLKEWSGglrteigekgvNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK10584 105 ALENVELpallrgeSSRQSRNGAKALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 540 LSAVDADTENLLCErLIFGAWKD--VTRIVVTHRLEHLAQFDQVIYIQHGRVQ 590
Cdd:PRK10584 174 TGNLDRQTGDKIAD-LLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1017-1227 |
4.33e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1017 ITFKveAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQD-PTLFMGTIRN----- 1090
Cdd:PRK10575 32 LTFP--AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRElvaig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1091 ------NLDRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEATASV 1164
Cdd:PRK10575 110 rypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1165 DV--QTD--ALLQKVIRTSfaGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQEEIEESL 1227
Cdd:PRK10575 179 DIahQVDvlALVHRLSQER--GLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGETLEQI 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1015-1223 |
5.05e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1015 KGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVN-TASVPLEKLRRSLAIIPQD--PTLFMG--TIR 1089
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPLDAVKKGMAYITESrrDNGFFPnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1090 NNLDRYNEYSDDE---VMGALKHASMWDYVQSLPDGMN---SAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATAS 1163
Cdd:PRK09700 360 QNMAISRSLKDGGykgAMGLFHEVDEQRTAENQRELLAlkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 1164 VDVQTDALLQKVIRT-SFAGVTMLIIAHRLGTI-ADCDQIVEISAGEVKSIRRPT-EFSQEEI 1223
Cdd:PRK09700 440 IDVGAKAEIYKVMRQlADDGKVILMVSSELPEIiTVCDRIAVFCEGRLTQILTNRdDMSEEEI 502
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1013-1189 |
5.49e-10 |
|
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: 60.20 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPTLFMGTIRNNL 1092
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1093 DRYNEY-SDDEVMGALKHASMWDYvQSLPDGmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDAL 1171
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170
....*....|....*...
gi 499478341 1172 LQKVIRTSFAGVTMLIIA 1189
Cdd:cd03231 164 FAEAMAGHCARGGMVVLT 181
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
76-359 |
6.72e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 61.78 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIG--TISAGVTAETLPTALIYGVALGLCGFLSGLCMqhyFFNSLKAYQVTTNiLNERLFKHSL 153
Cdd:cd18778 9 LLSTLLGLVPPWLIRELVDlvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRI---YLNHVAEQKVVAD-LRSDLYDKLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 154 KLSQKSRQKNQVGDIVNHMSSDSDNVSDFpMVFG--DLISASFLIIGVVAMLFyYIGWsALAALAVL---FILAPLTNY- 227
Cdd:cd18778 85 RLSLRYFDDRQTGDLMSRVINDVANVERL-IADGipQGITNVLTLVGVAIILF-SINP-KLALLTLIpipFLALGAWLYs 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 228 --VAKKFthldeemmehrdRRVTLMTQAMNA--------IRVVKYFAWE----KSVAKEVTEVREKELTSRRRLA----K 289
Cdd:cd18778 162 kkVRPRY------------RKVREALGELNAllqdnlsgIREIQAFGREeeeaKRFEALSRRYRKAQLRAMKLWAifhpL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 290 AEVVSSLGYLAVstlvlfvaLAVHAWR--GEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18778 230 MEFLTSLGTVLV--------LGFGGRLvlAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
989-1190 |
6.93e-10 |
|
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: 63.03 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 989 PTWPEFGE--ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFIEAEE----GSISI-DGVN 1061
Cdd:TIGR03719 313 PPGPRLGDkvIEAENLTKAFGDKL--LIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMITGQEqpdsGTIEIgETVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1062 TASVplEKLRRSLaiipqDP--TLFmgtirnnldryneysdDEVMGALKHASMWDYVqslpdgMNSAVSEGGLN------ 1133
Cdd:TIGR03719 387 LAYV--DQSRDAL-----DPnkTVW----------------EEISGGLDIIKLGKRE------IPSRAYVGRFNfkgsdq 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1134 ------LSQGQRQLLCLARALLTKARVIVMDEATASVDVQT-----DALLqkvirtSFAGVTMlIIAH 1190
Cdd:TIGR03719 438 qkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETlraleEALL------NFAGCAV-VISH 498
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
974-1217 |
7.25e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 974 PGEVS--VLKPLPEPLRPTWPEFGE--ISVEGLKVRYASHLPQVLK---GITFKVEAGSRVGIIGRTGSGKSTFFQSLFR 1046
Cdd:TIGR03269 253 PDEVVavFMEGVSEVEKECEVEVGEpiIKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1047 FIEAEEGSISI----DGVN-TASVPLEKLR--RSLAIIPQDPTLF-MGTIRNNL------DRYNEYSDDEVMGALKHASM 1112
Cdd:TIGR03269 333 VLEPTSGEVNVrvgdEWVDmTKPGPDGRGRakRYIGILHQEYDLYpHRTVLDNLteaiglELPDELARMKAVITLKMVGF 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1113 WD-YVQSLPDGMNSavsegglNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIA 1189
Cdd:TIGR03269 413 DEeKAEEILDKYPD-------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVS 485
|
250 260
....*....|....*....|....*....
gi 499478341 1190 HRLGTIAD-CDQIVEISAGEVKSIRRPTE 1217
Cdd:TIGR03269 486 HDMDFVLDvCDRAALMRDGKIVKIGDPEE 514
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
996-1217 |
7.69e-10 |
|
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: 60.82 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 996 EISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFI----EAEEGSISIDGVNTASVPLEKlr 1071
Cdd:cd03296 2 SIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTT----LLRLIagleRPDSGTILFGGEDATDVPVQE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLAIIPQDPTLF--MgTIRNNL-------DRYNEYSDDE----VMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQ 1138
Cdd:cd03296 74 RNVGFVFQHYALFrhM-TVFDNVafglrvkPRSERPPEAEirakVHELLKLVQLDWLADRYPA-----------QLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1139 RQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRT--SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRP 1215
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTP 221
|
..
gi 499478341 1216 TE 1217
Cdd:cd03296 222 DE 223
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
678-966 |
8.61e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 61.37 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILATLLLGATAATLLP------LAQKAWLSYYSGHQTEWVALTAIGIYGLIGVLVLVGSLLNHLF-WLdrGIRAGKNMH 750
Cdd:cd18563 2 ILGFLLMLLGTALGLVPpyltkiLIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLaRL--GERITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 751 DKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMP---LMVFVIAPVMAL- 826
Cdd:cd18563 80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWklaLLVLIPVPLVVWg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 827 -YYVLQRDYRRPAREVKRFDSVArspryAHFKESLQGLVVIRSFNKGPWFMQNFYAKlshSNRMFYSHVMINRWFSSRIP 905
Cdd:cd18563 160 sYFFWKKIRRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAFGQEKREIKRFDEA---NQELLDANIRAEKLWATFFP 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 906 LVGGLISMAT----AVGVsLSAYYGVMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIER 966
Cdd:cd18563 232 LLTFLTSLGTlivwYFGG-RQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1012-1223 |
8.75e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDP--TLFMGTIR 1089
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1090 N-------NLDRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEATA 1162
Cdd:PRK13652 98 QdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1163 SVDVQTDALLQKVIR--TSFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTE-FSQEEI 1223
Cdd:PRK13652 167 GLDPQGVKELIDFLNdlPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEiFLQPDL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
399-588 |
9.05e-10 |
|
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: 62.65 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLL--MS-----LLGEVAPREGSlqfvpempgrpRMAYVPQEAYIVNT-SLLEN 470
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLriMAgvdkdFNGEARPQPGI-----------KVGYLPQEPQLDPTkTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 471 LQFG-----------EEVS----------------KEELRRAL-----HNscLSRDLKEWSGGLRTEIGEKGV-NLSGGQ 517
Cdd:TIGR03719 89 VEEGvaeikdaldrfNEISakyaepdadfdklaaeQAELQEIIdaadaWD--LDSQLEIAMDALRCPPWDADVtKLSGGE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 518 KQRVALARAFLRKPQIVLLDDPLSAVDADTEnllcerlifgAWkdvtrivvthrLE-HLAQFD-QVIYIQHGR 588
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESV----------AW-----------LErHLQEYPgTVVAVTHDR 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
399-642 |
9.64e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.26 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSS-------LLMSLLGEV--------------------------APREGSLQFVP 445
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIewifkdeknkkktkekekvleklviqKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 446 EMpgRPRMAYVPQ--EAYIVNTSLLENLQFGEE---VSKEE-LRRAlhnsclsRDLKEWSGgLRTEIGEKG-VNLSGGQK 518
Cdd:PRK13651 102 EI--RRRVGVVFQfaEYQLFEQTIEKDIIFGPVsmgVSKEEaKKRA-------AKYIELVG-LDESYLQRSpFELSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 519 QRVALARAFLRKPQIVLLDDPLSAVD-ADTENLLcerLIFGAWKDV--TRIVVTHRLEH-LAQFDQVIYIQHGRVQGQG- 593
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDpQGVKEIL---EIFDNLNKQgkTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGd 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 594 TFSELVKTcapfaEFYKEH-----------GKTQGEGHEVRPAETAQEAAS-INTELEAKT 642
Cdd:PRK13651 249 TYDILSDN-----KFLIENnmeppkllnfvNKLEKKGIDVPKVTSIEELASeINMYLEKKN 304
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
383-598 |
1.18e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSL--RHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLL------------GEVAPREGSLQFVPEMP 448
Cdd:PRK15134 6 LAIENLSVafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILrllpsppvvypsGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 449 GRP----RMAYVPQEAyIVNTSLLENL--QFGEEVS-----KEELRRALHNSCLSRDlkewsgGLR---TEIGEKGVNLS 514
Cdd:PRK15134 86 LRGvrgnKIAMIFQEP-MVSLNPLHTLekQLYEVLSlhrgmRREAARGEILNCLDRV------GIRqaaKRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 515 GGQKQRVALARAFLRKPQIVLLDDPLSAVD----ADTENLLCE-------RLIFgawkdvtrivVTHRLEHLAQF-DQVI 582
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRElqqelnmGLLF----------ITHNLSIVRKLaDRVA 228
|
250
....*....|....*.
gi 499478341 583 YIQHGRVQGQGTFSEL 598
Cdd:PRK15134 229 VMQNGRCVEQNRAATL 244
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
678-945 |
1.18e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 60.94 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILATLLLGATAATLLP--LAQKAWLSYYSGHQTE---WVALTAIGIYGLIGVLVLVGSLLnhLFWLdrGIRAGKNMHDK 752
Cdd:cd18545 3 LLALLLMLLSTAASLAGpyLIKIAIDEYIPNGDLSgllIIALLFLALNLVNWVASRLRIYL--MAKV--GQRILYDLRQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 753 MLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMP---LMVFVIAPVMALY-Y 828
Cdd:cd18545 79 LFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVrlaLVTLAVLPLLVLVvF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 829 VLQRDYRRPAREVKRfdsvARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFyAKLSHSNR-MFYSHVMINRWFSSriplv 907
Cdd:cd18545 159 LLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSFAREDENEEIF-DELNRENRkANMRAVRLNALFWP----- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499478341 908 ggLISMATAVGVSLSAYYGVMDAG----TAGLV---TLYSLSFWG 945
Cdd:cd18545 229 --LVELISALGTALVYWYGGKLVLggaiTVGVLvafIGYVGRFWQ 271
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
997-1208 |
1.46e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQV--LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGV-----NTASVPL-- 1067
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrSRQVIELse 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1068 ---EKLRR----SLAIIPQDPTLFMG-------TIRNNLDRYNEYSDDEVMGALKHasMWDYVQsLPDGmNSAVSEGGLN 1133
Cdd:PRK10261 93 qsaAQMRHvrgaDMAMIFQEPMTSLNpvftvgeQIAESIRLHQGASREEAMVEAKR--MLDQVR-IPEA-QTILSRYPHQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1134 LSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAGVTM--LIIAHRLGTIAD-CDQIVEISAGE 1208
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEiADRVLVMYQGE 246
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
996-1217 |
1.48e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.32 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 996 EISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFI----EAEEGSISIDG--VNTASVPLEk 1069
Cdd:COG1118 2 SIEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTT----LLRIIagleTPDSGRIVLNGrdLFTNLPPRE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 lrRSLAIIPQDPTLF--MgTIRNN-------LDRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsegglNLSQGQRQ 1140
Cdd:COG1118 75 --RRVGFVFQHYALFphM-TVAENiafglrvRPPSKAEIRARVEELLELVQLEGLADRYPS-----------QLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1141 LLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIAH------RLgtiadCDQIVEISAGEVKSI 1212
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQV 215
|
....*
gi 499478341 1213 RRPTE 1217
Cdd:COG1118 216 GTPDE 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
397-598 |
1.53e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 397 SDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE---------MPGRPRMAYVPQ--EAYIVNT 465
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkkslLEVRKTVGIVFQnpDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 SLLENLQFGE---EVSKEELRRALHNSclsrdLKEwsgglrteIGEKGV------NLSGGQKQRVALARAFLRKPQIVLL 536
Cdd:PRK13639 95 TVEEDVAFGPlnlGLSKEEVEKRVKEA-----LKA--------VGMEGFenkpphHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 537 DDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYaDKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1003-1206 |
1.57e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.34 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1003 KVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPT 1082
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1083 LFMGTIRNNL----DRYNEYSDDEVMGAlkhasmwDYVQ-SLPDGM-NSAVSEgglnLSQGQRQLLCLARALLTKARVIV 1156
Cdd:PRK10247 92 LFGDTVYDNLifpwQIRNQQPDPAIFLD-------DLERfALPDTIlTKNIAE----LSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1157 MDEATASVDVQTDALLQKVIR--TSFAGVTMLIIAHRLGTIADCDQIVEISA 1206
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHryVREQNIAVLWVTHDKDEINHADKVITLQP 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1012-1201 |
1.65e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTA-SVPLEKLRRSLAIIPQD----PTLfmg 1086
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQElnliPQL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 TIRNNLDRYNEYSDdeVMGALKHASMWDYVQSLPDGMNSAVSEGGL--NLSQGQRQLLCLARALLTKARVIVMDEAT-AS 1163
Cdd:PRK10762 95 TIAENIFLGREFVN--RFGRIDWKKMYAEADKLLARLNLRFSSDKLvgELSIGEQQMVEIAKVLSFESKVIIMDEPTdAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499478341 1164 VDVQTDALLqKVIRT-SFAGVTMLIIAHRLGTIAD-CDQI 1201
Cdd:PRK10762 173 TDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEiCDDV 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
402-656 |
2.08e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG-------RPRMAYVPQE-AYIVNTSLLE 469
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdgvdIAKISDaelrevrRKKIAMVFQSfALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFGEE---VSKEELRRALHNSCLSRDLKEWSGGLRTEigekgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDAD 546
Cdd:PRK10070 126 NTAFGMElagINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 547 TENLLCERLI-FGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVKTCApfaefyKEHGKTQGEGHEVRP 624
Cdd:PRK10070 199 IRTEMQDELVkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPA------NDYVRTFFRGVDISQ 272
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499478341 625 AETAQEAASINTELEAKTT---------RVTEDEDREVGAV 656
Cdd:PRK10070 273 VFSAKDIARRTPNGLIRKTpgfgprsalKLLQDEDREYGYV 313
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
400-589 |
2.32e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.76 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEM-----------PGRPRMAYVPQ--EAYIVNTS 466
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikQIRKKVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENLQFGEE---VSKEEL----RRALHNSCLSRDLKEWSGglrteigekgVNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK13649 103 VLKDVAFGPQnfgVSQEEAealaREKLALVGISESLFEKNP----------FELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499478341 540 LSAVDADTENLLCErlIFGAW--KDVTRIVVTHRLEHLAQF-DQVIYIQHGRV 589
Cdd:PRK13649 173 TAGLDPKGRKELMT--LFKKLhqSGMTIVLVTHLMDDVANYaDFVYVLEKGKL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
399-593 |
2.46e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLgEVAPREGSLQFVPE----------MPGRPRMAYVPQEAyivNTSLL 468
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQplhnlnrrqlLPVRHRIQVVFQDP---NSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 469 ENLQFgEEVSKEELRraLHNSCLSRDLKEWSggLRTEIGEKGVN----------LSGGQKQRVALARAFLRKPQIVLLDD 538
Cdd:PRK15134 377 PRLNV-LQIIEEGLR--VHQPTLSAAQREQQ--VIAVMEEVGLDpetrhrypaeFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 539 PLSAVDADTENLLCERLifgawkdvTRIVVTHRLEHL----------AQFDQVIYIQHGRVQGQG 593
Cdd:PRK15134 452 PTSSLDKTVQAQILALL--------KSLQQKHQLAYLfishdlhvvrALCHQVIVLRQGEVVEQG 508
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
76-359 |
2.50e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 59.81 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRfigTISAGVTAETLPTALIYGVALGLCGFLSGLCMQhyffnslkAYQVTTNILNE--------R 147
Cdd:cd18546 9 VVDTAASLAGPLLVRY---GIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQR--------AQTRLTGRTGErllydlrlR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 148 LFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMV-FGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTN 226
Cdd:cd18546 78 VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTgLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 227 YVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSLGYLAVSTLVL 306
Cdd:cd18546 158 WFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLAT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 307 FVALAVHAWR--GEKLDAAVIFTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18546 238 AAVLLVGAWRvaAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1013-1191 |
2.57e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDgvntasVPLEKLRRSLAIIpqdptlfmgtirNNL 1092
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFGREASLI------------DAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1093 DRynEYSDDEVMGALKHAsmwdyvqslpdGMNSAV------SEgglnLSQGQRQLLCLARALLTKARVIVMDEATASVDV 1166
Cdd:COG2401 107 GR--KGDFKDAVELLNAV-----------GLSDAVlwlrrfKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*....
