|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
224-1578 |
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: 828.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 224 LLSKGTYWWMNAFIKTAHRKPI---DLRAIGK----LPIAMRALTNYQRLCAAFDAQ------ARKDTQSQQGAR----- 285
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsEMVVPVLVENWKKECKKTRKQpvsavyGKKDPSKPKGSSqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 286 -----------------AIWRALCHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVdhlgkeNHVFQPKTQFLGVYFVSS 348
Cdd:TIGR00957 289 eevealivksphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLI------RFVNDPMAPDWQGYFYTG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 349 QEFLgnayvlavllflALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKImhLSTSNLSMGEMTAGQICNLVAIDTNQL 428
Cdd:TIGR00957 363 LLFV------------CACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKA--LVITNSARKSSTVGEIVNLMSVDAQRF 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 429 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 508
Cdd:TIGR00957 429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 509 LKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVT 588
Cdd:TIGR00957 509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 589 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIrEEQCAPREPAPQGQAgkyqavplkvvnrkrpareevrdllgplqrltp 668
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLSHEEL-EPDSIERRTIKPGEG--------------------------------- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 669 smdgdadnFCVQIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpdsege 748
Cdd:TIGR00957 635 --------NSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------- 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 749 dpsnperetaadsdaRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGIN 828
Cdd:TIGR00957 696 ---------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVN 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQ--AGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGT 906
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRILVTHGISYLPQVDVIIVMSGGK 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 907 I----------QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE-LEKETVM----------ERK---APEPSQGLP 956
Cdd:TIGR00957 839 IsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEaKLIENGMlvtdvvgkqlQRQlsaSSSDSGDQS 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 957 RAMSSRDGLLLDEDEEEEEAAESEEDDNLSSVlhqRAKIPWractKYLSSAGVLLLSLLVFSQLLKHMVLVAIDYWLAKW 1036
Cdd:TIGR00957 919 RHHGSSAELQKAEAKEETWKLMEADKAQTGQV---ELSVYW----DYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLW 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1037 TDSALVLSPAARNcslsqecALDQSVYAmvftvlcSLGI---ALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFE 1113
Cdd:TIGR00957 992 TDDPMVNGTQNNT-------SLRLSVYG-------ALGIlqgFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE 1057
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1114 TTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDD 1193
Cdd:TIGR00957 1058 RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLES 1137
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1194 TTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNslHR 1273
Cdd:TIGR00957 1138 VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVIS--RH 1215
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1274 ELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQN 1348
Cdd:TIGR00957 1216 SLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE------APWQIqetapPSGWPPRGRVEFRN 1289
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1349 LSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP 1428
Cdd:TIGR00957 1290 YCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDP 1369
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1429 VLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEAT 1508
Cdd:TIGR00957 1370 VLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1509 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKdSVFASFVR 1578
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
222-1579 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 715.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 222 VNLLSKGTYWWMNAFIKTAHRKPIDLRAIGKLPIAMRALTNYQRLCAAFDAQARKDTQsqqgaraiW--RALCHAFGRRL 299
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKP--------WllRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 300 VLSSTFRILADLLGFAGPLcifgIVDHLGKENHVFQPKTQ--------FLGVyfvssqeFLGnayvlavllflalllqrT 371
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPL----LLNLLLESMQNGEPAWIgyiyafsiFVGV-------VLG-----------------V 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 372 FLQASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 450
Cdd:PLN03130 356 LCEAQYFQNVmRVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMV 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 451 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEM 530
Cdd:PLN03130 434 LLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDEL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 531 TSLRAFAVYTSISIFMNTAIPIAAVLITFvGHVSFFKeSDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:PLN03130 514 SWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLG-GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 611 SEFLSsAEirEEQCAPREPAPQGQagkyqavplkvvnrkrPAreevrdllgplqrltpsmdgdadnfcVQIIGGFFTWTP 690
Cdd:PLN03130 592 EELLL-AE--ERVLLPNPPLEPGL----------------PA--------------------------ISIKNGYFSWDS 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSgavfwnslpdsegedpsnperetaaDSDARSRGPV 769
Cdd:PLN03130 627 KAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS-------------------------DASVVIRGTV 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNV 849
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 850 VFLDDPFSALDVHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-------FQrsecQ 922
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEElsnngplFQ----K 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 923 LFEHWKTLMNRQDQELEKE---TVMERKAPEPSQGLPRAMSSRDgllldedeeeeeaaeseEDDNLSSVLHQRAK----- 994
Cdd:PLN03130 836 LMENAGKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSKK-----------------KSKEGKSVLIKQEEretgv 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 995 IPWRACTKYLSSAGVLLLSLLVFSQLLKHMVL-VAIDYWLAKWTDSALVLS--PAARNcslsqecaldqSVYAMVF--TV 1069
Cdd:PLN03130 899 VSWKVLERYKNALGGAWVVMILFLCYVLTEVFrVSSSTWLSEWTDQGTPKThgPLFYN-----------LIYALLSfgQV 967
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1070 LCSLGIALCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLC 1149
Cdd:PLN03130 968 LVTLLNSYWLIMS------SLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQL 1041
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1150 VSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEY 1229
Cdd:PLN03130 1042 LSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRS 1121
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1230 TDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSI---SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEI 1306
Cdd:PLN03130 1122 MDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVmqnGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAEN 1201
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1307 QLGAVKRIHTLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTG 1381
Cdd:PLN03130 1202 SLNAVERVGTYIDLPSE------APLVIennrpPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTG 1275
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1382 SGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKL 1461
Cdd:PLN03130 1276 AGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKD 1355
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1462 VVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHT 1541
Cdd:PLN03130 1356 VIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNT 1435
|
1370 1380 1390
....*....|....*....|....*....|....*...
gi 1274095655 1542 ILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRA 1579
Cdd:PLN03130 1436 IIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-1579 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 708.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 223 NLLSKGTYWWMNAFIKTAHRKPIDLRAIGKLPIAMRALTNYQRLcaafdaQARKDTQSQQGARAIWRALCHAFGRRLVLS 302
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRF------QRCWTEESRRPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 303 STFRILADLLGFAGPLcifgIVDHLGKENHVFQPKtqFLGvYFVSSQEFLGNAYVlavllflalllqrTFLQASYYVAI- 381
Cdd:PLN03232 307 GIFKIGHDLSQFVGPV----ILSHLLQSMQEGDPA--WVG-YVYAFLIFFGVTFG-------------VLCESQYFQNVg 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 382 ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSAL 461
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 462 IGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTS 541
Cdd:PLN03232 445 FGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 542 ISIFMNTAIPIAAVLITFvgHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSaeirE 621
Cdd:PLN03232 525 FNSFILNSIPVVVTLVSF--GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLS----E 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 622 EQCAPREPapqgqagkyqavplkvvnrkrpareevrdllgPLQRLTPSmdgdadnfcVQIIGGFFTW-TPDGIPTLSNIT 700
Cdd:PLN03232 599 ERILAQNP--------------------------------PLQPGAPA---------ISIKNGYFSWdSKTSKPTLSDIN 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 701 IRIPRGQLTMIVGQVGCGKSSLLLATLGEmqrvsgavfwnsLPDSEgedpsnperetaaDSDARSRGPVAYASQKPWLLN 780
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGE------------LSHAE-------------TSSVVIRGSVAYVPQVSWIFN 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 781 ATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALD 860
Cdd:PLN03232 693 ATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 861 VHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEcQLFEHWKT---LMNRQDQE 937
Cdd:PLN03232 773 AHVAHQVFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG-SLFKKLMEnagKMDATQEV 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 938 LEKETVMERKAPEPS-----QGLPRAMSSRDGllldedeeeeeaaeseeddnlSSVL-----HQRAKIPWRACTKYLSSA 1007
Cdd:PLN03232 850 NTNDENILKLGPTVTidvseRNLGSTKQGKRG---------------------RSVLvkqeeRETGIISWNVLMRYNKAV 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1008 GVLLLSLLVFSQLLKHMVL-VAIDYWLAKWTDSALVLSpaarncslsqecaLDQSVYAMVFTVLCSLGIALCLVTSVTVE 1086
Cdd:PLN03232 909 GGLWVVMILLVCYLTTEVLrVSSSTWLSIWTDQSTPKS-------------YSPGFYIVVYALLGFGQVAVTFTNSFWLI 975
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1087 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVA 1166
Cdd:PLN03232 976 SSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWA 1055
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1167 LLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRW 1246
Cdd:PLN03232 1056 IMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRW 1135
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1247 LEVRMEYIGACVVLIAAATSI---SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAE 1323
Cdd:PLN03232 1136 LTIRLETLGGVMIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSE 1215
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1324 syegllAPSLIPKN-----WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMF 1398
Cdd:PLN03232 1216 ------ATAIIENNrpvsgWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE 1289
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1399 EGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGG 1478
Cdd:PLN03232 1290 KGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGG 1369
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILE 1558
Cdd:PLN03232 1370 ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
1370 1380
....*....|....*....|.