gi 499478341 1167 QTDAL----LQKVIRTsfAGVTMLIIAHR 1191
Cdd:COG2401 170 QTAKRvarnLQKLARR--AGITLVVATHH 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
400-573 |
2.81e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRPR------------MAYVPQEAYIV-NTS 466
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL----IDGQEMrfasttaalaagVAIIYQELHLVpEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENLQFGEEVSKEELRRalhnsclSRDLKEWSGGLRTEIGE------KGVNLSGGQKQRVALARAFLRKPQIVLLDDPL 540
Cdd:PRK11288 96 VAENLYLGQLPHKGGIVN-------RRLLNYEAREQLEHLGVdidpdtPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 499478341 541 SAVDA-DTENLLceRLIfGAWKDVTRIV--VTHRLE 573
Cdd:PRK11288 169 SSLSArEIEQLF--RVI-RELRAEGRVIlyVSHRME 201
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
392-539 |
3.10e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 392 HDGAVSdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPG----RPRMAYVPQEAYIV 463
Cdd:PRK11614 14 HYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFdgkdITDWQTakimREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 N-TSLLENLQFGE-EVSKEELRRALhnsclsrdlkEWSGGLRTEIGEKGVN----LSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:PRK11614 93 SrMTVEENLAMGGfFAERDQFQERI----------KWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLD 162
|
..
gi 499478341 538 DP 539
Cdd:PRK11614 163 EP 164
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
397-607 |
3.48e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 397 SDV--LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF---------VPEMPGRPRMAYVPQEAYIVNT 465
Cdd:PRK13642 18 SDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdgelltaenVWNLRRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 SLLENLQFGEE---VSKEELRRALHNSCLSRDLKEWSGglrteigEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSA 542
Cdd:PRK13642 98 TVEDDVAFGMEnqgIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 543 VDADTENLLCErlIFGAWKD---VTRIVVTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPFAE 607
Cdd:PRK13642 171 LDPTGRQEIMR--VIHEIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1012-1209 |
3.56e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQDPT--------- 1082
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1083 --LFMGTIRNNLDRYNEYSDDEVMGALKHASMwdyvqsLPDGMNSAVSEgglnLSQGQRQLLCLARALLTKARVIVMDEA 1160
Cdd:PRK15112 107 sqILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPDHASYYPHM----LAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1161 TASVDV----QTDALLQKVIRTSfaGVTMLIIAHRLGTIAD-CDQIVEISAGEV 1209
Cdd:PRK15112 177 LASLDMsmrsQLINLMLELQEKQ--GISYIYVTQHLGMMKHiSDQVLVMHQGEV 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1013-1059 |
4.08e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.55 E-value: 4.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 499478341 1013 VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG 1059
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
997-1190 |
5.12e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 58.72 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLPQ--VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVntasvPLEKLRRSL 1074
Cdd:COG4525 4 LTVRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-----PVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQDPTLFmgTIRNNLDryneysddEVMGALK---------HASMWDYVQ--SLPDGMNSAVSEgglnLSQGQRQLLC 1143
Cdd:COG4525 79 GVVFQKDALL--PWLNVLD--------NVAFGLRlrgvpkaerRARAEELLAlvGLADFARRRIWQ----LSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1144 LARALLTKARVIVMDEATASVDV----QTDALLQKVIRTSfaGVTMLIIAH 1190
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDAltreQMQELLLDVWQRT--GKGVFLITH 193
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
996-1192 |
5.77e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 996 EISVEGLKVRYASHLP---QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISI----DGVNTASVPLE 1068
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1069 K--------------------LRRSLAIIPQ--DPTLFMGTIRNNLdRYNEYSddevMG-----ALKHASMWDYVQSLPD 1121
Cdd:PRK13651 82 KvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDI-IFGPVS----MGvskeeAKKRAAKYIELVGLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1122 gmnSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQ-TDALLQKVIRTSFAGVTMLIIAHRL 1192
Cdd:PRK13651 157 ---SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDL 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1012-1190 |
5.86e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGS-----RVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEklrrslaIIPQdptlFMG 1086
Cdd:cd03237 8 KTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKAD----YEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 TIRNNL-----DRYNE-YSDDEVMGALKHASMWDyvQSLPDgmnsavsegglnLSQGQRQLLCLARALLTKARVIVMDEA 1160
Cdd:cd03237 77 TVRDLLssitkDFYTHpYFKTEIAKPLQIEQILD--REVPE------------LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190
....*....|....*....|....*....|...
gi 499478341 1161 TASVDVQTDALLQKVIRtSFA---GVTMLIIAH 1190
Cdd:cd03237 143 SAYLDVEQRLMASKVIR-RFAennEKTAFVVEH 174
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
981-1209 |
6.86e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.15 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 981 KPLPEPLRPTWPefgeISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISidgv 1060
Cdd:PRK11247 1 MMNTARLNQGTP----LLLNAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1061 nTASVPLEKLRRSLAIIPQDPTL--FMGTIrnnldryneysdDEVMGALKHASMWDYVQSLPD-GMNSAVSEGGLNLSQG 1137
Cdd:PRK11247 71 -AGTAPLAEAREDTRLMFQDARLlpWKKVI------------DNVGLGLKGQWRDAALQALAAvGLADRANEWPAALSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 1138 QRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIAHRLG-TIADCDQIVEISAGEV 1209
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
391-551 |
8.49e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 391 RHDGAVSDVLHdvnVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VPEMPG-RPR-MAYVPQ-EAYIVNT 465
Cdd:PRK13543 21 RNEEPVFGPLD---FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdgKTATRGdRSRfMAYLGHlPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 466 SLLENLQFgeevskeelRRALHnsclSRDLKEWSGGLRTEIGEKGV------NLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK13543 98 STLENLHF---------LCGLH----GRRAKQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170
....*....|..
gi 499478341 540 LSAVDADTENLL 551
Cdd:PRK13543 165 YANLDLEGITLV 176
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1012-1223 |
9.65e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNtasvpLEKLRRSLAiipqdPTLFMGTIRNN 1091
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-----YNKLDHKLA-----AQLGIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1092 LDRYNEYSDDE-----------VMGA--LKHASMWDYVQSLPD--GMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIV 1156
Cdd:PRK09700 89 LSVIDELTVLEnlyigrhltkkVCGVniIDWREMRVRAAMMLLrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 1157 MDEATASV-DVQTDALLQKVIRTSFAGVTMLIIAHRLGTI-ADCDQIVEISAGEVKSIRRPTEFSQEEI 1223
Cdd:PRK09700 169 MDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIrRICDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
678-879 |
1.01e-08 |
|
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: 58.18 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILATLLLGATAATLLP-LAQKAWLSYYSGHQTEW-VALTAIGIY-GLIGVLVLVGSLLNHLF-WLDRGI--RAGKNMHD 751
Cdd:cd18547 3 LVIILAIISTLLSVLGPyLLGKAIDLIIEGLGGGGgVDFSGLLRIlLLLLGLYLLSALFSYLQnRLMARVsqRTVYDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 752 KMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLM---VFVIAPVMALYY 828
Cdd:cd18547 83 DLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtliVLVTVPLSLLVT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 829 VL-----QRDYRrparevKRFDSVARSprYAHFKESLQGLVVIRSFNKGPWFMQNF 879
Cdd:cd18547 163 KFiakrsQKYFR------KQQKALGEL--NGYIEEMISGQKVVKAFNREEEAIEEF 210
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
76-359 |
1.25e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 57.87 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFvNRFIgtISAGVTAETLPTALIYGVALGLCGFLSGLCMqhYFFNSLkAYQVTTNI---LNERLFKHS 152
Cdd:cd18540 12 LLVALLDAVFPLL-TKYA--IDHFITPGTLDGLTGFILLYLGLILIQALSV--FLFIRL-AGKIEMGVsydLRKKAFEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 153 LKLSQKSRQKNQVGDIVNHMSSDSDNVSD-FPMVFGDLISASFLIIGVVAMLFyYIGWS-ALAALAVLFILAPLTNYVAK 230
Cdd:cd18540 86 QTLSFSYFDKTPVGWIMARVTSDTQRLGEiISWGLVDLVWGITYMIGILIVML-ILNWKlALIVLAVVPVLAVVSIYFQK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 231 KFthldeeMMEHRDRRVT--LMTQAMN----AIRVVKYFAWEKSVAKEVtevreKELTSRRRLA--KAEVVSSLgYLAVS 302
Cdd:cd18540 165 KI------LKAYRKVRKInsRITGAFNegitGAKTTKTLVREEKNLREF-----KELTEEMRRAsvRAARLSAL-FLPIV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 303 TLVLFVALAVHAWRGEKLDAAVIFT--CISLF-----GLLEgPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18540 233 LFLGSIATALVLWYGGILVLAGAITigTLVAFisyatQFFE-PIQQLARVLAELQSAQASAERV 295
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
413-570 |
1.53e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 413 LAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpempgRPRMAYVPQeaYIVNTS------LLENL--QFGEEVSKEELRR 484
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP------ELKISYKPQ--YIKPDYdgtvedLLRSItdDLGSSYYKSEIIK 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 485 ALhnsclsrdlkewsgGLrTEIGEKGVN-LSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADtENLLCERLI--FGAWK 561
Cdd:PRK13409 440 PL--------------QL-ERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRLAVAKAIrrIAEER 503
|
....*....
gi 499478341 562 DVTRIVVTH 570
Cdd:PRK13409 504 EATALVVDH 512
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1017-1225 |
1.60e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1017 ITFKVEAGSRVGIIGRTGSGKSTFFQSLF-RFIEAEEGSISIDG--VNTASvPLEKLRRSLAIIPQDP-----TLFMGTI 1088
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGkpVKIRN-PQQAIAQGIAMVPEDRkrdgiVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1089 RN----NLDRYNEYS--DDevmgALKHASMWDYVQSLPDGMNSAVSEGGlNLSQGQRQLLCLARALLTKARVIVMDEATA 1162
Cdd:PRK13549 360 KNitlaALDRFTGGSriDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1163 SVDVQTDALLQKVIrTSFA--GVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTEFSQEEIEE 1225
Cdd:PRK13549 435 GIDVGAKYEIYKLI-NQLVqqGVAIIVISSELPEVLGlSDRVLVMHEGKLKGDLINHNLTQEQVME 499
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
415-612 |
1.63e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.94 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 415 IVGPVGAGKSSLLMSLLGEVAPREGSLQ---------FVPEMPG--------------RPRMAYVPQ--EAYIVNTSLLE 469
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiyigdkKNNHELItnpyskkiknfkelRRRVSMVFQfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFGE---EVSKEELRR---------ALHNSCLSRDLKEwsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:PRK13631 137 DIMFGPvalGVKKSEAKKlakfylnkmGLDDSYLERSPFG---------------LSGGQKRRVAIAGILAIQPEILIFD 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 538 DPLSAVDADTENLLCErLIFGAWKD-VTRIVVTHRLEHLAQF-DQVIYIQHGrvqgqgtfsELVKTCAPFAEFYKEH 612
Cdd:PRK13631 202 EPTAGLDPKGEHEMMQ-LILDAKANnKTVFVITHTMEHVLEVaDEVIVMDKG---------KILKTGTPYEIFTDQH 268
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
403-599 |
2.16e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.28 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 403 VNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFV------------PEMPGR--PRMAYVPQE-AYIVNTSL 467
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpgPDGRGRakRYIGILHQEyDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENL--QFGEEVSKE-ELRRALHNsclsrdLKewSGGLRTEIGEKGVN-----LSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:TIGR03269 383 LDNLteAIGLELPDElARMKAVIT------LK--MVGFDEEKAEEILDkypdeLSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 540 LSAVDADTENLLCERlIFGAWKDV--TRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELV 599
Cdd:TIGR03269 455 TGTMDPITKVDVTHS-ILKAREEMeqTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
76-313 |
2.32e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 56.82 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFV----NRFIGTISAgvtaETLpTALIYGV--ALGLCGFLSGLcmQHYFFNSLKAyqVTTNILNERLF 149
Cdd:cd18566 12 LFINILALATPLFIlqvyDRVIPNESI----PTL-QVLVIGVviAILLESLLRLL--RSYILAWIGA--RFDHRLSNAAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 150 KHSLKLSQKSRQKNQVGDIVNHMSsDSDNVSDF---PMVFGdLISASFLIIGVVAMlFYYIGWSALAALAVLFILAPLTN 226
Cdd:cd18566 83 EHLLSLPLSFFEREPSGAHLERLN-SLEQIREFltgQALLA-LLDLPFVLIFLGLI-WYLGGKLVLVPLVLLGLFVLVAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 227 YVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAK-AEVVSSLGYL-AVSTL 304
Cdd:cd18566 160 LLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKiNAVAQTLGQLfSQVSM 239
|
....*....