gi 1274095655 1559 FDKPEKLLSQKDSVFASFVRA 1579
Cdd:PLN03232 1450 YDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
369-1579 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 626.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 369 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDT---NQLMWFfflCPNLWAMPVQI 445
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVeriNSFMQY---CMYLWSSPMVL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 446 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMT 525
Cdd:PTZ00243 375 LLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 526 RRKEMTSLRAFAVYTSISIFMNTAIP---IAAVLITF--VGHvsffkesDFSPSVAFASLSLFHILVTPLFLLSSVVRST 600
Cdd:PTZ00243 455 RARELRYLRDVQLARVATSFVNNATPtlmIAVVFTVYylLGH-------ELTPEVVFPTIALLGVLRMPFFMIPWVFTTV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 601 VKALVSVQKLSEFLSS---------------AEIREEQCA--------------------PREPA--------------- 630
Cdd:PTZ00243 528 LQFLVSIKRISTFLECdnatcstvqdmeeywREQREHSTAcqlaavlenvdvtafvpvklPRAPKvktsllsralrmlcc 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 631 PQGQAGKYQAVPLKVVNR------KRPAREEVRDLLGPLQRLTPSMDGDADNFCVQIiGGFFTWTPDGIptLSNITIRIP 704
Cdd:PTZ00243 608 EQCRPTKRHPSPSVVVEDtdygspSSASRHIVEGGTGGGHEATPTSERSAKTPKMKT-DDFFELEPKVL--LRDVSVSVP 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 705 RGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfWNslpdsegedpsnperetaadsdARSrgpVAYASQKPWLLNATVE 784
Cdd:PTZ00243 685 RGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WA----------------------ERS---IAYVPQQAWIMNATVR 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 785 ENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLS 864
Cdd:PTZ00243 739 GNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 865 DHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS---------ECQLFEHWKTLMNRQD 935
Cdd:PTZ00243 819 ERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTslyatlaaeLKENKDSKEGDADAEV 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 936 QELE----KETVMERKAPEP----SQGLPRAMSSRDGLLLdedeeeeeaaeseeddnlssVLHQRA--KIPWRACTKYLS 1005
Cdd:PTZ00243 897 AEVDaapgGAVDHEPPVAKQegnaEGGDGAALDAAAGRLM--------------------TREEKAsgSVPWSTYVAYLR 956
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1006 S-AGVLLLSLLVFSQLLKHMVLVAIDYWLAKWTdsalvlspaarncslSQECALDQSVYAMVFTVLCSLGIA---LCLVT 1081
Cdd:PTZ00243 957 FcGGLHAAGFVLATFAVTELVTVSSGVWLSMWS---------------TRSFKLSAATYLYVYLGIVLLGTFsvpLRFFL 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1082 SVTVEWTGlkvAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP 1161
Cdd:PTZ00243 1022 SYEAMRRG---SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQP 1098
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1162 VFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLT 1241
Cdd:PTZ00243 1099 FVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLEN 1178
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1242 AANRWLEVRMEYIGACVVLIAAATSISNSLHRELS--AGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKR----IH 1315
Cdd:PTZ00243 1179 VANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERllyyTD 1258
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1316 TL-------LKTE---AESYEGLLA---------PSLIPKNWP---DQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQK 1373
Cdd:PTZ00243 1259 EVphedmpeLDEEvdaLERRTGMAAdvtgtvviePASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREK 1338
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1374 IGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEA 1453
Cdd:PTZ00243 1339 VGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAA 1418
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1454 LEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFI-MDEATASIDMATENILQKVVMTAFADRTV 1532
Cdd:PTZ00243 1419 LELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQATVMSAFSAYTV 1498
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*..
gi 1274095655 1533 VTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRA 1579
Cdd:PTZ00243 1499 ITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1342-1581 |
4.04e-151 |
|
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: 460.92 E-value: 4.04e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1342 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1501
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1502 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRADK 1581
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
679-906 |
7.09e-144 |
|
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: 439.84 E-value: 7.09e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 679 VQIIGGFFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSlpdsegedpSNPERETA 758
Cdd:cd03290 1 VQVTNGYFSWGS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---------KNESEPSF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 759 ADSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRIS 838
Cdd:cd03290 71 EATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 906
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
1022-1316 |
7.92e-142 |
|
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: 438.19 E-value: 7.92e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1022 KHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLL 1101
Cdd:cd18602 11 KQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1102 NRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF 1181
Cdd:cd18602 91 RNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1182 RVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLI 1261
Cdd:cd18602 171 RASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1262 AAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHT 1316
Cdd:cd18602 251 AALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLE 305
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
301-610 |
5.66e-140 |
|
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: 433.20 E-value: 5.66e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVA 380
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVSYVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 381 IETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYT 540
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 541 SISIFMNTAIPIAAVLITFVGHVsFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYP-YLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
223-1581 |
4.82e-125 |
|
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: 427.40 E-value: 4.82e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 223 NLLSKGTYWWMNAFIKTAHRKPIDLRAIGKLPIAMRALTNYQRLCAAFDaqaRKDTQSQQGARAIwRALCHAFGRRLVLs 302
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWD---RELASAKKNPKLL-NALRRCFFWRFVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 303 stfriladllgfagplciFGIVDHLGKENHVFQPKT--QFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVA 380
Cdd:TIGR01271 85 ------------------YGILLYFGEATKAVQPLLlgRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 381 IETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:TIGR01271 147 HHLGMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAvyt 540
Cdd:TIGR01271 225 FCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 541 SISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHIL-VTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEI 619
Cdd:TIGR01271 302 YLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 620 R--EEQCAPREpapqgqagkyqavpLKVVNRKRPAREEVRDLLGPLQ-----RLTPsmDGDAdnfcvqiiGGFFT-WTPD 691
Cdd:TIGR01271 382 KtlEYNLTTTE--------------VEMVNVTASWDEGIGELFEKIKqnnkaRKQP--NGDD--------GLFFSnFSLY 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQrvsgavfwnslpdsegedPSnperetaaDSDARSRGPVAY 771
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE------------------PS--------EGKIKHSGRISF 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVF 851
Cdd:TIGR01271 492 SPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYL 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 852 LDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE---------CQ 922
Cdd:TIGR01271 572 LDSPFTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfsslllgLE 649
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 923 LFEHWK----------TL---------------------------------------------------------MNRQD 935
Cdd:TIGR01271 650 AFDNFSaerrnsilteTLrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkfsfvqmgpqkAQATT 729
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 936 QELEKETVMERK---APEPSQG---LPRAMSSRDGLLLDEDEEEEEAAESEEDDNLSSVLHQRakipwRACTKYLSSAGV 1009
Cdd:TIGR01271 730 IEDAVREPSERKfslVPEDEQGeesLPRGNQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQL-----QTSFRKKSSITQ 804
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1010 LLLSLLVF-----------------------------------------------SQLLKHMVLVAI---DYWLAKWTDS 1039
Cdd:TIGR01271 805 QNELASELdiysrrlskdsvyeiseeineedlkecfaderenvfetttwntylryITTNRNLVFVLIfclVIFLAEVAAS 884
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1040 ALVL-----SPAARNcSLSQECALDQS---VYAMVFTVLCSLGI------------ALCLVTSVTVEWTGLKVAKRLHRS 1099
Cdd:TIGR01271 885 LLGLwlitdNPSAPN-YVDQQHANASSpdvQKPVIITPTSAYYIfyiyvgtadsvlALGFFRGLPLVHTLLTVSKRLHEQ 963
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1100 LLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQK 1179
Cdd:TIGR01271 964 MLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRA 1043
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1180 YFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF----RYEARFQQKLLEYTdsnniASLFLTAAN-RWLEVRMEYI 1254
Cdd:TIGR01271 1044 YFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFgrqsYFETLFHKALNLHT-----ANWFLYLSTlRWFQMRIDII 1118
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1255 gaCVVLIAAATSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAESYE-------G 1327
Cdd:TIGR01271 1119 --FVFFFIAVTFIAIGTNQD-GEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRpsggggkY 1195
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1328 LLAPSLIPKN------WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMfEGR 1401
Cdd:TIGR01271 1196 QLSTVLVIENphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGE 1274
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1402 IIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENF 1481
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVL 1354
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1482 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDK 1561
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
1530 1540
....*....|....*....|
gi 1274095655 1562 PEKLLSQKDSVFASFVRADK 1581
Cdd:TIGR01271 1435 IQKLLNETSLFKQAMSAADR 1454
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1342-1562 |
1.83e-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: 354.49 E-value: 1.83e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1342 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1501
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 1502 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKP 1562
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
679-906 |
1.98e-101 |
|
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: 322.88 E-value: 1.98e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 679 VQIIGGFFTWTPDGI---PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdsegedpsnper 755
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 756 etaadsdarsrGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQ 835
Cdd:cd03250 66 -----------GSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 836 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 906
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1063-1579 |
1.78e-93 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 315.18 E-value: 1.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1063 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1142
Cdd:COG1132 63 LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1143 SRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1218
Cdd:COG1132 143 VRSVVTLIGALVVLFVIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAE----LNGRLQESLSGIRVVKAFGR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1219 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMV 1298
Cdd:COG1132 219 EERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1299 RNLADMEIQLGAVKRIHTLLKTEAESYEGLLAPSLIPknwpDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICG 1378
Cdd:COG1132 299 NVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPP----VRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1379 RTGSGKSSF-SLaFFRM------------VDMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPE 1442
Cdd:COG1132 374 PSGSGKSTLvNL-LLRFydptsgrilidgVDI------------RDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1443 KkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 1522
Cdd:COG1132 441 A--TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1523 VMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFASFVRA 1579
Cdd:COG1132 519 LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL-ARGGLYARLYRL 574
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
1027-1315 |
5.12e-85 |
|
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: 280.16 E-value: 5.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1027 VAIDYWLAKWTDSAlvlspaarncslSQECALDQSVYAMVFTVLCSLG-IALCLVTSVTVEWTGLKVAKRLHRSLLNRII 1105
Cdd:cd18580 16 QFSNIWLDWWSSDW------------SSSPNSSSGYYLGVYAALLVLAsVLLVLLRWLLFVLAGLRASRRLHDKLLRSVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1106 LAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVAS 1185
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1186 RDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAAT 1265
Cdd:cd18580 164 RQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1266 SIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1315
Cdd:cd18580 244 AV--LLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERIL 291
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
1023-1315 |
8.19e-82 |
|
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: 271.27 E-value: 8.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1023 HMVLVAIDYWLAKWTDSALVLSPAA---RNCSLSqecaldqsVYAM--VFTVLCSLGIALCLVTSvtvewtGLKVAKRLH 1097
Cdd:cd18603 12 QAFSVGSNIWLSEWSDDPALNGTQDteqRDYRLG--------VYGAlgLGQAIFVFLGSLALALG------CVRASRNLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1098 RSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFI 1177
Cdd:cd18603 78 NKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1178 QKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGAC 1257
Cdd:cd18603 158 QRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 1258 VVLIAAATSIsnsLHRE-LSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1315
Cdd:cd18603 238 IVLFAALFAV---LSRDsLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIK 293
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1062-1578 |
1.07e-78 |
|
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: 276.33 E-value: 1.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1062 VYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLEC 1141
Cdd:COG2274 197 VLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1142 LSRSTLLCVSALTVISY----VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 1217
Cdd:COG2274 276 ALLDLLFVLIFLIVLFFysppLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQ----SLLVETLRGIETIKALG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1218 YEARFQQK-------LLEYTDSNNIASLFLTAANRWLEVrmeyIGACVVLIAAATSIsnsLHRELSAGlvglGLTYALMV 1290
Cdd:COG2274 352 AESRFRRRwenllakYLNARFKLRRLSNLLSTLSGLLQQ----LATVALLWLGAYLV---IDGQLTLG----QLIAFNIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1291 SNYLNWMVRNLADM--EIQ--LGAVKRIHTLLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSLKPVLKHVNA 1366
Cdd:COG2274 421 SGRFLAPVAQLIGLlqRFQdaKIALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGDSPPVLDNISL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1367 LIAPGQKIGICGRTGSGKSSFS--LAFFRM----------VDMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGT 1434
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLklLLGLYEptsgrilidgIDL------------RQIDPASLRRQIGVVLQDVFLFSGT 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1435 IRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASI 1511
Cdd:COG2274 565 IRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1512 DMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFASFVR 1578
Cdd:COG2274 643 DAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL-ARKGLYAELVQ 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1338-1562 |
3.33e-78 |
|
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: 257.34 E-value: 3.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1338 WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTL 1417
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1418 RSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEiaqlklvvkalpggldaiITEGGENFSQGQRQLFCLARAFVR 1497
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1498 KTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKP 1562
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
1023-1315 |
6.39e-78 |
|
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: 260.09 E-value: 6.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1023 HMVLVAIDYWLAKWT---DSALVLSPAARNcslsqecaldQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRS 1099
Cdd:cd18604 12 QLLSVGQSWWLGIWAsayETSSALPPSEVS----------VLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1100 LLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQK 1179
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1180 YFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVV 1259
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 1260 LIAAATSISNslhRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1315
Cdd:cd18604 242 FATAALLVYG---PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQ 294
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
1028-1315 |
2.08e-72 |
|
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: 244.36 E-value: 2.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1028 AIDYWLAKWTDSAlvlspaarNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILA 1107
Cdd:cd18605 17 LIDFWLSYWVSHS--------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1108 PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRD 1187
Cdd:cd18605 89 KMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1188 LQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSI 1267
Cdd:cd18605 169 LKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1274095655 1268 -SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1315
Cdd:cd18605 249 vQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVR 297
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
301-610 |
1.05e-71 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 242.01 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENHvfQPKTQ-------FLGVYFVSSqeflgnayvlavllflalllqrTFL 373
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD--EPLSEgyllalaLFLVSLLQS----------------------LLL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 374 QASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 453
Cdd:cd18579 57 HQYFFLSFRLGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 454 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSL 533
Cdd:cd18579 135 RLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKAL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 534 RAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKEsdFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18579 215 RKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNP--LTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
1030-1316 |
3.83e-67 |
|
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: 229.76 E-value: 3.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1030 DYWLAKW------TDSALVLSPAARNCSLSQECALD--QSVYAMVFTVLCSLGIALCLVTSVTVewtgLKVAKRLHRSLL 1101