gi 499478341 305 VLFVALAVH 313
Cdd:cd18566 240 VAVVAFGAL 248
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
409-610 |
2.46e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 409 AGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqFVPEMP----------GRPRMAYV-------PQE--AYIVNTSLLE 469
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPlhfgdysyrsQRIRMIFQdpstslnPRQriSQILDFPLRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLrteigekgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTE- 548
Cdd:PRK15112 117 NTDLEPEQREKQIIETLRQVGLLPDHASYYPHM----------LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRs 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 549 ---NLLCErliFGAWKDVTRIVVTHRL---EHLAqfDQVIYIQHGRVQGQGTFSELVktCAPFAEFYK 610
Cdd:PRK15112 187 qliNLMLE---LQEKQGISYIYVTQHLgmmKHIS--DQVLVMHQGEVVERGSTADVL--ASPLHELTK 247
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1012-1197 |
2.87e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLfRFIEA-EEGSISIDGVNTASVPLEK---LRRSLAIIPQDPtlfMGT 1087
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLL-TMIETpTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNP---YGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1088 ----------------IRNNLDRYNEYSDDEVMGA---LK--HASMWDYVqslpdgmnsavsegglnLSQGQRQLLCLAR 1146
Cdd:PRK11308 105 lnprkkvgqileepllINTSLSAAERREKALAMMAkvgLRpeHYDRYPHM-----------------FSGGQRQRIAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 1147 ALLTKARVIVMDEATASVDV--QTDAL-----LQKVIRTSFagvtmLIIAHRLGT---IAD 1197
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVsvQAQVLnlmmdLQQELGLSY-----VFISHDLSVvehIAD 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
399-539 |
2.88e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPempgRPRMAYVPQ---EAYIVNTSLLENL-QFG 474
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE----NANIGYYAQdhaYDFENDLTLFDWMsQWR 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 475 EEVSKEELRRALhnscLSRDLkeWSGglrTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:PRK15064 410 QEGDDEQAVRGT----LGRLL--FSQ---DDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1012-1159 |
3.85e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEK-LRRSLAIIPQDPTLFMG-TIR 1089
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1090 NNLdryneysddeVMGALkHASMWDYVQSL-------PDGMNSAVSEGGlNLSQGQRQLLCLARALLTKARVIVMDE 1159
Cdd:PRK11614 99 ENL----------AMGGF-FAERDQFQERIkwvyelfPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
399-590 |
4.14e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMpgrpRMAYVPQEAyivntslLENLQfGEEVS 478
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI----KLGYFAQHQ-------LEFLR-ADESP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 479 KEELRRaLHNSCLSRDLKEWSGGLR------TEIGEKgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLC 552
Cdd:PRK10636 395 LQHLAR-LAPQELEQKLRDYLGGFGfqgdkvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499478341 553 ERLI-F-GAWkdvtrIVVTHRLEHLAQFDQVIYIQH-GRVQ 590
Cdd:PRK10636 471 EALIdFeGAL-----VVVSHDRHLLRSTTDDLYLVHdGKVE 506
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
678-967 |
5.13e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 55.90 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILATLLLGATAATLLPLAQKaWL--SYYSGHQTEWVALTAIGIyglIGVlVLVGSLLNHL--FWLDR-GIRAGKNMHDK 752
Cdd:cd18542 3 LAILALLLATALNLLIPLLIR-RIidSVIGGGLRELLWLLALLI---LGV-ALLRGVFRYLqgYLAEKaSQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 753 MLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGL---MPLMVFVIAPVMALYYV 829
Cdd:cd18542 78 LYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSInwkLTLISLAIIPFIALFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 830 -----LQRDYRRPAREVKRFDSVArspryahfKESLQGLVVIRSFNKGPWFMQNFYAKlshsNRMFYSHVM-INRWFSSR 903
Cdd:cd18542 158 vffkkVRPAFEEIREQEGELNTVL--------QENLTGVRVVKAFAREDYEIEKFDKE----NEEYRDLNIkLAKLLAKY 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 904 IPLVGGLISMATAVGVSLSAYY---GVMDAGTagLVTLYSLSfwGFLNWGVR----IFADIESRMTSIERL 967
Cdd:cd18542 226 WPLMDFLSGLQIVLVLWVGGYLvinGEITLGE--LVAFISYL--WMLIWPVRqlgrLINDMSRASASAERI 292
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
997-1165 |
7.10e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.11 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKlrRSLAI 1076
Cdd:PRK09452 15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLF--MgTIRNNLD---RYNEYSDDE----VMGALKHASMWDYVQSLPdgmnsavseggLNLSQGQRQLLCLARA 1147
Cdd:PRK09452 91 VFQSYALFphM-TVFENVAfglRMQKTPAAEitprVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARA 158
|
170
....*....|....*...
gi 499478341 1148 LLTKARVIVMDEATASVD 1165
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD 176
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
410-584 |
8.50e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.76 E-value: 8.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 410 GSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpempgrprmayvpqeayivntslleNLQFGEEVSKEELRralhns 489
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------DGEDILEEVLDQLL------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 490 clsrdlkewsgglRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFGAWKDVTR---- 565
Cdd:smart00382 51 -------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSeknl 117
|
170 180
....*....|....*....|....*..
gi 499478341 566 --IVVTHRLEHLAQ------FDQVIYI 584
Cdd:smart00382 118 tvILTTNDEKDLGPallrrrFDRRIVL 144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
410-570 |
9.82e-08 |
|
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: 56.33 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 410 GSSLAIVGPVGAGKSSLLMSLLGEVAPREGslqfvpEMPGRPRMAYVPQeaYIVNTSLLENLQFGEEVSKEELRRALHNS 489
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEG------EVDEDLKISYKPQ--YISPDYDGTVEEFLRSANTDDFGSSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 490 CLSRDLkewsgGLrTEIGEKGV-NLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADtENLLCERLI--FGAWKDVTRI 566
Cdd:COG1245 438 EIIKPL-----GL-EKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRLAVAKAIrrFAENRGKTAM 510
|
....
gi 499478341 567 VVTH 570
Cdd:COG1245 511 VVDH 514
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
998-1193 |
9.86e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.55 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 998 SVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKL----RRS 1073
Cdd:PRK11701 8 SVRGLTKLYGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAiipqdptlfmgtirnnldryneysddevmgalkhASMWDYVQSLP-DGMNSAVSEGGlNL------------------ 1134
Cdd:PRK11701 86 LL----------------------------------RTEWGFVHQHPrDGLRMQVSAGG-NIgerlmavgarhygdirat 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1135 ----------------------SQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFA--GVTMLIIAH 1190
Cdd:PRK11701 131 agdwlerveidaariddlpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTH 210
|
...
gi 499478341 1191 RLG 1193
Cdd:PRK11701 211 DLA 213
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
673-966 |
1.11e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 54.79 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 673 KFTKPLILATLLLGATAAtLLPLAQKAWLSYYSGHQTEWVALTAIGIYGLigvLVLVGSLLNHLFwldrgIR-AGK---- 747
Cdd:cd18540 2 KLLILLIILMLLVALLDA-VFPLLTKYAIDHFITPGTLDGLTGFILLYLG---LILIQALSVFLF-----IRlAGKiemg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 748 ---NMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGL---MPLMVFVIA 821
Cdd:cd18540 73 vsyDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILnwkLALIVLAVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 822 PVMAL-YYVLQRDYRRPAREVKRFDSvarspRY-AHFKESLQGLVVIRSFNKGPWFMQNFyakLSHSNRMfYSHVMINRW 899
Cdd:cd18540 153 PVLAVvSIYFQKKILKAYRKVRKINS-----RItGAFNEGITGAKTTKTLVREEKNLREF---KELTEEM-RRASVRAAR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 900 FSS-RIPLVGGLISMATAV-----GVSLSAyyGVMDAGTAGLVTLYSLSFWGFLNWGVRIFADIESRMTSIER 966
Cdd:cd18540 224 LSAlFLPIVLFLGSIATALvlwygGILVLA--GAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
76-338 |
1.21e-07 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 54.76 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTIsagvtaetLPTAlIYGVALGLCGFLSGLcmqhYFFNSLKAYQVT-------TNI---LN 145
Cdd:cd18549 12 VLIAALDLVFPLIVRYIIDDL--------LPSK-NLRLILIIGAILLAL----YILRTLLNYFVTywghvmgARIetdMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 146 ERLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDF----PmvfGDLISASFLIIGVVAMLFYyIGWS-ALAALAVLFI 220
Cdd:cd18549 79 RDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELahhgP---EDLFISIITIIGSFIILLT-INVPlTLIVFALLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 221 LAPLTNYVAKKfthldeemMEHRDRRVTLMTQAMNA--------IRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEV 292
Cdd:cd18549 155 MIIFTIYFNKK--------MKKAFRRVREKIGEINAqledslsgIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499478341 293 VSSLGYLAVSTLVLFVALAVHAW--RGEKLDAAVIFTCISLFGLLEGP 338
Cdd:cd18549 227 YFFSGMNFFTNLLNLVVLVAGGYfiIKGEITLGDLVAFLLYVNVFIKP 274
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-603 |
1.24e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 372 TEERTDGAAVgLQMQHFSLRH-DGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG--------EV-------- 434
Cdd:PRK13549 250 REPHTIGEVI-LEVRNLTAWDpVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaypgrwegEIfidgkpvk 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 435 --APREG---SLQFVPEmpGRPRMAYVPQEAYIVNTSL--LENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLRteIG 507
Cdd:PRK13549 329 irNPQQAiaqGIAMVPE--DRKRDGIVPVMGVGKNITLaaLDRFTGGSRIDDAAELKTILESIQRLKVKTASPELA--IA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 508 ekgvNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD--ADTEnllCERLIFG-AWKDVTRIVVTHRL-EHLAQFDQVIY 583
Cdd:PRK13549 405 ----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYE---IYKLINQlVQQGVAIIVISSELpEVLGLSDRVLV 477
|
250 260
....*....|....*....|....
gi 499478341 584 IQHGRVQG----QGTFSELVKTCA 603
Cdd:PRK13549 478 MHEGKLKGdlinHNLTQEQVMEAA 501
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
400-589 |
1.35e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLlMSLL-GEVAPREGSLQF--VPEMPGRPRMA------YVPQEAYIVNT-SLLE 469
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MKILyGLYQPDSGEILIdgKPVRIRSPRDAialgigMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFGEE------VSKEELRRALHNscLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPlSAV 543
Cdd:COG3845 100 NIVLGLEptkggrLDRKAARARIRE--LSERY-----GLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEP-TAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 544 --DADTENLlcerliFGAWKDVTR-----IVVTHRLE---HLAqfDQVIYIQHGRV 589
Cdd:COG3845 172 ltPQEADEL------FEILRRLAAegksiIFITHKLRevmAIA--DRVTVLRRGKV 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
997-1192 |
1.36e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.96 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDgvntasvplEKLRrsLAI 1076
Cdd:PRK09544 5 VSLENVSVSFGQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQ----DPTLFMGTIRNNLDRYNEYSDDeVMGALKHASMWDYVQSlpdGMNSavsegglnLSQGQRQLLCLARALLTKA 1152
Cdd:PRK09544 72 VPQklylDTTLPLTVNRFLRLRPGTKKED-ILPALKRVQAGHLIDA---PMQK--------LSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499478341 1153 RVIVMDEATASVDVQTDALLQKVI---RTSFaGVTMLIIAHRL 1192
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIdqlRREL-DCAVLMVSHDL 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1014-1201 |
1.60e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1014 LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASVPlEKLRRSLAIIPQDPTLFMG-TIRN 1090
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSK-EALENGISMVHQELNLVLQrSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1091 N--LDRYNEYSddevmGALKHASMWDYVQSLPDGMNSAVS--EGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDV 1166
Cdd:PRK10982 93 NmwLGRYPTKG-----MFVDQDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 499478341 1167 QTDALLQKVIRT-SFAGVTMLIIAHRLGTIAD-CDQI 1201
Cdd:PRK10982 168 KEVNHLFTIIRKlKERGCGIVYISHKMEEIFQlCDEI 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
402-591 |
1.64e-07 |
|
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: 55.60 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG---------------EVAPR------EGSLQFVPEmpGRPRMAYVPQEA 460
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvfingkPVDIRnpaqaiRAGIAMVPE--DRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 461 YIVNTSL--LENLQFGEEVSKEELRRALHNSCLSRDLKEWSGGLrtEIGekgvNLSGGQKQRVALARAFLRKPQIVLLDD 538
Cdd:TIGR02633 356 VGKNITLsvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFL--PIG----RLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 539 PLSAVDADTENLLcERLIFG-AWKDVTRIVVTHRL-EHLAQFDQVIYIQHGRVQG 591
Cdd:TIGR02633 430 PTRGVDVGAKYEI-YKLINQlAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
399-550 |
1.72e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--VPEMPGRPRMAY------VPQEAYIV-NTSLLE 469
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggNPCARLTPAKAHqlgiylVPQEPLLFpNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 470 NLQFG---EEVSKEELRRALHNSCLSRDLKEWSGGLrtEIGEkgvnlsggqKQRVALARAFLRKPQIVLLDDPLSAVD-A 545
Cdd:PRK15439 106 NILFGlpkRQASMQKMKQLLAALGCQLDLDSSAGSL--EVAD---------RQIVEILRGLMRDSRILILDEPTASLTpA 174
|
....*
gi 499478341 546 DTENL 550
Cdd:PRK15439 175 ETERL 179
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1002-1223 |
1.85e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1002 LKVRYASHLPQ-VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASvPLEKL-------- 1070
Cdd:PRK10982 251 LEVRNLTSLRQpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkINNHN-ANEAInhgfalvt 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1071 --RRSLAIIPQDPTLFMGTIrNNLDRYNEYsddevMGALKHASMWDYVQSLPDGMN----SAVSEGGlNLSQGQRQLLCL 1144
Cdd:PRK10982 330 eeRRSTGIYAYLDIGFNSLI-SNIRNYKNK-----VGLLDNSRMKSDTQWVIDSMRvktpGHRTQIG-SLSGGNQQKVII 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1145 ARALLTKARVIVMDEATASVDVQTD-ALLQKVIRTSFAGVTMLIIAHR----LGTiadCDQIVEISAGEVKSIRRPTEFS 1219
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEmpelLGI---TDRILVMSNGLVAGIVDTKTTT 479
|
....