Cdd:cd18599 23 DWWLSYWlkqgsgNTTNNVDNSTVDSGNISDNPDLNfyQLVYGGSILVILLLSLIRGFVFVKVT----LRASSRLHNKLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1102 NRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF 1181
Cdd:cd18599 99 QKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1182 RVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLI 1261
Cdd:cd18599 179 RRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLI 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1262 AAATSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHT 1316
Cdd:cd18599 259 TALLVV--LLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILE 311
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
1027-1315 |
5.45e-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: 5.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1027 VAIDYWLAKWTDSALVLSpaarncslsqecaldQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIIL 1106
Cdd:cd18606 16 VFTNLWLSFWTEDFFGLS---------------QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1107 APMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASR 1186
Cdd:cd18606 81 APMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1187 DLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASlFLTAAN-RWLEVRMEYIGACVVLIAAAT 1265
Cdd:cd18606 161 ELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAY-FLTIANqRWLAIRLDLLGSLLVLIVALL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1266 SISNSLHreLSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1315
Cdd:cd18606 240 CVTRRFS--ISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLL 287
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1342-1570 |
7.09e-61 |
|
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: 208.23 E-value: 7.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1342 GKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFSGTIRFNLDPEKKCSDSTLW-EALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1501 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 1570
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
285-912 |
1.43e-60 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 219.27 E-value: 1.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 285 RAIWRALcHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGkENHVFQPKTQFLGVYFVSsqeFLGNAyvlavllfl 364
Cdd:COG1132 10 RRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSALLLLLLLLLGL---ALLRA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 365 alllqrTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFF-FLCPNLWAMPV 443
Cdd:COG1132 76 ------LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 444 QIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FC 519
Cdd:COG1132 148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 520 SRVEMTRRKEMTSLRAFAVYTSISIFMNTaipIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRS 599
Cdd:COG1132 228 EANEELRRANLRAARLSALFFPLMELLGN---LGLALVLLVG-GLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 600 TVKALVSVQKLSEFLSsaeireeqcaprepAPQGQAGKYQAVPLKvvnrkrPAREEVRdllgpLQRLTpsmdgdadnfcv 679
Cdd:COG1132 304 LQRALASAERIFELLD--------------EPPEIPDPPGAVPLP------PVRGEIE-----FENVS------------ 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 680 qiiggfFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNslpdseGEDPsnpeRET 757
Cdd:COG1132 347 ------FSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnLLLRFYDPT--SGRILID------GVDI----RDL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 758 AADSdARSRgpVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQ 833
Cdd:COG1132 408 TLES-LRRQ--IGVVPQDTFLFSGTIRENIRYGRPdATDEE---VEEAAkaaQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 834 RQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
369-610 |
2.10e-59 |
|
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: 206.55 E-value: 2.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 369 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVG 448
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 449 VILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRK 528
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 529 EMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 1274095655 609 KL 610
Cdd:cd18595 289 RL 290
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1089-1569 |
4.46e-59 |
|
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: 214.24 E-value: 4.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1089 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFL 1164
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWlsglILL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1165 VA--LLPLAVVcyFIQKYFRVASRdlQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASL---- 1238
Cdd:COG4988 166 VTapLIPLFMI--LVGKGAAKASR--RQWRALARLS--GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMkvlr 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1239 --FLTAAnrwleVrME---YIGACVVLIAAATSisnslhreLSAGLVGL--GLTYALMVSNYLNWMvRNL-----ADMEI 1306
Cdd:COG4988 240 vaFLSSA-----V-LEffaSLSIALVAVYIGFR--------LLGGSLTLfaALFVLLLAPEFFLPL-RDLgsfyhARANG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1307 qLGAVKRIHTLLKTEAESyeglLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSS 1386
Cdd:COG4988 305 -IAAAEKIFALLDAPEPA----APAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKST 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1387 FSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVV 1463
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPD--ASDEELEAALEAAGLDEFV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1464 KALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL 1543
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
490 500
....*....|....*....|....*.
gi 1274095655 1544 SADLVMVLKRGAILEFDKPEKLLSQK 1569
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
1030-1314 |
1.51e-56 |
|
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: 199.08 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1030 DYWLAKWTDS-----ALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRI 1104
Cdd:cd18601 23 DWWLSYWANLeeklnDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1105 ILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVA 1184
Cdd:cd18601 103 LRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1185 SRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIA-SLFLTaANRWLEVRMEYIgaCVVLIAA 1263
Cdd:cd18601 183 SREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAwFLFLA-TSRWLAVRLDAL--CALFVTV 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 1264 ATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1314
Cdd:cd18601 260 VAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
371-912 |
2.45e-55 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 206.61 E-value: 2.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 371 TFLQASYYVAIETGINLRgaIQTKIYNKIMHLSTSNL---SMGEMTA-----GQICNLVaidTNQLMWFFFLCPnlwamp 442
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDLASrfrdvESIREFL---TGSLLTALLDLL------ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 443 vQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRV 522
Cdd:COG2274 282 -FVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRW 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 523 E-MTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTV 601
Cdd:COG2274 361 EnLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 602 KALVSVQKLSEFLSsaeireeqcAPREPAPqgqagkyqavplkvvnrkrpareevrdllGPLQRLTPSMDGDadnfcVQI 681
Cdd:COG2274 440 DAKIALERLDDILD---------LPPEREE-----------------------------GRSKLSLPRLKGD-----IEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 682 IGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLpDSEGEDPSnperetaads 761
Cdd:COG2274 477 ENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI-DLRQIDPA---------- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 762 DARSRgpVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRI 837
Cdd:COG2274 546 SLRRQ--IGVVLQDVFLFSGTIRENITLGDPdATDEE---IIEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRL 620
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 838 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
372-610 |
3.54e-53 |
|
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: 188.82 E-value: 3.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMT 531
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 532 SLRAFAVYTSISIFMNTAIPIAAVLITFVghVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18597 217 YVRKLQILRSILTAVAFSLPVLASMLSFI--TYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1080-1575 |
6.80e-53 |
|
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: 196.48 E-value: 6.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1080 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISY- 1158
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYy 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1159 ---VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTtqlplLSHFA-ETVEGLTTIRAFRYEARFQQKLLEYTDSNN 1234
Cdd:TIGR02203 153 swqLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQ-----VTTVAeETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1235 IASLFLTAANRWLEVRMEYIG--ACVVLIAAATSISNSlhRELSAG-LVGLGLTYALMVSNylnwmVRNLADMEIQ---- 1307
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIAslALAVVLFIALFQAQA--GSLTAGdFTAFITAMIALIRP-----LKSLTNVNAPmqrg 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1308 LGAVKRIHTLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1387
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1388 SLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkCSDSTLWEALEIAQLKLVVK 1464
Cdd:TIGR02203 375 VNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTEQ-ADRAEIERALAAAYAQDFVD 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1465 ALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILS 1544
Cdd:TIGR02203 454 KLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK 533
|
490 500 510
....*....|....*....|....*....|.