gi 499478341 1220 QEEI 1223
Cdd:PRK10982 480 QNEI 483
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
383-588 |
2.06e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSdvLHDVNVHVPAGSSLAIVGPVGAGKSSLlMSLLGEVAPR---EGSLQFvpemPGRPRMAY---- 455
Cdd:PRK13549 6 LEMKNITKTFGGVKA--LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHgtyEGEIIF----EGEELQASnird 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 456 --------VPQEAYIV-NTSLLENLQFGEEVSKEELrraLHNSCLSRDLKEWSGGLRTEI--GEKGVNLSGGQKQRVALA 524
Cdd:PRK13549 79 teragiaiIHQELALVkELSVLENIFLGNEITPGGI---MDYDAMYLRAQKLLAQLKLDInpATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 525 RAFLRKPQIVLLDDPLSAV-DADTENLLceRLIfgawKD-----VTRIVVTHRLEHLAQF-DQVIYIQHGR 588
Cdd:PRK13549 156 KALNKQARLLILDEPTASLtESETAVLL--DII----RDlkahgIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
680-885 |
2.23e-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: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 680 LATLLLGATAATLLPlaqkawlsYYSGHQTEWVALT--------AIGIYGLIGVL-VLVGSLLNHLFWLdRGIRAGKNMH 750
Cdd:cd18572 2 FVFLVVAALSELAIP--------HYTGAVIDAVVADgsreafyrAVLLLLLLSVLsGLFSGLRGGCFSY-AGTRLVRRLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 751 DKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGL---MPLMVFVIAPVMAL- 826
Cdd:cd18572 73 RDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLswrLTLLAFITVPVIALi 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 827 YYVLQRDYRRPAREVKrfDSVARSPRYAHfkESLQGLVVIRSFNKGPWFMQNFYAKLSH 885
Cdd:cd18572 153 TKVYGRYYRKLSKEIQ--DALAEANQVAE--EALSNIRTVRSFATEEREARRYERALDK 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
399-616 |
2.61e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE---------MPGRPRMAYVPQ--EAYIVNTSL 467
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrglLALRQQVATVFQdpEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 LENLQFGEE---VSKEELRRALHNSCLSRDLKewsgGLRTEIGEkgvNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:PRK13638 96 DSDIAFSLRnlgVPEAEITRRVDEALTLVDAQ----HFRHQPIQ---CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 545 --ADTENLLCERLIFGAWKDVtrIVVTHRLEHLAQFDQVIYI-QHGRVQGQGTFSElVKTCapfAEFYKEHGKTQ 616
Cdd:PRK13638 169 paGRTQMIAIIRRIVAQGNHV--IISSHDIDLIYEISDAVYVlRQGQILTHGAPGE-VFAC---TEAMEQAGLTQ 237
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
997-1191 |
2.91e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.14 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRF--IEAEEGSISIDGVNTASVPL-EKLRRS 1073
Cdd:cd03217 1 LEIKDLHVSVGGK--EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1074 LAIIPQDPTLFMGtIRNNldryneysddevmgalkhasmwDYVQSLPDGmnsavsegglnLSQGQRQLLCLARALLTKAR 1153
Cdd:cd03217 79 IFLAFQYPPEIPG-VKNA----------------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 499478341 1154 VIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHR 1191
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHY 163
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
402-570 |
3.02e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.94 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFV-------------------------PEMPGRPRMAyv 456
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLgkdllgmkddewravrsdiqmifqdPLASLNPRMT-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 457 pqeayiVNTSLLENLQ-FGEEVSKEELRRALHNSCLSRDLkewsggLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVL 535
Cdd:PRK15079 117 ------IGEIIAEPLRtYHPKLSRQEVKDRVKAMMLKVGL------LPNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499478341 536 LDDPLSAVD----ADTENLLCE-------RLIFGAwKDVTriVVTH 570
Cdd:PRK15079 185 CDEPVSALDvsiqAQVVNLLQQlqremglSLIFIA-HDLA--VVKH 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
367-539 |
3.20e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 367 EVEISTEERTDGAAVgLQMQHFSLRHDGAVsDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF--- 443
Cdd:COG3845 243 LLRVEKAPAEPGEVV-LEVENLSVRDDRGV-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdge 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 444 -VPEMPGRPR----MAYVPQE----AYIVNTSLLENLQFGEEVSKEELRRALHNSclsRDLKEWS-----------GGLR 503
Cdd:COG3845 321 dITGLSPRERrrlgVAYIPEDrlgrGLVPDMSVAENLILGRYRRPPFSRGGFLDR---KAIRAFAeelieefdvrtPGPD 397
|
170 180 190
....*....|....*....|....*....|....*.
gi 499478341 504 TEIGekgvNLSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:COG3845 398 TPAR----SLSGGNQQKVILARELSRDPKLLIAAQP 429
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
761-888 |
3.31e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 53.26 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 761 PVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMP---LMVFVIAPVMALYYVLQRDYRRP 837
Cdd:cd18546 86 SLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPrlaLVALAALPPLALATRWFRRRSSR 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499478341 838 AREVKRfDSVARSprYAHFKESLQGLVVIRSFNKGPwFMQNFYAKLSHSNR 888
Cdd:cd18546 166 AYRRAR-ERIAAV--NADLQETLAGIRVVQAFRRER-RNAERFAELSDDYR 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1012-1222 |
4.02e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 53.24 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVN----TASVPLEKLRRSLAIIPQDP--TLFm 1085
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRPVRKRIGMVFQFPesQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1086 gtiRNNLDRYNEYSDDEVMGALKHASMWDYVQSLPDGMNSAV-SEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASV 1164
Cdd:PRK13646 100 ---EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 1165 DVQTDALLQKVIRT--SFAGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTE-FSQEE 1222
Cdd:PRK13646 177 DPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKElFKDKK 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
383-588 |
4.34e-07 |
|
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: 54.06 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVSdvLHDVNVHVPAGSSLAIVGPVGAGKSSLlMSLLGEVAPR---EGSLQFVPEM--------PGRP 451
Cdd:TIGR02633 2 LEMKGIVKTFGGVKA--LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHgtwDGEIYWSGSPlkasnirdTERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 452 RMAYVPQEAYIV-NTSLLENLQFGEEVSKEELRR---ALHNSC--LSRDLKEWSGGLRTEIGEKGvnlsGGQKQRVALAR 525
Cdd:TIGR02633 79 GIVIIHQELTLVpELSVAENIFLGNEITLPGGRMaynAMYLRAknLLRELQLDADNVTRPVGDYG----GGQQQLVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 526 AFLRKPQIVLLDDPLSAV-DADTENLLceRLIfgawKDVTR-----IVVTHRLEHLAQF-DQVIYIQHGR 588
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLtEKETEILL--DII----RDLKAhgvacVYISHKLNEVKAVcDTICVIRDGQ 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1017-1190 |
4.59e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1017 ITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIdgvntasvpleklrrslaiipqDPTLFMGTIRNNLDRYN 1096
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL----------------------DPNERLGKLRQDQFAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1097 EYS--DDEVMGalkHASMW------DYVQSLP-----DGMNSAVSEG---------------------GLNLSQ------ 1136
Cdd:PRK15064 78 EFTvlDTVIMG---HTELWevkqerDRIYALPemseeDGMKVADLEVkfaemdgytaearagelllgvGIPEEQhyglms 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1137 ----GQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVI--RTSfagvTMLIIAH 1190
Cdd:PRK15064 155 evapGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLneRNS----TMIIISH 210
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
717-956 |
4.75e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 52.86 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 717 IGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVdvylQWSFDSAV 796
Cdd:cd18577 50 ALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLI----QDGIGEKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 797 HCALQVIVSIV--LILGL-----MPLMVFVIAPVMAL-YYVLQRDYRRPAREVKRFDSVARSprYAHfkESLQGLVVIRS 868
Cdd:cd18577 126 GLLIQSLSTFIagFIIAFiyswkLTLVLLATLPLIAIvGGIMGKLLSKYTKKEQEAYAKAGS--IAE--EALSSIRTVKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 869 FNKGPWFMQNFYAKLSHSNRMFyshvminrwfssriplvgglISMATAVGVSLSAYYGVMdagtaglVTLYSLSFWgfln 948
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAG--------------------IKKGLVSGLGLGLLFFII-------FAMYALAFW---- 250
|
....*...
gi 499478341 949 WGVRIFAD 956
Cdd:cd18577 251 YGSRLVRD 258
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
399-588 |
5.29e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpeMPGRpRMAYVPQEAYIVNT-SLLENLQFG--- 474
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP---APGI-KVGYLPQEPQLDPEkTVRENVEEGvae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 475 --------EEVSKE----------------ELRRAL-----HNscLSRDLKEWSGGLRTEIGEKGV-NLSGGQKQRVALA 524
Cdd:PRK11819 98 vkaaldrfNEIYAAyaepdadfdalaaeqgELQEIIdaadaWD--LDSQLEIAMDALRCPPWDAKVtKLSGGERRRVALC 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 525 RAFLRKPQIVLLDDPLSAVDADTEnllcerlifgAWkdvtrivvthrLE-HLAQFD-QVIYIQHGR 588
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAESV----------AW-----------LEqFLHDYPgTVVAVTHDR 220
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
76-359 |
5.32e-07 |
|
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: 52.83 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTIsagvtaetLPTALIYGVALGLCGFLSGlcmqhYFFNSLKAY--QVTTNILNERL----- 148
Cdd:cd18570 12 LLITLLGIAGSFFFQILIDDI--------IPSGDINLLNIISIGLILL-----YLFQSLLSYirSYLLLKLSQKLdirli 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 149 ---FKHSLKLSQK---SRQknqVGDIVNHMSsDSDN----VSDfpmVFGDLISASFLIIGVVAMLFYYIGWSALAALAVL 218
Cdd:cd18570 79 lgyFKHLLKLPLSffeTRK---TGEIISRFN-DANKireaISS---TTISLFLDLLMVIISGIILFFYNWKLFLITLLII 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 219 FILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSSlgy 298
Cdd:cd18570 152 PLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQS--- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 299 lAVSTLVLFVALAVHAWRGEKLdaaVI---------FTCISLFGLLEGPFGDLSRLISRATNAKVGARRI 359
Cdd:cd18570 229 -SIKGLISLIGSLLILWIGSYL---VIkgqlslgqlIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
714-942 |
5.98e-07 |
|
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: 52.83 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 714 LTAIGIygLIGVLVLVGSLLNHLfwldRG---IRAGKNMHDKML----KSVLSSPVRFFDSTPVGRIIQRFS-----RDV 781
Cdd:cd18570 41 LNIISI--GLILLYLFQSLLSYI----RSyllLKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRFNdankiREA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 782 ESvdvylqwsfDSAVHCALQVIVSIVlILGLM-------PLMVFVIAPVMAL-YYVLQRDYRRPAREVKRFDSVARSpry 853
Cdd:cd18570 115 IS---------STTISLFLDLLMVII-SGIILffynwklFLITLLIIPLYILiILLFNKPFKKKNREVMESNAELNS--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 854 aHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSRIPLVGGLISMAT-AVGVSLsayygVMDAG- 931
Cdd:cd18570 182 -YLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLIlWIGSYL-----VIKGQl 255
|
250
....*....|..
gi 499478341 932 TAG-LVTLYSLS 942
Cdd:cd18570 256 SLGqLIAFNALL 267
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
713-881 |
6.46e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 52.59 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 713 ALTAIGIyGLIGVLVLVG--SLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSrDVESVDVYL-Q 789
Cdd:cd18782 40 TLYVIGV-VMLVAALLEAvlTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLtG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 790 WSFDSAVHCALQVIVSIVLIL--GLMPLMVFVIAPVMALYY-----VLQRDYRRparevkRFDSVARSprYAHFKESLQG 862
Cdd:cd18782 118 TALTTLLDVLFSVIYIAVLFSysPLLTLVVLATVPLQLLLTflfgpILRRQIRR------RAEASAKT--QSYLVESLTG 189
|
170 180
....*....|....*....|..
gi 499478341 863 LVVIRSFNKGP---WFMQNFYA 881
Cdd:cd18782 190 IQTVKAQNAELkarWRWQNRYA 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
400-598 |
6.74e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLmSLL-GEVAPREGSLQ-FVPEMPGR-------PRMAYVPQ----EAYiVNTS 466
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLIaGARKIQQGRVEvLGGDMADArhrravcPRIAYMPQglgkNLY-PTLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENLQF-----GEevSKEElRRA-----LHNSCLSRDLKEWSGglrteigekgvNLSGGQKQRVALARAFLRKPQIVLL 536
Cdd:NF033858 95 VFENLDFfgrlfGQ--DAAE-RRRridelLRATGLAPFADRPAG-----------KLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 537 D------DPLSavdadtenllceRLIFgaWKDVTRI----------VVTHRLEHLAQFDQVIYIQHGRVQGQGTFSEL 598
Cdd:NF033858 161 DepttgvDPLS------------RRQF--WELIDRIraerpgmsvlVATAYMEEAERFDWLVAMDAGRVLATGTPAEL 224
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
747-947 |
7.02e-07 |
|
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: 52.42 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 747 KNMHDKMLKsvLSspVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMPLMVFVIAPVMAL 826
Cdd:cd18554 83 KDLFDHLQK--LS--LRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 827 YYVLQRDYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVminRWFSSRIPL 906
Cdd:cd18554 159 YILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHT---RWNAKTFSA 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499478341 907 VGGLISMATAVGVSLSAYYGVmdagtAGLVTLYSL-SFWGFL 947
Cdd:cd18554 236 VNTITDLAPLLVIGFAAYLVI-----EGNLTVGTLvAFVGYM 272
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1012-1190 |
7.79e-07 |
|
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: 53.40 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRfIEAeegsisidGVNTASVPLEKLRRSLAI--IPQDPTL------ 1083
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKST----LLR-IMA--------GVDKDFNGEARPQPGIKVgyLPQEPQLdptktv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1084 ------FMGTIRNNLDRYNE----YSD-DEVMGAL-----------KHASMWDYVQSL---------PDGmNSAVSeggl 1132
Cdd:TIGR03719 86 renveeGVAEIKDALDRFNEisakYAEpDADFDKLaaeqaelqeiiDAADAWDLDSQLeiamdalrcPPW-DADVT---- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1133 NLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRtSFAGvTMLIIAH 1190
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ-EYPG-TVVAVTH 216
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
982-1159 |
7.88e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.26 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 982 PLPEPLRPTWPEFGEISVEGLKVRYASHLPQ---VLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISID 1058
Cdd:COG4615 313 AADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1059 GVNTASVPLEKLRRSLAIIPQDPTLFmgtiRNNLDRYNEYSDDEVMgalkhasmwDYVQSLpdGMNSAVS-EGG----LN 1133
Cdd:COG4615 393 GQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARAR---------ELLERL--ELDHKVSvEDGrfstTD 457
|
170 180
....*....|....*....|....*.