gi 1274095655 1545 ADLVMVLKRGAILEFDKPEKLLSQkDSVFAS 1575
Cdd:TIGR02203 534 ADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1344-1554 |
8.50e-50 |
|
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: 174.11 E-value: 8.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPVLFSGTIRFNLdpekkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFI 1503
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 1504 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRG 1554
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
311-608 |
1.39e-49 |
|
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: 178.84 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 311 LLGFAGPLCIFGIVDHLgkENHVFQPKTQ--------FLGVyFVSSQeflgnayvlavllflalllqrtFLQASYYVAIE 382
Cdd:cd18596 11 VLSFAPPFFLNRLLRYL--EDPGEDATVRpwvwvlllFLGP-LLSSL----------------------LDQQYLWIGRR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 383 TGINLRGAIQTKIYNKIMHL-----------------STSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQI 445
Cdd:cd18596 66 LSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 446 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMT 525
Cdd:cd18596 146 VIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 526 RRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKEsDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALV 605
Cdd:cd18596 226 REEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQ-ELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKV 304
|
...
gi 1274095655 606 SVQ 608
Cdd:cd18596 305 SLD 307
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
690-920 |
1.25e-46 |
|
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: 177.64 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNperetaADSDARSRGpV 769
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN------GVDLSD------LDPASWRRQ-I 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 848
Cdd:COG4988 414 AWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 849 VVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:COG4988 494 LLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1064-1569 |
4.86e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 176.45 E-value: 4.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1064 AMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1143
Cdd:PRK10790 68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1144 RSTLLcVSALTVISYVTP--VFLVALL--PLAVVCYFIQKYF------RVASRdLQQLDDTtqlpllshFAETVEGLTTI 1213
Cdd:PRK10790 148 RSAAL-IGAMLVAMFSLDwrMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEVINGMSVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1214 RAFRYEARFQQKLLEYTDSNNIASL-------FLTaanRWLEVRMEYIGACVVLIAAATSisnslhrelSAGLVGLGLTY 1286
Cdd:PRK10790 218 QQFRQQARFGERMGEASRSHYMARMqtlrldgFLL---RPLLSLFSALILCGLLMLFGFS---------ASGTIEVGVLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1287 ALMvsNYLNWMVRNLADMEIQ-------LGAVKRIHTLLKTEAESYegllAPSLIPKNwpdQGKIQIQNLSVRYDSSlKP 1359
Cdd:PRK10790 286 AFI--SYLGRLNEPLIELTTQqsmlqqaVVAGERVFELMDGPRQQY----GNDDRPLQ---SGRIDIDNVSFAYRDD-NL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1360 VLKHVNALIAPGQKIGICGRTGSGKSSfsLAFFRM----VDMFEGRIIIDGIdiAKLPLHTLRSRLSIILQDPVLFSGTI 1435
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyypLTEGEIRLDGRPL--SSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1436 RFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1515
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 1516 ENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 1569
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
372-610 |
7.05e-46 |
|
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: 167.35 E-value: 7.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLStsnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMT 531
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 532 SLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAHVAL--GNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1342-1581 |
7.91e-46 |
|
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: 166.95 E-value: 7.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1342 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMfEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1501
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1502 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRADK 1581
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDR 239
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1344-1575 |
1.41e-45 |
|
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: 164.71 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1501 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFAS 1575
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAE 231
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
305-610 |
2.49e-44 |
|
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: 163.11 E-value: 2.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 305 FRILADLLGFAGPLCIFGIVDHLgkENHVFQPKTQFL--GVYFVSSqeFLGnayvlavllflalllqrTFLQASY-YVAI 381
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFL--EDSSEPLSDGYLyaLGLVLSS--LLG-----------------ALLSSHYnFQMN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 382 ETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFfflCPNL---WAMPVQIIVGVILLYYILGV 458
Cdd:cd18598 64 KVSLKVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 459 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLR---- 534
Cdd:cd18598 139 AFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKgrky 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 535 --AFAVYtsisiFMNTAiPIAAVLITFVGHVsfFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18598 219 ldALCVY-----FWATT-PVLISILTFATYV--LMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1344-1569 |
2.41e-42 |
|
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: 155.47 E-value: 2.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 1501 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 1569
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1023-1294 |
7.40e-42 |
|
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: 155.49 E-value: 7.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1023 HMVLVAIDYWLAKWTDSALVLSPAARNcslsqecalDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLN 1102
Cdd:pfam00664 12 GAISPAFPLVLGRILDVLLPDGDPETQ---------ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1103 RIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFR 1182
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1183 VASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIA 1262
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 1274095655 1263 AATSISNSLHRELSAGLVGLGLTYALMVSNYL 1294
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
692-917 |
1.03e-41 |
|
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: 155.40 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpdsegedpsnperetaadsdaRSRGPVAY 771
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------------------KHSGRISF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVF 851
Cdd:cd03291 103 SSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 852 LDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 917
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1344-1579 |
1.54e-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: 153.08 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 1422
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1423 IILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1499
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1500 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKdSVFASFVRA 1579
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1092-1570 |
1.65e-41 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 164.51 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1092 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVAL 1167
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrltmVTLINL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1168 LPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPLlshfaETVEGLTTIRAF---RYEA-RFQQKLLEYTDSN---NIASLF 1239
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFaaeEGEAsRFKEALEETLQLNkrkALAYAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1240 LTAANRWLE----VRMEYIGACVVLIAaatsisnslhrELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1315
Cdd:TIGR00958 387 YLWTTSVLGmliqVLVLYYGGQLVLTG-----------KVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVF 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1316 TLL-KTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFR 1393
Cdd:TIGR00958 456 EYLdRKPNIPLTGTLAPL------NLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1394 MVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPE-KKCSDSTLWEALEIAQLKLVVKALPGGLDA 1472
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDT 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1473 IITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILSADLVMVLK 1552
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLK 687
|
490
....*....|....*...
gi 1274095655 1553 RGAILEFDKPEKLLSQKD 1570
Cdd:TIGR00958 688 KGSVVEMGTHKQLMEDQG 705
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
445-912 |
3.85e-41 |
|
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: 161.09 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 445 IIVGVILLYYILGVSALI---GAAVIILLAPVqyFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSR 521
Cdd:COG4987 143 ILAAVAFLAFFSPALALVlalGLLLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALAR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 522 VEMTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPS----VAFASLSLFHILVTplflLSSVV 597
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPllalLVLAALALFEALAP----LPAAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 598 RSTVKALVSVQKLSEFLSSAeireeqcaPREPAPQGQAGKYQAVPLKvvnrkrpareevrdllgpLQRLTpsmdgdadnf 677
Cdd:COG4987 297 QHLGRVRAAARRLNELLDAP--------PAVTEPAEPAPAPGGPSLE------------------LEDVS---------- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 678 cvqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdsegedpsnpERET 757
Cdd:COG4987 341 --------FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-------------GVDL 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 758 AADSDARSRGPVAYASQKPWLLNATVEENITFESPfNKQRYKM--VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQ 835
Cdd:COG4987 400 RDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP-DATDEELwaALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 836 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1073-1578 |
8.80e-40 |
|
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: 159.34 E-value: 8.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1073 LGIALCLVTSVTVEWTGLKVAKRLHRSL--------LNRIILAPMRFFETTPLGSILNRFSSDcNTIDQHIPSTLECLSR 1144
Cdd:TIGR03796 198 LGMGLTALLQGVLTWLQLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTAL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1145 STLLCV-SALTVISYVTPVFLVALLPLAV---VCYFIQKYFRVASRDLQQldDTTQLpllshFAETVEGLTTIR------ 1214
Cdd:TIGR03796 277 DAVMLVfYALLMLLYDPVLTLIGIAFAAInvlALQLVSRRRVDANRRLQQ--DAGKL-----TGVAISGLQSIEtlkasg 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1215 ----AFRYEARFQQKLL----EYTDSNNIASL---FLTAAN----------RWLEVRMEyIGACVvliaAATSISNSLHR 1273
Cdd:TIGR03796 350 lesdFFSRWAGYQAKLLnaqqELGVLTQILGVlptLLTSLNsalilvvgglRVMEGQLT-IGMLV----AFQSLMSSFLE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1274 ELSaGLVGLGLTyalmvsnylnwmvrnLADMEiqlGAVKRIHTLLKTEAESYEGLLAP--SLIPKNWPDQGKIQIQNLSV 1351
Cdd:TIGR03796 425 PVN-NLVGFGGT---------------LQELE---GDLNRLDDVLRNPVDPLLEEPEGsaATSEPPRRLSGYVELRNITF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1352 RYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVD----------MFEGRIIidgidiAKLPLHTLRSRL 1421
Cdd:TIGR03796 486 GYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpwsgeiLFDGIPR------EEIPREVLANSV 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFSGTIRFNL---DPekKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRK 1498
Cdd:TIGR03796 556 AMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1499 TSIFIMDEATASIDMATEnilqKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFASF 1576
Cdd:TIGR03796 634 PSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELW-AVGGAYARL 708
|
..