gi 499478341 1134 LSQGQRQLLCLARALLTKARVIVMDE 1159
Cdd:COG4615 458 LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
997-1209 |
8.98e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.15 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYAS--HLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE----EGSISIDGVNTASVPLEKL 1070
Cdd:COG4172 7 LSVEDLSVAFGQggGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1071 RR----SLAIIPQDPT-----LFmgTIRNNLdryneysdDEVMgaLKHASM------------WDYVQsLPDgmnsavSE 1129
Cdd:COG4172 87 RRirgnRIAMIFQEPMtslnpLH--TIGKQI--------AEVL--RLHRGLsgaaararalelLERVG-IPD------PE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1130 GGLN-----LSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDA----LLQKVIRTSfaGVTMLIIAHRLGTIAD-CD 1199
Cdd:COG4172 148 RRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAqildLLKDLQREL--GMALLLITHDLGVVRRfAD 225
|
250
....*....|
gi 499478341 1200 QIVEISAGEV 1209
Cdd:COG4172 226 RVAVMRQGEI 235
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
73-227 |
8.99e-07 |
|
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: 52.12 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 73 IWYLASSVLALLSPVFVNRFIGTISAGVTAETLPTALIYGVALGLCGFLSGLCMQHYFFN-SLKAyqvtTNILNERLFKH 151
Cdd:cd18580 6 LLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLaGLRA----SRRLHDKLLRS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 152 SLKLSQKSRQKNQVGDIVNHMSSDSDNV-SDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNY 227
Cdd:cd18580 82 VLRAPMSFFDTTPSGRILNRFSKDIGLIdEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRY 158
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
400-591 |
9.98e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.03 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMPGRPRMAYVP----------QEAYIV-NTSLL 468
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrrqigmifQDHHLLmDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 469 ENLQFG---EEVSKEELRRALhNSCLSRDlkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVD- 544
Cdd:PRK10908 98 DNVAIPliiAGASGDDIRRRV-SAALDKV------GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDd 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 545 ADTENLLceRLiFGAWK--DVTRIVVTHRLEHLAQFD-QVIYIQHGRVQG 591
Cdd:PRK10908 171 ALSEGIL--RL-FEEFNrvGVTVLMATHDIGLISRRSyRMLTLSDGHLHG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
413-570 |
1.01e-06 |
|
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: 51.25 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 413 LAIVGPVGAGKSSLLMSLLGEVAPREGSlqfvPEMPgRPRMAYVPQEAYIVNTSLLENLQFgeEVSKEELRRALHNSCLS 492
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGD----IEIE-LDTVSYKPQYIKADYEGTVRDLLS--SITKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 493 RDLKewsgglRTEIGEKGVN-LSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADtENLLCERLI--FGAWKDVTRIVVT 569
Cdd:cd03237 101 KPLQ------IEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIrrFAENNEKTAFVVE 173
|
.
gi 499478341 570 H 570
Cdd:cd03237 174 H 174
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1017-1190 |
1.14e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.15 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1017 ITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASV-----PLEKLRRSLAIIPQ---DPTLFMGTI 1088
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyqrPINMMFQSYALFPHmtvEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1089 RNNLDRYNEYSDDEVMGALKHasMWDYVQSLPDgmnsavsegglNLSQGQRQLLCLARALLTKARVIVMDEATASVD--- 1165
Cdd:PRK11607 118 QDKLPKAEIASRVNEMLGLVH--MQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkl 184
|
170 180 190
....*....|....*....|....*....|
gi 499478341 1166 ---VQTDA--LLQKVirtsfaGVTMLIIAH 1190
Cdd:PRK11607 185 rdrMQLEVvdILERV------GVTCVMVTH 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1000-1192 |
1.19e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1000 EGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKLRRSLAIIPQ 1079
Cdd:PRK10253 11 EQLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1080 DPTLFMGTIRNNL------------DRYNEYSDDEVMGALKHAsmwdyvqslpdGMNSAVSEGGLNLSQGQRQLLCLARA 1147
Cdd:PRK10253 89 NATTPGDITVQELvargryphqplfTRWRKEDEEAVTKAMQAT-----------GITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499478341 1148 LLTKARVIVMDEATASVDV--QTD--ALLQKVIRTSfaGVTMLIIAHRL 1192
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDIshQIDllELLSELNREK--GYTLAAVLHDL 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
995-1223 |
1.25e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLP---QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISidgVNTASVP----- 1066
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI---VGDYAIPanlkk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1067 ---LEKLRRSLAIIPQDP--TLFMGTIRN-------NLDRYNEYSDDEVMGALKHASM-WDYVQSLPdgmnsavseggLN 1133
Cdd:PRK13645 82 ikeVKRLRKEIGLVFQFPeyQLFQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLpEDYVKRSP-----------FE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1134 LSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDA----LLQKVIRTSfaGVTMLIIAHRLGTIAD-CDQIVEISAGE 1208
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEY--KKRIIMVTHNMDQVLRiADEVIVMHEGK 228
|
250
....*....|....*.
gi 499478341 1209 VKSIRRPTE-FSQEEI 1223
Cdd:PRK13645 229 VISIGSPFEiFSNQEL 244
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
997-1190 |
1.80e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLpqVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRFIEAEE----GSISI-DGVNTASVplEKLR 1071
Cdd:PRK11819 325 IEAENLSKSFGDRL--LIDDLSFSLPPGGIVGIIGPNGAGKST----LFKMITGQEqpdsGTIKIgETVKLAYV--DQSR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLaiipqDP--TLFmgtirnnldryneysdDEVMGALKHASMWDYVqslpdgMNSAVSEGGLN------------LSQG 1137
Cdd:PRK11819 397 DAL-----DPnkTVW----------------EEISGGLDIIKVGNRE------IPSRAYVGRFNfkggdqqkkvgvLSGG 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499478341 1138 QRQLLCLARALLTKARVIVMDEATASVDVQT-----DALLQkvirtsFAGVTMlIIAH 1190
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETlraleEALLE------FPGCAV-VISH 500
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1016-1173 |
1.81e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1016 GITFKVEAGSRVGIIGRTGSGKStffqSLFR----FIEAEEGSISIDGVntasvPLEKLRRSLAiipQDpTLFMG----- 1086
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKT----SLLRilagLARPDAGEVLWQGE-----PIRRQRDEYH---QD-LLYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 ----TIRNNLDRY----NEYSDDEVMGALKHASMWDYvQSLPDGmnsavsegglNLSQGQRQLLCLARALLTKARVIVMD 1158
Cdd:PRK13538 86 ktelTALENLRFYqrlhGPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWILD 154
|
170
....*....|....*
gi 499478341 1159 EATASVDVQTDALLQ 1173
Cdd:PRK13538 155 EPFTAIDKQGVARLE 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
997-1192 |
2.60e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.63 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKV--RYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE-----EGSISIDGVNTASVPLEK 1069
Cdd:PRK15134 6 LAIENLSVafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 LRR----SLAIIPQDPTLFMGTIRN---------NLDR--YNEYSDDEVMGALKHASMWDYVQSLPDGMNsavsegglNL 1134
Cdd:PRK15134 86 LRGvrgnKIAMIFQEPMVSLNPLHTlekqlyevlSLHRgmRREAARGEILNCLDRVGIRQAAKRLTDYPH--------QL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1135 SQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIR--TSFAGVTMLIIAHRL 1192
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNL 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
389-598 |
2.89e-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: 51.61 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 389 SLRHDGAVSDVLHDVNVHVPAGSSLAIVGPVGAGKS--SL-LMSLLGE-VAPREGSLQF-------VPE-----MPGRpR 452
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtALsILRLLPDpAAHPSGSILFdgqdllgLSErelrrIRGN-R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 453 MAYVPQEAYivnTSL----------LENLQFGEEVSKEELR-RALHnsCLSRDlkewsgGLRTEigEKGVN-----LSGG 516
Cdd:COG4172 94 IAMIFQEPM---TSLnplhtigkqiAEVLRLHRGLSGAAARaRALE--LLERV------GIPDP--ERRLDayphqLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 517 QKQRVALARAFLRKPQIVLLDDPLSAVD----ADTENLLcerlifgawKDVTR------IVVTHRL---EHLAqfDQVIY 583
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLL---------KDLQRelgmalLLITHDLgvvRRFA--DRVAV 229
|
250
....*....|....*
gi 499478341 584 IQHGRVQGQGTFSEL 598
Cdd:COG4172 230 MRQGEIVEQGPTAEL 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1017-1191 |
3.30e-06 |
|
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: 51.29 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1017 ITFKVEAGSRVGIIGRTGSGKStffqSLFRFIeaeeGSISIDGVNTASVPLEKlrrSLAIIPQDPTLFMGTIRNNL---D 1093
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKS----SLFRIL----GELWPVYGGRLTKPAKG---KLFYVPQRPYMTLGTLRDQIiypD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1094 RYNE-----YSDDEVMGALKHASMWDYVQSlpDGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQT 1168
Cdd:TIGR00954 540 SSEDmkrrgLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|...
gi 499478341 1169 DALLQKVIRTsfAGVTMLIIAHR 1191
Cdd:TIGR00954 618 EGYMYRLCRE--FGITLFSVSHR 638
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1002-1209 |
3.61e-06 |
|
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: 49.18 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1002 LKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAE---EGSISIDGVnTASVPLEKLRRSLAIIP 1078
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGI-PYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1079 QD----PTLfmgTIRNNLD-----RYNEYsddeVMGalkhasmwdyvqslpdgmnsavsegglnLSQGQRQLLCLARALL 1149
Cdd:cd03233 90 EEdvhfPTL---TVRETLDfalrcKGNEF----VRG----------------------------ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 1150 TKARVIVMDEATASVDVQTDALLQKVIRT---SFAGVTMLIIAHRLGTIADC-DQIVEISAGEV 1209
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTmadVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQ 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
997-1190 |
4.06e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.70 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEKlrrslAI 1076
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1077 IPQDPTLFmgTIRNNLDryNEYSDDEVMGALKHASMWDYVQSLPD-GMNSAVSEGGLNLSQGQRQLLCLARALLTKARVI 1155
Cdd:PRK11248 75 VFQNEGLL--PWRNVQD--NVAFGLQLAGVEKMQRLEIAHQMLKKvGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 499478341 1156 VMDEATASVDV----QTDALLQKVIRTSfaGVTMLIIAH 1190
Cdd:PRK11248 151 LLDEPFGALDAftreQMQTLLLKLWQET--GKQVLLITH 187
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
986-1226 |
4.73e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 986 PLRPTWPEFGEISVEGLKVRYASHLPQVlKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASV 1065
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1066 PLEKLRRSLAIIPQDPTLFMGTirnnLDRYNEYSDDEVMGA-LKHASMWDYVQsLPDGMNSavsegGLNLSQGQRQLLCL 1144
Cdd:PRK10522 391 QPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLE-LEDGRIS-----NLKLSKGQKKRLAL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1145 ARALLTKARVIVMDEATASVDVQTDALLQKVI--RTSFAGVTMLIIAHRLGTIADCDQIVEISAGEVksirrpTEFSQEE 1222
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHFRREFYQVLlpLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL------SELTGEE 534
|
....
gi 499478341 1223 IEES 1226
Cdd:PRK10522 535 RDAA 538
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
144-350 |
4.84e-06 |
|
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: 49.73 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 144 LNERLFKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSDFPMV-FGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILA 222
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTgLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 223 PLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAEVVSslgYLAVS 302
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKT---FSAVN 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 303 TLVLFVALAVHAWRGEK--LDAAVIFTCISLFGLLEGPFGDLSRLISRAT 350
Cdd:cd18554 238 TITDLAPLLVIGFAAYLviEGNLTVGTLVAFVGYMERMYSPLRRLVNSFT 287
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
76-263 |
4.87e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 49.70 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIgtiSAGVTAETLPTALIYG---VALGLCGFLSGLCMQhyFFNSLKAYQVTTNiLNERLFKHS 152
Cdd:cd18548 9 LLEVLLELLLPTLMADII---DEGIANGDLSYILRTGllmLLLALLGLIAGILAG--YFAAKASQGFGRD-LRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 153 LKLSQKSRQKNQVGDIVNHMSSDSDNVSDF-PMVFGDLISASFLIIGVVAMLFY---YIGWSALAALAVLFI-LAPLTNY 227
Cdd:cd18548 83 QSFSFAEIDKFGTSSLITRLTNDVTQVQNFvMMLLRMLVRAPIMLIGAIIMAFRinpKLALILLVAIPILALvVFLIMKK 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 499478341 228 VAKKFTHLDEEMmehrDRRVTLMTQAMNAIRVVKYF 263
Cdd:cd18548 163 AIPLFKKVQKKL----DRLNRVVRENLTGIRVIRAF 194
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
678-824 |
5.15e-06 |
|
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: 49.74 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 678 LILATLL-LGATAATLL-PLAQKAWLSYYSGHQTEWVALtaigiyGLIGVLVLVGSLLNHL--FWLDR-GIRAGKNMHDK 752
Cdd:cd18551 1 LILALLLsLLGTAASLAqPLLVKNLIDALSAGGSSGGLL------ALLVALFLLQAVLSALssYLLGRtGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 753 MLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVL-----------ILGLMPLMVFVIA 821
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLmflldwvltlvTLAVVPLAFLIIL 154
|
...
gi 499478341 822 PVM 824
Cdd:cd18551 155 PLG 157
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
383-609 |
5.48e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 383 LQMQHFSLRHDGAVsdVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGE----VAPREGSLQFVPEMPGRPRMAYVPQ 458
Cdd:PRK13547 2 LTADHLHVARRHRA--ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltggGAPRGARVTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 459 EAYIVNTSLLENLQFGEEVSKEEL---------RRALHNSCLSRDLKEWS---GGLRTEIGEKGVNLSGGQKQRVALARA 526
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFAFSAREIvllgryphaRRAGALTHRDGEIAWQAlalAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 527 F---------LRKPQIVLLDDPLSAVDADTENLLCERLifgawKDVTR------IVVTHRLEHLAQF-DQVIYIQHGRVQ 590
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTV-----RRLARdwnlgvLAIVHDPNLAARHaDRIAMLADGAIV 234
|
250
....*....|....*....
gi 499478341 591 GQGTFSElVKTCAPFAEFY 609
Cdd:PRK13547 235 AHGAPAD-VLTPAHIARCY 252
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1014-1166 |
7.46e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1014 LKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDG--VNTASvPLEKLRRSLAIIPQDP-----TLFMG 1086
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRS-PQDGLANGIVYISEDRkrdglVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 TIRN-NLDRYNEYSDDevMGALKHAsmwDYVQSLPD----------GMNSAVSegglNLSQGQRQLLCLARALLTKARVI 1155
Cdd:PRK10762 347 VKENmSLTALRYFSRA--GGSLKHA---DEQQAVSDfirlfniktpSMEQAIG----LLSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|.
gi 499478341 1156 VMDEATASVDV 1166
Cdd:PRK10762 418 ILDEPTRGVDV 428
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1030-1209 |
8.69e-06 |
|
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: 50.40 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1030 IGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASvPLEKLRRSLAIIPQDPTLFMG-TIRNNLDRYNEysddevmgaLK 1108
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQ---------LK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1109 HASmWDYVQ-----SLPD-GMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTSFAG 1182
Cdd:TIGR01257 1032 GRS-WEEAQlemeaMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180
....*....|....*....|....*....
gi 499478341 1183 VTMLIIAHRLGTiADC--DQIVEISAGEV 1209
Cdd:TIGR01257 1111 RTIIMSTHHMDE-ADLlgDRIAIISQGRL 1138
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
400-598 |
1.04e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSL--------QFVPEMPGRPRMAYVPQEAYIVNT-SLLEN 470
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynKLDHKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 471 LQFGeevskeelrRALHNSCLSRDLKEWSG------------GLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDD 538
Cdd:PRK09700 101 LYIG---------RHLTKKVCGVNIIDWREmrvraammllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 539 PLSAV-DADTENLLCerLIFGAWKDVTRIV-VTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK09700 172 PTSSLtNKEVDYLFL--IMNQLRKEGTAIVyISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1000-1177 |
1.16e-05 |
|
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: 48.04 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1000 EGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIE---AEEGSISIDGvntasVPLEK--LRRSL 1074
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNG-----QPRKPdqFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 AIIPQD----PTL-------FMGTIRN---NLDRYNEYSD-DEVMGALKHASMWDYVQSlpdgmnsavsegglNLSQGQR 1139
Cdd:cd03234 84 AYVRQDdillPGLtvretltYTAILRLprkSSDAIRKKRVeDVLLRDLALTRIGGNLVK--------------GISGGER 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 499478341 1140 QLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIR 1177
Cdd:cd03234 150 RRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLS 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
402-547 |
1.27e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMpgrpRMAYVPQEayivNTSLLENLQFGEEVskee 481
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV----KLAYVDQS----RDALDPNKTVWEEI---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 482 lrralhnsclsrdlkewSGGLRT-EIGEKGVN---------------------LSGGQKQRVALARAFLRKPQIVLLDDP 539
Cdd:TIGR03719 408 -----------------SGGLDIiKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
....*...
gi 499478341 540 LSAVDADT 547
Cdd:TIGR03719 471 TNDLDVET 478
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
87-329 |
1.33e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 48.62 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 87 VFVNRFIGTIS-AGVTAETLPTALIYgVALGLCGFLSGLcMQHYFFNSLKAYQVTTniLNERLFKHSLKLSQKSRQKNQV 165
Cdd:cd18577 28 AFTDFGSGESSpDEFLDDVNKYALYF-VYLGIGSFVLSY-IQTACWTITGERQARR--IRKRYLKALLRQDIAWFDKNGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 166 GDIVNHMSSDSDNVSD-FPMVFGDLISASFLIIG--VVAmlFYYiGWS-ALAALAVLFILAPLTNYVAKKFTHLDEEMME 241
Cdd:cd18577 104 GELTSRLTSDTNLIQDgIGEKLGLLIQSLSTFIAgfIIA--FIY-SWKlTLVLLATLPLIAIVGGIMGKLLSKYTKKEQE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 242 HRDRRVTLMTQAMNAIRVVKYFAWEKsvaKEVTEVREKELTSRRRLAKAEVVSSLGyLAVSTLVLFVALAVHAWRGEKL- 320
Cdd:cd18577 181 AYAKAGSIAEEALSSIRTVKAFGGEE---KEIKRYSKALEKARKAGIKKGLVSGLG-LGLLFFIIFAMYALAFWYGSRLv 256
|
250
....*....|....
gi 499478341 321 -----DAAVIFTCI 329
Cdd:cd18577 257 rdgeiSPGDVLTVF 270
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
144-312 |
1.62e-05 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 48.37 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 144 LNERLFKHSLKLSQKSRQKNQVGDIVNhmssDSDNVSDF-----PMVFGDLISAsFLIIGVVAMLFYYIGWSALAALAVL 218
Cdd:cd18586 77 LGRRVFRAVLELPLESRPSGYWQQLLR----DLDTLRNFltgpsLFAFFDLPWA-PLFLAVIFLIHPPLGWVALVGAPVL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 219 FILAPLTNYVAKKFthLDEEMMEHRDRRVTLMTQAMNAiRVVKYFAWEKSVAKEVTEVREKEL-TSRRRLAKAEVVSSLG 297
Cdd:cd18586 152 VGLAWLNHRATRKP--LGEANEAQAARDALAAETLRNA-ETIKALGMLGNLRRRWEARHAETLeLQIRASDLAGAISAIG 228
|
170
....*....|....*....
gi 499478341 298 ---YLAVSTLVLFV-ALAV 312
Cdd:cd18586 229 ktlRMALQSLILGVgAYLV 247
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
80-289 |
1.62e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 48.28 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 80 VLALLSPVFVNRFIGTISAGVTAETLPTALIYGVALGLCgflsglcmqHYFFNSLKAYQVT---TNI---LNERLFKHSL 153
Cdd:cd18555 16 LLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLL---------YGLFSFLRGYIIIklqTKLdksLMSDFFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 154 KLSQKSRQKNQVGDIVNHMSSdsdNVSDFPMVFGDLISA---SFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNYVAK 230
Cdd:cd18555 87 KLPYSFFENRSSGDLLFRANS---NVYIRQILSNQVISLiidLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499478341 231 KFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAK 289
Cdd:cd18555 164 KIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKER 222
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
71-308 |
1.87e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 47.86 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 71 AYIWYLASSVLALLSPVFVNRFIGTISAGVTAETLPTALIY--GVALGLcGFLSGLcmQHYFFNSLkAYQVTTNIlNERL 148
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLllAVALVL-ALASAL--RFYLVSWL-GERVVADL-RKAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 149 FKHSLKLSQKSRQKNQVGDIVNHMSSDSDNVSdfpMVFGDLIS----ASFLIIGVVAMLFYY-IGWSALAALAVLFILAP 223
Cdd:cd18575 76 FAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQ---TVVGSSLSialrNLLLLIGGLVMLFITsPKLTLLVLLVIPLVVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 224 LTnYVAKKFTHLDeemMEHRDRRVTLMTQA---MNAIRVVKYFAWEKSVAKEVTEVREKELTSRRRLAKAE-----VVSS 295
Cdd:cd18575 153 II-LFGRRVRRLS---RASQDRLADLSAFAeetLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARalltaLVIF 228
|
250
....*....|...
gi 499478341 296 LGYLAVsTLVLFV 308
Cdd:cd18575 229 LVFGAI-VFVLWL 240
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1019-1211 |
2.01e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1019 FKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGvntaSVPLEKLRrslaiipQDP------TLF------MG 1086
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ----DLIVARLQ-------QDPprnvegTVYdfvaegIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1087 TIRNNLDRYNEYSDD--------------EVMGALKHASMWdyvqSLPDGMNSAVSEGGLN-------LSQGQRQLLCLA 1145
Cdd:PRK11147 93 EQAEYLKRYHDISHLvetdpseknlnelaKLQEQLDHHNLW----QLENRINEVLAQLGLDpdaalssLSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 1146 RALLTKARVIVMDEATASVDVQTDALLQKVIRtSFAGvTMLIIAHRLGTIAD-CDQIVEISAGEVKS 1211
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLK-TFQG-SIIFISHDRSFIRNmATRIVDLDRGKLVS 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
407-596 |
2.06e-05 |
|
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: 47.75 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 407 VPA-GSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE--------------------MPGRPRMAYVPQeaYI--- 462
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdeildefrgselqnyftklLEGDVKVIVKPQ--YVdli 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 ---VNTSLLENLQFGEEVSK-EELRRALH-NSCLSRDLKEwsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:cd03236 100 pkaVKGKVGELLKKKDERGKlDELVDQLElRHVLDRNIDQ---------------LSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 538 DPLSAVDAdTENLLCERLIFGAWKDVTR-IVVTHRLEHLAQFDQVIYIQHGRVQGQGTFS 596
Cdd:cd03236 165 EPSSYLDI-KQRLNAARLIRELAEDDNYvLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVT 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
997-1209 |
2.06e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVryASHLPQVlKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRF----IEAEEGSISIDGVntaSVPLEKLR- 1071
Cdd:PRK10418 5 IELRNIAL--QAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGK---PVAPCALRg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1072 RSLAIIPQDPTLFMGTIRNNLDRYNE-------YSDDEVMGALKHASMWDYVQSLPDGMNSAVSEGGLnlsqgQRQLLCL 1144
Cdd:PRK10418 79 RKIATIMQNPRSAFNPLHTMHTHAREtclalgkPADDATLTAALEAVGLENAARVLKLYPFEMSGGML-----QRMMIAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1145 arALLTKARVIVMDEATASVDVQTDA----LLQKVIRTSfaGVTMLIIAHRLGTIADC-DQIVEISAGEV 1209
Cdd:PRK10418 154 --ALLCEAPFIIADEPTTDLDVVAQArildLLESIVQKR--ALGMLLVTHDMGVVARLaDDVAVMSHGRI 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
995-1190 |
2.31e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 995 GEISVEGLKVRYASHLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIdGVNTASVPLEKLRRSL 1074
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1075 aiipqDPTlfmGTIRNNLDRyneySDDEVM--GALKHAsmWDYVQSL---PDGMNSAVSEgglnLSQGQRQLLCLARALL 1149
Cdd:PRK11147 395 -----DPE---KTVMDNLAE----GKQEVMvnGRPRHV--LGYLQDFlfhPKRAMTPVKA----LSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499478341 1150 TKARVIVMDEATASVDVQTDALLQKVIrTSFAGvTMLIIAH 1190
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSH 495
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
682-871 |
2.41e-05 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 47.51 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 682 TLLLGATAATL-LPLAQKAWLSYYSGH--QTEWVALTAIGIYGLIGVLVLVGSLLNHL-FWLDR--GIRAGKNMHDKMLK 755
Cdd:cd18573 3 ALLLVSSAVTMsVPFAIGKLIDVASKEsgDIEIFGLSLKTFALALLGVFVVGAAANFGrVYLLRiaGERIVARLRKRLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 756 SVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMP----LMVFVIAPVMALYYVLQ 831
Cdd:cd18573 83 SILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkltlVMLLVVPPIAVGAVFYG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499478341 832 RDYRRPAREVKrfDSVARSPRYAhfKESLQGLVVIRSFNK 871
Cdd:cd18573 163 RYVRKLSKQVQ--DALADATKVA--EERLSNIRTVRAFAA 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1009-1210 |
3.10e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.70 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1009 HLPQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLE---KLR--------RSLAII 1077
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRakhvgfvfQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1078 P--------QDPTLFMGTIRNNldryneySDDEVMGALKHASMWDYVQSLPdgmnsavseggLNLSQGQRQLLCLARALL 1149
Cdd:PRK10584 101 PtlnalenvELPALLRGESSRQ-------SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499478341 1150 TKARVIVMDEATASVDVQTDallQKVIRTSFA-----GVTMLIIAHRLGTIADCDQIVEISAGEVK 1210
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTG---DKIADLLFSlnrehGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
507-629 |
3.43e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 507 GEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRLEHLAQF-DQVIYIQ 585
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLaHELTVID 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 499478341 586 HGRVQGQGTFSELvKTcapfaefykehgKTQGEGHEVRPAETAQ 629
Cdd:NF000106 219 RGRVIADGKVDEL-KT------------KVGGRTLQIRPAHAAE 249
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
399-600 |
4.06e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 46.70 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQfvpeMPGRP-----------RMAYVPQEayivntsl 467
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIL----LDAQPleswsskafarKVAYLPQQ-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 468 lenLQFGEEVSKEEL----RRALHNScLSRDLKEWSGGLRTEIGEKGV---------NLSGGQKQRVALARAFLRKPQIV 534
Cdd:PRK10575 94 ---LPAAEGMTVRELvaigRYPWHGA-LGRFGAADREKVEEAISLVGLkplahrlvdSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 535 LLDDPLSAVDA--DTENL-LCERLifGAWKDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGTFSELVK 600
Cdd:PRK10575 170 LLDEPTSALDIahQVDVLaLVHRL--SQERGLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
395-597 |
4.12e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 395 AVSDVLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGeVAPREGSLQF----VPEMPGRP---RMAYVPQE---AYIVN 464
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFagqpLEAWSAAElarHRAYLSQQqtpPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 465 TSLLENLQFGEEVSKEELRRALHNSCLSRDLKEwsgGLRTEIGekgvNLSGGQKQRVALARAFLR-----KP--QIVLLD 537
Cdd:PRK03695 86 VFQYLTLHQPDKTRTEAVASALNEVAEALGLDD---KLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 538 DPLSAVDADTENLLcERLI--FGAwKDVTRIVVTHRLEH-LAQFDQVIYIQHGRVQGQGTFSE 597
Cdd:PRK03695 159 EPMNSLDVAQQAAL-DRLLseLCQ-QGIAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDE 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1024-1197 |
4.37e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1024 GSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSIsidgvntasvpleklrrslaiipqdptlfmgtIRNNLDRYNEYSDDEV 1103
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------IYIDGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1104 MGALKHasmwdyvqslpdgmnsavsEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRT----- 1178
Cdd:smart00382 50 LLIIVG-------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllll 110
|
170 180
....*....|....*....|.
gi 499478341 1179 --SFAGVTMLIIAHRLGTIAD 1197
Cdd:smart00382 111 lkSEKNLTVILTTNDEKDLGP 131
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
76-273 |
4.51e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 46.72 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVL---ALLSPVFVNRFIGTIsagVTAETLPTALIYGVALGLCGFLSGLcmqhyfFNSLKAYQV--TTN----ILNE 146
Cdd:cd18588 9 LASLFLqlfALVTPLFFQVIIDKV---LVHRSLSTLDVLAIGLLVVALFEAV------LSGLRTYLFshTTNridaELGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 147 RLFKHSLKLSQKSRQKNQVGDIVNHMsSDSDNVSDFP-----MVFGDLIsasFLIIGVVAMLFY--YIGWSALAALAVLF 219
Cdd:cd18588 80 RLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLtgsalTLVLDLV---FSVVFLAVMFYYspTLTLIVLASLPLYA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499478341 220 ILAPLtnyVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVKYFA--------WEKSVAKEV 273
Cdd:cd18588 156 LLSLL---VTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAvepqfqrrWEELLARYV 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
400-593 |
4.67e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAP---------REGSLQFVPEMP-------GRPRMAYVPQEAyiv 463
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPdagevhyrmRDGQLRDLYALSeaerrrlLRTEWGFVHQHP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 ntslLENLQFGeeVSK-----EELRR--ALHNSCLSRDLKEWSGglRTEIGEKGVN-----LSGGQKQRVALARAFLRKP 531
Cdd:PRK11701 99 ----RDGLRMQ--VSAggnigERLMAvgARHYGDIRATAGDWLE--RVEIDAARIDdlpttFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 532 QIVLLDDPLSAVDADTEnllcERLIfgawkDVTR----------IVVTH-----RLehLAqfDQVIYIQHGRVQGQG 593
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQ----ARLL-----DLLRglvrelglavVIVTHdlavaRL--LA--HRLLVMKQGRVVESG 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
399-588 |
4.77e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.57 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPR--EGSLQFVPEMPGRP---RMAYVPQEAYIV-NTSLLENLQ 472
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQilkRTGFVTQDDILYpHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 473 FgeeVSKEELRRALhnsclSRDLKEWSG-------GL----RTEIGEKGVN-LSGGQKQRVALARAFLRKPQIVLLDDPL 540
Cdd:PLN03211 163 F---CSLLRLPKSL-----TKQEKILVAesviselGLtkceNTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499478341 541 SAVDADTENLLCERLIFGAWKDVTRIVVTHRLEH--LAQFDQVIYIQHGR 588
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
679-832 |
5.02e-05 |
|
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: 46.71 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 679 ILATLLLGATAATLL-PLAQKAWLSYYSGHQTEWVAlTAIGIYGLIGVLVLVGSLLNHLFWLdRGIRAGKNM-------- 749
Cdd:cd18579 1 LAGLLKLLEDLLSLAqPLLLGLLISYLSSYPDEPLS-EGYLLALALFLVSLLQSLLLHQYFF-LSFRLGMRVrsalssli 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 750 HDKMLKsvLSSPVRffDSTPVGRIIQRFSRDVESVDVYLQWSFDsAVHCALQVIVSIVLI-----------LGLMPLMVF 818
Cdd:cd18579 79 YRKALR--LSSSAR--QETSTGEIVNLMSVDVQRIEDFFLFLHY-LWSAPLQIIVALYLLyrllgwaalagLGVLLLLIP 153
|
170
....*....|....