gi 1274095655 1577 VR 1578
Cdd:TIGR03796 709 IR 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
686-905 |
1.02e-39 |
|
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: 145.22 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgedpsnperetAADSDARS 765
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD-----------LDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RgpVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQ 845
Cdd:cd03228 77 N--IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 846 HTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 905
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEA-LRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
686-911 |
2.06e-39 |
|
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: 146.20 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLpDSEGEDPSnperetaadsDARS 765
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT-DIRQLDPA----------DLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RgpVAYASQKPWLLNATVEENITFESPF-NKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 844
Cdd:cd03245 79 N--IGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 845 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 911
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1342-1556 |
5.83e-39 |
|
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: 145.04 E-value: 5.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1342 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRK 1498
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1499 TSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 1556
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
685-912 |
1.51e-38 |
|
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: 144.30 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNslpdseGEDpsnperetAADSD 762
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPRFYDVD--SGRILID------GHD--------VRDYT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 763 ARS-RGPVAYASQKPWLLNATVEENITFESPfNKQRyKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRIS 838
Cdd:cd03251 71 LASlRRQIGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1080-1569 |
7.62e-37 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 148.24 E-value: 7.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1080 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYV 1159
Cdd:PRK11176 84 ISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1160 T---PVFLVALLPL-AVVCYFIQKYFRVASRDLQ----QLDDTTQLPL------LSHFAETVEglttirafryEARFQQK 1225
Cdd:PRK11176 164 SwqlSLILIVIAPIvSIAIRVVSKRFRNISKNMQntmgQVTTSAEQMLkghkevLIFGGQEVE----------TKRFDKV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1226 lleytdSNNI--ASLFLTAANRWLEVRMEYIGA---CVVLIAAATSisnSLHRELSAGlvglglTYALMVSNYLNWM--V 1298
Cdd:PRK11176 234 ------SNRMrqQGMKMVSASSISDPIIQLIASlalAFVLYAASFP---SVMDTLTAG------TITVVFSSMIALMrpL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1299 RNLADMEIQ----LGAVKRIHTLLKTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKI 1374
Cdd:PRK11176 299 KSLTNVNAQfqrgMAACQTLFAILDLEQEKDEGKRVIE------RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1375 GICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPEKKCSDSTLWE 1452
Cdd:PRK11176 373 ALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1453 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 1532
Cdd:PRK11176 453 AARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS 532
|
490 500 510
....*....|....*....|....*....|....*..
gi 1274095655 1533 VTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQK 1569
Cdd:PRK11176 533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
318-610 |
1.27e-36 |
|
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: 140.85 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 318 LCIFGIVDHLGKenhVFQPktQFLG---VYFV-SSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQT 393
Cdd:cd18594 2 LGILLFLEESLK---IVQP--LLLGrlvAYFVpDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 394 KIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPV 473
Cdd:cd18594 77 LIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 474 QYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLR--AFAVYTSISIFMNTAIP 551
Cdd:cd18594 155 QAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRkaAYIRAFNMAFFFFSPTL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 552 IaaVLITFVGHVSFFKESDfsPSVAFASLSLFHILVTPL-FLLSSVVRSTVKALVSVQKL 610
Cdd:cd18594 235 V--SFATFVPYVLTGNTLT--ARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
376-617 |
2.52e-36 |
|
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: 140.05 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 376 SYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQL-MWFFFLcPNLWAMPVQIIVGVILLYY 454
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 455 ILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLR 534
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 535 --AFAVYTSISIFMntaipIAAVLITFVGHVSFF-KESDFSPSVAFASLSLFHilvtplfllssVVRSTVKALV--SVQK 609
Cdd:cd18593 217 rtSFLRALNMGLFF-----VSSKLILFLTFLAYIlLGNILTAERVFVTMALYN-----------AVRLTMTLFFpfAIQF 280
|
....*...
gi 1274095655 610 LSEFLSSA 617
Cdd:cd18593 281 GSELSVSI 288
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1344-1568 |
4.74e-36 |
|
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: 137.23 E-value: 4.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPVLFSGTIRFNL---DPekKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1501 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 1568
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1099-1569 |
8.87e-36 |
|
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: 146.81 E-value: 8.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1099 SLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLeclsRSTLLCVSALTVISYV-----TPVFLVALLPL--- 1170
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTI----LSLFLDMWILVIVGLFlvrqnMLLFLLSLLSIpvy 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1171 AVVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYEA-RFQQ----------KLLEYTDSNNIASLF 1239
Cdd:TIGR01193 309 AVIIILFKRTFNKLNHDAMQ----ANAVLNSSIIEDLNGIETIKSLTSEAeRYSKidsefgdylnKSFKYQKADQGQQAI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1240 LTAANRWLEVRMEYIGACVVLIAAATsisnslhrelsaglVGLGLTYALMVSNYLNwMVRNLADMEIQLGAVK----RIH 1315
Cdd:TIGR01193 385 KAVTKLILNVVILWTGAYLVMRGKLT--------------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvannRLN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1316 TLLKTEAESYEGLLAPSLIPKNwpdqGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV 1395
Cdd:TIGR01193 450 EVYLVDSEFINKKKRTELNNLN----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1396 DMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAI 1473
Cdd:TIGR01193 525 QARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1474 ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILSADLVMVL 1551
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSDKIIVL 681
|
490
....*....|....*...