gi 499478341 819 VIAPVMALYYVLQR 832
Cdd:cd18579 154 LQAFLAKLISKLRK 167
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
400-544 |
5.61e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLqfvpEMPGRPRMAYVPQE------AYIVNTSLLENLQF 473
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYV----TLDGHEVVTRSPQDglangiVYISEDRKRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 474 GEEVsKEELrralhNSCLSRDLKEWSGGLRTEIGEKGV-------------------NLSGGQKQRVALARAFLRKPQIV 534
Cdd:PRK10762 344 GMSV-KENM-----SLTALRYFSRAGGSLKHADEQQAVsdfirlfniktpsmeqaigLLSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|
gi 499478341 535 LLDDPLSAVD 544
Cdd:PRK10762 418 ILDEPTRGVD 427
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
718-964 |
6.13e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 46.68 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 718 GIYGLIGVLVLVGSLLNHLF-------WLDRgIRAgknmhdKMLKSVLSSPVRFFD----STpvGRIIQRFSRDVESVdv 786
Cdd:cd18578 56 LMFLVLAIVAGIAYFLQGYLfgiagerLTRR-LRK------LAFRAILRQDIAWFDdpenST--GALTSRLSTDASDV-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 787 ylQWSFDSAVHCALQVIVSIV--LILGL-----MPLMVFVIAPVMALYYVLQrdyrrpAREVKRFD-----SVARSPRYA 854
Cdd:cd18578 125 --RGLVGDRLGLILQAIVTLVagLIIAFvygwkLALVGLATVPLLLLAGYLR------MRLLSGFEeknkkAYEESSKIA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 855 HfkESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFyshvminrwfssripLVGGLISMAtAVGVSLSAYYGVmdagtag 934
Cdd:cd18578 197 S--EAVSNIRTVASLTLEDYFLEKYEEALEEPLKKG---------------LRRALISGL-GFGLSQSLTFFA------- 251
|
250 260 270
....*....|....*....|....*....|
gi 499478341 935 lvtlYSLSFWgflnWGVRIFADIESRMTSI 964
Cdd:cd18578 252 ----YALAFW----YGGRLVANGEYTFEQF 273
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1017-1192 |
7.09e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1017 ITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAeEGSISIDGVNTASVPLEKLRRSLA-IIPQDPTLFMgtirnnldry 1095
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFA---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1096 neysddevMgalkhaSMWDYVQ-SLPDGMNSAVSEGGLN------------------LSQGQRQLLCLARALLT------ 1150
Cdd:PRK03695 84 --------M------PVFQYLTlHQPDKTRTEAVASALNevaealglddklgrsvnqLSGGEWQRVRLAAVVLQvwpdin 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499478341 1151 -KARVIVMDEATASVDVQTDALLQKVIRT-SFAGVTMLIIAHRL 1192
Cdd:PRK03695 150 pAGQLLLLDEPMNSLDVAQQAALDRLLSElCQQGIAVVMSSHDL 193
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
410-615 |
7.50e-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: 44.87 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 410 GSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFvpempGRPRMAYVPQEayivntsllenlqfgeevskeelrralhns 489
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-----DGITPVYKPQY------------------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 490 clsrdlkewsgglrteigekgVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADtENLLCERLI--FGAWKDVTRIV 567
Cdd:cd03222 70 ---------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE-QRLNAARAIrrLSEEGKKTALV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499478341 568 VTHRLEHLAQFDQVIYIQHGRVQGQGTFSELVKTCAPFAEFYKEHGKT 615
Cdd:cd03222 128 VEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLIT 175
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
400-587 |
7.77e-05 |
|
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: 44.62 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVapregslqfvpempGRPRMAYVPQEAYIVNTSLLENLQFGEEVSK 479
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYAS--------------GKARLISFLPKFSRNKLIFIDQLQFLIDVGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 480 EELRralhnsclsrdlkewsgglrteIGEKGVNLSGGQKQRVALARaFL---RKPQIVLLDDPLSAVDADTENLLCE--- 553
Cdd:cd03238 77 GYLT----------------------LGQKLSTLSGGELQRVKLAS-ELfsePPGTLFILDEPSTGLHQQDINQLLEvik 133
|
170 180 190
....*....|....*....|....*....|....
gi 499478341 554 RLIFgawKDVTRIVVTHRLEHLAQFDQVIYIQHG 587
Cdd:cd03238 134 GLID---LGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
414-594 |
8.18e-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: 47.32 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 414 AIVGPVGAGKSSLLMSLLGEVAPREG-----------SLQFVpempgRPRMAYVPQEAYIVN-TSLLENLQFGEEVSKEE 481
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGtvlvggkdietNLDAV-----RQSLGMCPQHNILFHhLTVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 482 LRRA-LHNSCLSRDLkewsgGLRTEIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCErLIFGAW 560
Cdd:TIGR01257 1035 WEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD-LLLKYR 1108
|
170 180 190
....*....|....*....|....*....|....*
gi 499478341 561 KDVTRIVVTHRLEHLAQF-DQVIYIQHGRVQGQGT 594
Cdd:TIGR01257 1109 SGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
69-261 |
8.83e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 46.05 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 69 RPAYIWYLASS----VLALLSPVFVNRFIGTISAGVTAETLPT-ALIYGVALGLCGFLSGLcmQHYFFNSLkAYQVTTNi 143
Cdd:cd18782 1 RRALIEVLALSfvvqLLGLANPLLFQVIIDKVLVQQDLATLYViGVVMLVAALLEAVLTAL--RTYLFTDT-ANRIDLE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 144 LNERLFKHSLKLSQKSRQKNQVGDIVNHMsSDSDNVSDFPM--VFGDLISASFLIIGVVAMLFYyigwS---ALAALAVL 218
Cdd:cd18782 77 LGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTgtALTTLLDVLFSVIYIAVLFSY----SpllTLVVLATV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499478341 219 FILAPLTNYVAKKFTHLDEEMMEHRDRRVTLMTQAMNAIRVVK 261
Cdd:cd18782 152 PLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVK 194
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
992-1166 |
9.99e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 992 PEFGEI--SVEGLKVRYASHLP-QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLF-----RFIeaeEGSISIDG--VN 1061
Cdd:NF040905 251 PKIGEVvfEVKNWTVYHPLHPErKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDGkeVD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1062 TASVPlEKLRRSLAIIPQDPT----LFMGTIRNN--------------LDRYNEYSDDEvmgalkhasmwDYVQSlpdgM 1123
Cdd:NF040905 328 VSTVS-DAIDAGLAYVTEDRKgyglNLIDDIKRNitlanlgkvsrrgvIDENEEIKVAE-----------EYRKK----M 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499478341 1124 N---SAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEATASVDV 1166
Cdd:NF040905 392 NiktPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
410-544 |
1.06e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 410 GSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPE----------MPGRPRMAYVPQEAY-------IVNTSLLENLQ 472
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklQALRRDIQFIFQDPYasldprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499478341 473 FGEEVSKEELRRALhNSCLSRdlkewsGGLRTEIGEKGVN-LSGGQKQRVALARAFLRKPQIVLLDDPLSAVD 544
Cdd:PRK10261 430 VHGLLPGKAAAARV-AWLLER------VGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
705-932 |
1.47e-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: 45.09 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 705 SGHQTEWVALTAIGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESV 784
Cdd:cd18541 31 AGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 785 DVYLQW----SFDSAVHCALQVIVSIV-------LILGLMPLMVFVIapvmalYYVLQRDYRRpAREV-KRFDSVArspr 852
Cdd:cd18541 111 RMALGPgilyLVDALFLGVLVLVMMFTispkltlIALLPLPLLALLV------YRLGKKIHKR-FRKVqEAFSDLS---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 853 yAHFKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFssrIPLVGGLISMATAVGVSLSAYY---GVMD 929
Cdd:cd18541 180 -DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALF---FPLIGLLIGLSFLIVLWYGGRLvirGTIT 255
|
...
gi 499478341 930 AGT 932
Cdd:cd18541 256 LGD 258
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
400-551 |
1.53e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEM--------PgrPRmayvpQEAYIVNTSLLENL 471
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLivarlqqdP--PR-----NVEGTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 472 QFGEEVSKE--ELRRALHNSCLSRDLKE-------------WSggLRTEIGE-----------KGVNLSGGQKQRVALAR 525
Cdd:PRK11147 92 EEQAEYLKRyhDISHLVETDPSEKNLNElaklqeqldhhnlWQ--LENRINEvlaqlgldpdaALSSLSGGWLRKAALGR 169
|
170 180 190
....*....|....*....|....*....|
gi 499478341 526 AFLRKPQIVLLDDPLSAVDADT----ENLL 551
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETiewlEGFL 199
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
758-928 |
1.70e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 45.17 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 758 LSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVHCALQVIVSIVLILGLMP----LMVFVIAPVMALYYVLQRD 833
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltlLMLATVPVVVLVAVLFGRR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 834 YRRPAREVKrfDSVARSPRYAhfKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVMINRWFSSriplvggLISM 913
Cdd:cd18576 160 IRKLSKKVQ--DELAEANTIV--EETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSS-------FIIF 228
|
170
....*....|....*
gi 499478341 914 ATAVGVSLSAYYGVM 928
Cdd:cd18576 229 LLFGAIVAVLWYGGR 243
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1009-1166 |
1.84e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1009 HLPqvLKGITfkveagsrvGIIGRTGSGKSTFFQSLFRFIEAEEGSISI------DGVNTASVPLEKlrRSLAIIPQDPT 1082
Cdd:PRK11144 20 TLP--AQGIT---------AIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEK--RRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1083 LFMG-TIRNNLdrynEYSDDEVMgalkhASMWDYVQSLPdGMNSAVSEGGLNLSQGQRQLLCLARALLTKARVIVMDEAT 1161
Cdd:PRK11144 87 LFPHyKVRGNL----RYGMAKSM-----VAQFDKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
....*
gi 499478341 1162 ASVDV 1166
Cdd:PRK11144 157 ASLDL 161
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
513-598 |
2.12e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 513 LSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTE----NLLcERLIFGAWKDVtrIVVTHRLEHLAQF-DQVIYIQHG 587
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLF-ERLNKEYKKRI--IMVTHNMDQVLRIaDEVIVMHEG 227
|
90
....*....|.
gi 499478341 588 RVQGQGTFSEL 598
Cdd:PRK13645 228 KVISIGSPFEI 238
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
399-600 |
2.39e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLG--EVAPREGSLQFvpemPGRPRMAYVPQE----------AYIVNTS 466
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEF----KGKDLLELSPEDragegifmafQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENlQFGEEVSKEELRRALHNSCLSR----DLKEWSGGL---RTEIGEKGVNL--SGGQKQRVALARAFLRKPQIVLLD 537
Cdd:PRK09580 92 GVSN-QFFLQTALNAVRSYRGQEPLDRfdfqDLMEEKIALlkmPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 538 DPLSAVDADTENLLCERLifGAWKDVTR--IVVTH--RLEHLAQFDQVIYIQHGRVQGQGTFSeLVK 600
Cdd:PRK09580 171 ESDSGLDIDALKIVADGV--NSLRDGKRsfIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT-LVK 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
402-556 |
2.43e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 402 DVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMpgrpRMAYVPQ--EAYIVNTSLLENLQFGeevsK 479
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL----EVAYFDQhrAELDPEKTVMDNLAEG----K 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 480 EEL------RRALhnsclsrdlkewsGGL----------RTEIGEkgvnLSGGQKQRVALARAFLRKPQIVLLDDPLSAV 543
Cdd:PRK11147 409 QEVmvngrpRHVL-------------GYLqdflfhpkraMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170
....*....|...
gi 499478341 544 DADTENLLcERLI 556
Cdd:PRK11147 472 DVETLELL-EELL 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
399-613 |
2.48e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVA--------------PREGSLQfvpempgrPRMAYVPQE-AYIV 463
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvitggdrlvngrPLDSSFQ--------RSIGYVQQQdLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 464 NTSLLENLQFG------EEVSKEELRRALHNSCLSRDLKEWSGGLrteIGEKGVNLSGGQKQRVALARAFLRKPQ-IVLL 536
Cdd:TIGR00956 850 TSTVRESLRFSaylrqpKSVSKSEKMEYVEEVIKLLEMESYADAV---VGVPGEGLNVEQRKRLTIGVELVAKPKlLLFL 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 537 DDPLSAVDADTENLLCeRLIFGAWKDVTRIVVT-HR--LEHLAQFDQVIYIQHGrvqGQGT-FSELVKTCAPFAEFYKEH 612
Cdd:TIGR00956 927 DEPTSGLDSQTAWSIC-KLMRKLADHGQAILCTiHQpsAILFEEFDRLLLLQKG---GQTVyFGDLGENSHTIINYFEKH 1002
|
.
gi 499478341 613 G 613
Cdd:TIGR00956 1003 G 1003
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
997-1221 |
2.57e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 44.35 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 997 ISVEGLKVRYASHLP---QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSISIDGVNTASVPLEK---- 1069
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1070 LRRSLAIIPQDP--TLFMGTIRNNL----DRYNEYSDDEVMGALKHASMWDYVQSLPDgmnsavsEGGLNLSQGQRQLLC 1143
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALVGISESLFE-------KNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1144 LARALLTKARVIVMDEATASVDVQTdallQKVIRTSF-----AGVTMLIIAHRLGTIAD-CDQIVEISAGEVKSIRRPTE 1217
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKG----RKELMTLFkklhqSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKD 231
|
....
gi 499478341 1218 FSQE 1221
Cdd:PRK13649 232 IFQD 235
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
80-308 |
2.71e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 44.47 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 80 VLALLSPVFVNRFIGTISAGVTAETLPTALIYGVALGLCGFLSGLCMQH---YFFNSLKAyqvttnILNERLFKHSLKLS 156
Cdd:cd18568 16 LLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYlldYFANRIDL------SLLSDFYKHLLSLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 157 QKSRQKNQVGDIVNHMsSDSDNVSDFpMVFGDLISA--SFLIIGVVAMLFYYiGWS-ALAALAVLFILAPLTNYVAKKFT 233
Cdd:cd18568 90 LSFFASRKVGDIITRF-QENQKIRRF-LTRSALTTIldLLMVFIYLGLMFYY-NLQlTLIVLAFIPLYVLLTLLSSPKLK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 234 HLDEEMMEHRDRRVTLMTQAMNAIRVVKYFA--------WEKSVAKEVtevrEKELTSRRRLAKAEVVSSLGYLAVSTLV 305
Cdd:cd18568 167 RNSREIFQANAEQQSFLVEALTGIATIKALAaerpirwrWENKFAKAL----NTRFRGQKLSIVLQLISSLINHLGTIAV 242
|
...
gi 499478341 306 LFV 308
Cdd:cd18568 243 LWY 245
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
76-307 |
3.46e-04 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 44.04 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGVTAETLPTALIYGVALGLCGF--LSGLCM--QHYFFNSlkAYQVTTNILNERLFKH 151
Cdd:cd18573 6 LVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVfvVGAAANfgRVYLLRI--AGERIVARLRKRLFKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 152 SLklsqksRQ------KNQVGDIVNHMSSD--------SDNVSDFpmvfgdlISASFLIIGVVAMLFYYigwSALAALAV 217
Cdd:cd18573 84 IL------RQdaaffdKNKTGELVSRLSSDtsvvgkslTQNLSDG-------LRSLVSGVGGIGMMLYI---SPKLTLVM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 218 LFILAPLT-------NYVakkfthldeemmehrdRRVTLMTQA------------MNAIRVVKYFAWE----KSVAKEVT 274
Cdd:cd18573 148 LLVVPPIAvgavfygRYV----------------RKLSKQVQDaladatkvaeerLSNIRTVRAFAAErkevERYAKKVD 211
|
250 260 270
....*....|....*....|....*....|....*...
gi 499478341 275 EVrekeLTSRRRLAKAE-----VVSSLGYLAVSTLVLF 307
Cdd:cd18573 212 EV----FDLAKKEALASglffgSTGFSGNLSLLSVLYY 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1012-1190 |
3.86e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTffqsLFRfIEAeegsisidGVNTAS----VPLEKLRrsLAIIPQDPTL---- 1083
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKST----LLR-IMA--------GVDKEFegeaRPAPGIK--VGYLPQEPQLdpek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1084 --------FMGTIRNNLDRYNE----YSDD--------EVMGALK----HASMWDYVQSL---------PDGmNSAVSeg 1130
Cdd:PRK11819 86 tvrenveeGVAEVKAALDRFNEiyaaYAEPdadfdalaAEQGELQeiidAADAWDLDSQLeiamdalrcPPW-DAKVT-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1131 glNLSQGQRQLLCLARALLTKARVIVMDEATASVDVQTDALLQKVIRTsFAGvTMLIIAH 1190
Cdd:PRK11819 163 --KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD-YPG-TVVAVTH 218
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
701-943 |
5.19e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 43.61 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 701 LSYYSGHQTEWVA--------LTAIGIYGLIGVLVLVGSLLNHLFWLDRGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGR 772
Cdd:cd18589 15 IPYYTGRMTDWIMnkdapeafTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 773 IIQRFSRDVESVD-------VYLQWSFdsavhcaLQVIVSIVLILGLMPLMVFVIAPVMALYYVLQRD----YRRPAREV 841
Cdd:cd18589 95 IVSRVTTDTEDMSeslsenlSLLMWYL-------ARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFvgkfQQSLAVQV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 842 KrfDSVARSPRYAhfKESLQGLVVIRSFNKGPWFMQNFYAKLSHSNRMFYSHVM---INRWFSSriplvggLISMATAVG 918
Cdd:cd18589 168 Q--KSLARANQVA--VETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAayaVSMWTSS-------FSGLALKVG 236
|
250 260 270
....*....|....*....|....*....|..
gi 499478341 919 VslsAYYG--VMDAGTAG---LVT--LYSLSF 943
Cdd:cd18589 237 I---LYYGgqLVTAGTVSsgdLVTfvLYELQF 265
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
999-1055 |
5.80e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 5.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 999 VEGLKVRYASHlpQVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSLFRFIEAEEGSI 1055
Cdd:PRK15064 322 VENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
503-591 |
6.40e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 503 RTEIGekgvNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLLCERLIFGAWKDVTRIVVTHRL-EHLAQFDQV 581
Cdd:PRK10982 386 RTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRI 461
|
90
....*....|
gi 499478341 582 IYIQHGRVQG 591
Cdd:PRK10982 462 LVMSNGLVAG 471
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
165-227 |
1.24e-03 |
|
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: 42.46 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499478341 165 VGDIVNHMSSDSDNV-SDFPMVFGDLISASFLIIGVVAMLFYYIGWSALAALAVLFILAPLTNY 227
Cdd:cd18606 91 LGRILNRFSKDTDVLdNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANY 154
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
722-917 |
2.30e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 41.62 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 722 LIGVLVLVGSLLNHLFwldrGIRA----GKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDVYLQWSFDSAVH 797
Cdd:cd18548 47 LLALLGLIAGILAGYF----AAKAsqgfGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 798 CALQVIVSIVLILGLMP---LMVFVIAPVMAL--YYVLQRDYRRPAREVKRFDSVARSpryahFKESLQGLVVIRSFNKG 872
Cdd:cd18548 123 APIMLIGAIIMAFRINPklaLILLVAIPILALvvFLIMKKAIPLFKKVQKKLDRLNRV-----VRENLTGIRVIRAFNRE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499478341 873 PWFMQNFYAKlshSNRMFYSHVMINRWFSSRIPLVGGLISMATAV 917
Cdd:cd18548 198 DYEEERFDKA---NDDLTDTSLKAGRLMALLNPLMMLIMNLAIVA 239
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
683-869 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 683 LLLGATAATLLPlaqkawlsYYSGHQTEWVAL--------TAIGIYGLI------------GVLVLVGSLLNhlfwldrg 742
Cdd:cd18784 5 LLAAAVGEIFIP--------YYTGQVIDGIVIeksqdkfsRAIIIMGLLaiassvaagirgGLFTLAMARLN-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 743 IRagknMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDV--------ESVDVYLqWSFdsavhcaLQVIVSIVLILGL-- 812
Cdd:cd18784 69 IR----IRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTttmsdtvsLNLNIFL-RSL-------VKAIGVIVFMFKLsw 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499478341 813 -MPLMVFVIAPVMAL---YYvlQRDYRRPAREVKrfDSVARSPRYAhfKESLQGLVVIRSF 869
Cdd:cd18784 137 qLSLVTLIGLPLIAIvskVY--GDYYKKLSKAVQ--DSLAKANEVA--EETISSIRTVRSF 191
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
682-917 |
3.00e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 41.34 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 682 TLLLGATAATLLPLAQKAWLSYYSGHQTEWValtaigiyGLIGVLVLVGSLLNHLFWLdrgiragknmhdkmlksvlssP 761
Cdd:cd18564 51 ALLLLAAAALVGIALLRGLASYAGTYLTALV--------GQRVVLDLRRDLFAHLQRL---------------------S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 762 VRFFDSTPVGRIIQRFSRDVESV-DVYLQWSFDSAVHcalqvIVSIVLILGLM-------PLMVFVIAPVMALY-YVLQR 832
Cdd:cd18564 102 LSFHDRRRTGDLLSRLTGDVGAIqDLLVSGVLPLLTN-----LLTLVGMLGVMfwldwqlALIALAVAPLLLLAaRRFSR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 833 DYRRPAREVKRFDS--VARSpryahfKESLQGLVVIRSFNKGPWFMQNFYAklsHSNRMFYSHVMINRWFSSRIPLVGGL 910
Cdd:cd18564 177 RIKEASREQRRREGalASVA------QESLSAIRVVQAFGREEHEERRFAR---ENRKSLRAGLRAARLQALLSPVVDVL 247
|
....*..
gi 499478341 911 ISMATAV 917
Cdd:cd18564 248 VAVGTAL 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
400-598 |
3.75e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 400 LHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVpempGRPRMAYVP---QEA----------YIVNTS 466
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYL----GKEVTFNGPkssQEAgigiihqelnLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 467 LLENLQFGEEVS--------KEELRRAlhNSCLSR-DLKEWSgglRTEIGEkgvnLSGGQKQRVALARAFLRKPQIVLLD 537
Cdd:PRK10762 96 IAENIFLGREFVnrfgridwKKMYAEA--DKLLARlNLRFSS---DKLVGE----LSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499478341 538 DPLSAV-DADTENLLceRLIfGAWKDVTR-IV-VTHRLEHLAQF-DQVIYIQHGRVQGQGTFSEL 598
Cdd:PRK10762 167 EPTDALtDTETESLF--RVI-RELKSQGRgIVyISHRLKEIFEIcDDVTVFRDGQFIAEREVADL 228
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
399-551 |
3.95e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 399 VLHDVNVHVPAGSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQF----VPEMPgRPRMAYVPQEAYI-VNTSLLENLQF 473
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYkncnINNIA-KPYCTYIGHNLGLkLEMTVFENLKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 474 GEEV--SKEELRRALHNSCLSrDLkewsgglrteIGEKGVNLSGGQKQRVALARAFLRKPQIVLLDDPLSAVDADTENLL 551
Cdd:PRK13541 94 WSEIynSAETLYAAIHYFKLH-DL----------LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
76-311 |
4.15e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 40.54 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 76 LASSVLALLSPVFVNRFIGTISAGVTAETLPTALIYGVALGLCGFLSGLCmQHYFFNSLkAYQVTTNiLNERLFKHSLKL 155
Cdd:cd18550 9 LLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVV-QTYLSARI-GQGVMYD-LRVQLYAHLQRM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 156 SQKSRQKNQVGDIVNHMSSDSDNVSDfpmVFGDLISASF-----LIIGVVAMLfyYIGWS-ALAALAVLFILAPLTNYVA 229
Cdd:cd18550 86 SLAFFTRTRTGEIQSRLNNDVGGAQS---VVTGTLTSVVsnvvtLVATLVAML--ALDWRlALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 230 KKFTHLDEEMMEHRDRRVTLMTQAMNA--IRVVKYFAweksvakevtevREKELTSR-----RRLAKAEVVSSL-GYLAV 301
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFG------------REDDEAARfarrsRELRDLGVRQALaGRWFF 228
|
250
....*....|
gi 499478341 302 STLVLFVALA 311
Cdd:cd18550 229 AALGLFTAIG 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
410-583 |
5.67e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 410 GSSLAIVGPVGAGKSSLLMSLLGEVAPREGSLQFVPEMP--------------------GRPRMAYVPQeaYI------- 462
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDevlkrfrgtelqnyfkklynGEIKVVHKPQ--YVdlipkvf 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 463 ---VNtSLLENLQfgEEVSKEELRRALH-NSCLSRDLKEwsgglrteigekgvnLSGGQKQRVALARAFLRKPQIVLLDD 538
Cdd:PRK13409 177 kgkVR-ELLKKVD--ERGKLDEVVERLGlENILDRDISE---------------LSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499478341 539 PLSAVDAdTENLLCERLIFGAWKDVTRIVVTHR---LEHLAQFDQVIY 583
Cdd:PRK13409 239 PTSYLDI-RQRLNVARLIRELAEGKYVLVVEHDlavLDYLADNVHIAY 285
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
711-971 |
6.01e-03 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 40.13 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 711 WVALTAIGIYGLIGVLVLVGSLLNHLFwldrGIRAGKNMHDKMLKSVLSSPVRFFDSTPVGRIIQRFSRDVESVDvylqw 790
Cdd:cd18549 43 IIGAILLALYILRTLLNYFVTYWGHVM----GARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDIS----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 791 sfDSAVHCALQVIVSIVLILG----------LMPLMVFVIAPVMALYYVLQRdyrrparevKRFDSVARSPR------YA 854
Cdd:cd18549 114 --ELAHHGPEDLFISIITIIGsfiilltinvPLTLIVFALLPLMIIFTIYFN---------KKMKKAFRRVRekigeiNA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 855 HFKESLQGLVVIRSFNKGPWFMQNFyaklSHSNRMFYS------HVMinRWFSSRIPLVGGLISMATAVGVSLSAYYGVM 928
Cdd:cd18549 183 QLEDSLSGIRVVKAFANEEYEIEKF----DEGNDRFLEskkkayKAM--AYFFSGMNFFTNLLNLVVLVAGGYFIIKGEI 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499478341 929 DAGTagLVT--LYslsfwgflnwgVRIFadiesrMTSIERLKFFS 971
Cdd:cd18549 257 TLGD--LVAflLY-----------VNVF------IKPIRRLVNFT 282
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1012-1165 |
6.30e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 40.80 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1012 QVLKGITFKVEAGSRVGIIGRTGSGKSTFFQSL-FRFIEAEEGSISIdGVNTASVPLEKLRRSLAIIPQD----PTL--- 1083
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKGSGSV-LLNGMPIDAKEMRAISAYVQQDdlfiPTLtvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 1084 ----FMGTIRnnLDRYNEYSD-----DEVMGALKHASMWDYVQSLPDGMNSavsegglnLSQGQRQLLCLARALLTKARV 1154
Cdd:TIGR00955 118 ehlmFQAHLR--MPRRVTKKEkrervDEVLQALGLRKCANTRIGVPGRVKG--------LSGGERKRLAFASELLTDPPL 187
|
170
....*....|.
gi 499478341 1155 IVMDEATASVD 1165
Cdd:TIGR00955 188 LFCDEPTSGLD 198
|
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
340-433 |
6.34e-03 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 40.48 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 340 GDLSRLISRATN------AKVGARriLDYLNEDEVEISTEE-RTDGAAVGLQMQHfsLRHDGAVSDVLHDvnvhvpaGSS 412
Cdd:PRK05291 149 GALSKLINELREellellALVEAA--IDFPEEDIEFLSDEKiLEKLEELIAELEA--LLASARQGEILRE-------GLK 217
|
90 100
....*....|....*....|.
gi 499478341 413 LAIVGPVGAGKSSLLMSLLGE 433
Cdd:PRK05291 218 VVIAGRPNVGKSSLLNALLGE 238
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
711-924 |
8.28e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 39.83 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 711 WVALTAIGIYGLIGVLVLVGSLLNHLF-W-LDRGIRagKNMHDKMLKsvLSspVRFFDSTPVGRIIQRFSRDVESVDVYL 788
Cdd:cd18778 41 GLALLLLGAYLLRALLNFLRIYLNHVAeQkVVADLR--SDLYDKLQR--LS--LRYFDDRQTGDLMSRVINDVANVERLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499478341 789 QWSFDSAVHCALQVIVSIVLILGLMP-LMVFVIAPVMALYYVLQRdYRRPAREVKRFDSVARSPRYAHFKESLQGLVVIR 867
Cdd:cd18778 115 ADGIPQGITNVLTLVGVAIILFSINPkLALLTLIPIPFLALGAWL-YSKKVRPRYRKVREALGELNALLQDNLSGIREIQ 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499478341 868 SFNKGPWFMQNFYAKlshSNRMFYSHVMINRWFSSRIPLVGGLISMATAVGVSLSAY 924
Cdd:cd18778 194 AFGREEEEAKRFEAL---SRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGR 247
|
|
| |