gi 1274095655 1552 KRGAILEFDKPEKLLSQK 1569
Cdd:TIGR01193 682 DHGKIIEQGSHDELLDRN 699
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
692-912 |
1.67e-35 |
|
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: 135.43 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERETAadsdaRSRgpVAY 771
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID------GIDIRDISRKSL-----RSM--IGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLLNATVEENITFESPFNKQryKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 848
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 849 VVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03254 160 ILILDEATSNIDTE-TEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1146-1551 |
2.97e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 142.81 E-value: 2.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1146 TLLCVSALTVISYVTPVFLVALLPLAVVcYFIQKYFRVASRDLQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQK 1225
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPLIPI-FMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1226 LLEYTDSNniaslfltaANRWLEV-RMEYIGACVVLIAAATSISnslhreLSAGLVGLGLTY----------ALMVSNYL 1294
Cdd:TIGR02857 209 IRRSSEEY---------RERTMRVlRIAFLSSAVLELFATLSVA------LVAVYIGFRLLAgdldlatglfVLLLAPEF 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1295 NWMVRNL-----ADMEIQlGAVKRIHTLLkteaeSYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIA 1369
Cdd:TIGR02857 274 YLPLRQLgaqyhARADGV-AAAEALFAVL-----DAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVP 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1370 PGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkcS 1446
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--S 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1447 DSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTA 1526
Cdd:TIGR02857 425 DAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL 504
|
410 420
....*....|....*....|....*
gi 1274095655 1527 FADRTVVTIAHRVHTILSADLVMVL 1551
Cdd:TIGR02857 505 AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1071-1578 |
7.21e-35 |
|
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: 143.56 E-value: 7.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1071 CSLGIALCLVTSVTVEWT-GLKVAK-------RLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECL 1142
Cdd:TIGR03797 178 IALALLAAAVGAAAFQLAqSLAVLRletrmdaSLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLTT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1143 SRSTLLCVSALTVISYVTP---VFLVALLPLAVVCYFIQKYFRVA-SRDLQQLDDTTQLPLLshfaETVEGLTTIR---- 1214
Cdd:TIGR03797 257 LLSGIFALLNLGLMFYYSWklaLVAVALALVAIAVTLVLGLLQVRkERRLLELSGKISGLTV----QLINGISKLRvaga 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1215 ---AF-RYEARF-QQKLLEYtDSNNIASlFLTAANRWLEVRmeyigACVVLIAAATSIsnslhreLSAGLVGLG--LTYA 1287
Cdd:TIGR03797 333 enrAFaRWAKLFsRQRKLEL-SAQRIEN-LLTVFNAVLPVL-----TSAALFAAAISL-------LGGAGLSLGsfLAFN 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1288 LMVSNYLNWMvRNLADMEIQLGAV----KRIHTLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKH 1363
Cdd:TIGR03797 399 TAFGSFSGAV-TQLSNTLISILAViplwERAKPILEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1364 VNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGID----IAKLPLHTLRSRLSIILQDPVLFSGTIRFNL 1439
Cdd:TIGR03797 472 VSLQIEPGEFVAIVGPSGSGKSTL----LRLLLGFETPESGSVFYdgqdLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1440 dpekkCSDSTL-----WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDma 1514
Cdd:TIGR03797 548 -----AGGAPLtldeaWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD-- 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 1515 teNILQKVVMTAFA--DRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLsQKDSVFASFVR 1578
Cdd:TIGR03797 621 --NRTQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM-AREGLFAQLAR 683
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1292-1558 |
8.15e-35 |
|
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: 142.65 E-value: 8.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1292 NYLNWMVR----NLADMEiqlgavkRIHTLLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSlKPVLKHVNAL 1367
Cdd:COG5265 313 NFLGFVYReirqALADME-------RMFDLLDQPPEVADAPDAPPLVVG----GGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1368 IAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkk 1444
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPD-- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1445 CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM 1524
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270
....*....|....*....|....*....|....
gi 1274095655 1525 TAFADRTVVTIAHRVHTILSADLVMVLKRGAILE 1558
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
690-912 |
6.95e-34 |
|
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: 131.12 E-value: 6.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSlllaTLGEMQR----VSGAVFWNslpdsegedpsnperetaaDSDARS 765
Cdd:cd03249 14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfydpTSGEILLD-------------------GVDIRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 ------RGPVAYASQKPWLLNATVEENITFESPFNKQryKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQR 836
Cdd:cd03249 70 lnlrwlRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 837 ISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
449-912 |
1.12e-33 |
|
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: 138.70 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 449 VILLYYILGVSAligaaVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTN----EMLRGIKLLKLYAWE----NIFCS 520
Cdd:TIGR02203 147 IVLLYYSWQLTL-----IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaeETLQGYRVVKLFGGQayetRRFDA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 521 RVEMTRRKEMTSLRAFAVYTSISIFmntaipIAAVLITFVGHVSFFKESDFSPSVA-FASLSLFHILV-TPLFLLSSVVR 598
Cdd:TIGR02203 222 VSNRNRRLAMKMTSAGSISSPITQL------IASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALiRPLKSLTNVNA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 599 STVKALVSVQKLSEFLSSAeireeqcaprepaPQGQAGKyqavplKVVNRKRpAREEVRDLLgplqrltpsmdgdadnfc 678
Cdd:TIGR02203 296 PMQRGLAAAESLFTLLDSP-------------PEKDTGT------RAIERAR-GDVEFRNVT------------------ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 679 vqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNSLPdsegedpsnpere 756
Cdd:TIGR02203 338 -------FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYEPD--SGQILLDGHD------------- 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 757 tAADSDARS-RGPVAYASQKPWLLNATVEENITFESP--FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQ 833
Cdd:TIGR02203 396 -LADYTLASlRRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQ 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 834 RQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIVERGT 550
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
379-912 |
6.73e-33 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 135.94 E-value: 6.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 379 VAIETGINLRGAIQTKIYNKIMhlsTSNLSMGEMTAGQICNlvaiDTNQLMWF--------FFLCPnlWaMPVQIIVgVI 450
Cdd:TIGR01842 69 VLVRIGEKLDGALNQPIFAASF---SATLRRGSGDGLQALR----DLDQLRQFltgpglfaFFDAP--W-MPIYLLV-CF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 451 LLYYILGVSALIGAAVIILLAPV-QYFVATKLSQAQrstlEYSNERLKQTNEMLRGIKLLK-LYAWENIfcsrVEMTRRK 528
Cdd:TIGR01842 138 LLHPWIGILALGGAVVLVGLALLnNRATKKPLKEAT----EASIRANNLADSALRNAEVIEaMGMMGNL----TKRWGRF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 529 EMTSLRAFAVYTSISIFMNTAIPIAAV----LITFVG-HVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 603
Cdd:TIGR01842 210 HSKYLSAQSAASDRAGMLSNLSKYFRIvlqsLVLGLGaYLAI--DGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 604 LVSVQKLSEFLssAEIREEQCAPREPAPQGQagkyqavpLKVvnrkrparEEVrDLLGPLQRLtpsmdgdadnfcvqiig 683
Cdd:TIGR01842 288 RQAYKRLNELL--ANYPSRDPAMPLPEPEGH--------LSV--------ENV-TIVPPGGKK----------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 684 gfftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpDSEGEDPSNPERETAADSda 763
Cdd:TIGR01842 332 ----------PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV------RLDGADLKQWDRETFGKH-- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 764 rsrgpVAYASQKPWLLNATVEENIT-FESPFNKQRykmVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISV 839
Cdd:TIGR01842 394 -----IGYLPQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILRLPDGYDTVIGPGGATLSGGQRQRIAL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 840 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
690-912 |
9.84e-33 |
|
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: 127.73 E-value: 9.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNslpdseGEDPsnpeRETAADSDARSRG 767
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIlrLLFRFYDVS--SGSILID------GQDI----REVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVAyasQKPWLLNATVEENITFESP--FNKQrykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 842
Cdd:cd03253 79 VVP---QDTVLFNDTIGYNIRYGRPdaTDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 843 LYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03253 152 ILKNPPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGT 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
694-912 |
1.03e-32 |
|
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: 135.65 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEREtaadsdarSRGP-VAYA 772
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD------GADLSQWDRE--------ELGRhIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 773 SQKPWLLNATVEENItfeSPFNKQRYKMVIEACSLqpdIDI------LPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:COG4618 412 PQDVELFDGTIAENI---ARFGDADPEKVVAAAKL---AGVhemilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 847 TNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAA--IRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
299-590 |
1.46e-32 |
|
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: 128.53 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 299 LVLSSTFRILADLLGFAGPLCIFGIVDHLGKEN-HVFQPKTQFLGVYFVssqeflgnayvlavllflALLLQRTFLQASY 377
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGdPETQALNVYSLALLL------------------LGLAQFILSFLQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 378 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILG 457
Cdd:pfam00664 63 YLLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 458 VS-ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAF 536
Cdd:pfam00664 141 WKlTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKK 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 537 AVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPL 590
Cdd:pfam00664 221 AVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
690-902 |
3.16e-32 |
|
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: 133.57 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgedpsnperetaADSDARsRGPV 769
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD------------ADADSW-RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENITFESPFNKQ-RYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 848
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 849 VVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAM 902
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEA-LRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1341-1579 |
4.92e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 130.85 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1341 QGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSR 1420
Cdd:PRK13657 332 KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1421 LSIILQDPVLFSGTIRFNLDPEKK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1499
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1500 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILE---FDKpeklLSQKDSVFASF 1576
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAAL 566
|
...
gi 1274095655 1577 VRA 1579
Cdd:PRK13657 567 LRA 569
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1062-1313 |
2.64e-30 |
|
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: 122.32 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1062 VYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC 1141
Cdd:cd18559 39 VYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1142 LSRSTLLCVSALTVISYVTPVFLVAlLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEAR 1221
Cdd:cd18559 119 WMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1222 FQQKLLEYTDsNNIASLFLTAANRWLEVRMEYIGACVVLIAA-ATSISnslhRELSAGLVGLGLTYALMVSNYLNWMVRN 1300
Cdd:cd18559 198 FIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASfFAYVS----RHSLAGLVALKVFYSLALTTYLNWPLNM 272
|
250
....*....|...
gi 1274095655 1301 LADMEIQLGAVKR 1313
Cdd:cd18559 273 SPEVITNIVAAEV 285
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1095-1538 |
3.63e-30 |
|
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: 127.09 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1095 RLHRSLLnRIILAPMRFFETtplGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVC 1174
Cdd:TIGR02868 91 RVYERLA-RQALAGRRRLRR---GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1175 YFIQKYF-----RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEytdsnniASLFLTAANRwLEV 1249
Cdd:TIGR02868 167 GFVAPLVslraaRAAEQALARLRGE----LAAQLTDALDGAAELVASGALPAALAQVEE-------ADRELTRAER-RAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1250 RMEYIGACVVLIAAATSISNSLhreLSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAESYEGLL 1329
Cdd:TIGR02868 235 AATALGAALTLLAAGLAVLGAL---WAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1330 APSLI--------PKNWPDQG-KIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEG 1400
Cdd:TIGR02868 312 DAAGPvaegsapaAGAVGLGKpTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1401 RIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEG 1477
Cdd:TIGR02868 391 EVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRPD--ATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 1478 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1538
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
686-906 |
3.89e-30 |
|
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: 119.49 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdsegedpsnpERETAADSDARS 765
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-------------GKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 835
Cdd:cd03225 74 RRKVGLVFQNPddQFFGPTVEEEVAF-GLENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 836 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 906
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
686-910 |
8.69e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.81 E-value: 8.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEREtaadsdars 765
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD------GKPVTGPGPD--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 rgpVAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGG 832
Cdd:COG1116 82 ---RGVVFQEpallPWL---TVLDNVALglelrgVPK--AERRERArelLELVGLAGFEDAYPH-----------QLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 833 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAMKD--GTI 907
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSArpGRI 219
|
...
gi 1274095655 908 QRE 910
Cdd:COG1116 220 VEE 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
691-920 |
9.70e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 9.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPsnperetaadsdARSRGPVA 770
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF------GKPP------------RRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRISV 839
Cdd:COG1121 79 YVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADR-PIGE----LSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 840 ARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIqREGTLKDFQR 918
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVReYFDRVLLLNRGLV-AHGPPEEVLT 227
|
..
gi 1274095655 919 SE 920
Cdd:COG1121 228 PE 229
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1088-1314 |
1.64e-29 |
|
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: 121.06 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1088 TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVAL 1167
Cdd:cd18600 97 TLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLAT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1168 LPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFR----YEARFQQKLLEYTdsnniASLFL-TA 1242
Cdd:cd18600 177 VPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHT-----ANWFLyLS 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 1243 ANRWLEVRMEYIgaCVVLIAAATSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1314
Cdd:cd18600 252 TLRWFQMRIEMI--FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
686-920 |
1.81e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 118.36 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSslllaTLGEM-QRV----SGAVFwnslpdSEGEDpsnpereTAAD 760
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKS-----TLTKLiQRFyvpeNGRVL------VDGHD-------LALA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 761 SDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRykMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRI 837
Cdd:cd03252 70 DPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 838 SVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 917
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
...
gi 1274095655 918 RSE 920
Cdd:cd03252 225 AEN 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
690-916 |
4.42e-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: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERetaadSDARSRgpV 769
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD------GKDITKKNL-----RELRRK--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPW--LLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 839
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAF-GPENlglpreeiRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 840 ARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTIQREGTLKDF 916
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
687-912 |
5.76e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 117.45 E-value: 5.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 687 TWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSN-PERETAadsdaRS 765
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD------GRDLASlSRRELA-----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 rgpVAYASQK---PWLLnaTVEENI--------TFESPFNKQRYKMVIEACslqpdidilphgDQTQIG---ERGIN-LS 830
Cdd:COG1120 77 ---IAYVPQEppaPFGL--TVRELValgryphlGLFGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 831 GGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL-QYLPHADWIIAMKDG 905
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKDG 214
|
....*..
gi 1274095655 906 TIQREGT 912
Cdd:COG1120 215 RIVAQGP 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1164-1568 |
8.98e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 123.67 E-value: 8.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1164 LVALLPLAVVCYFIQKY-------FRVASRDLQQLDDTTQlpllshfaetvEGLTTIR---AFRyearfqqklLEYTDSN 1233
Cdd:PRK10789 141 LLALLPMPVMAIMIKRYgdqlherFKLAQAAFSSLNDRTQ-----------ESLTSIRmikAFG---------LEDRQSA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1234 NIASLFLTAANRWLEV-RMEYIGACVVLIAAATS------------ISNSLHR-ELSAGLVGLGLTYALMVSnyLNWMVr 1299
Cdd:PRK10789 201 LFAADAEDTGKKNMRVaRIDARFDPTIYIAIGMAnllaigggswmvVNGSLTLgQLTSFVMYLGLMIWPMLA--LAWMF- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1300 NLadMEIQLGAVKRIHTLLKTEAESYEGLLApslIPknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGR 1379
Cdd:PRK10789 278 NI--VERGSAAYSRIRAMLAEAPVVKDGSEP---VP---EGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1380 TGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpEKKCSDSTLWEALEIAQL 1459
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI--ALGRPDATQQEIEHVARL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1460 KLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAfADRTVVTI 1535
Cdd:PRK10789 428 ASVhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHNLRQWG-EGRTVIIS 506
|
410 420 430
....*....|....*....|....*....|...
gi 1274095655 1536 AHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 1568
Cdd:PRK10789 507 AHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1344-1554 |
7.10e-28 |
|
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: 112.56 E-value: 7.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDS---SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAffrmvdmfegriiidgiDIAKLPLH----T 1416
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSA-----------------LLGELEKLsgsvS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1417 LRSRLSIILQDPVLFSGTIRFN------LDPEKkcsdstLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFC 1490
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENilfgkpFDEER------YEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 1491 LARAFVRKTSIFIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILSADLVMVLKRG 1554
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
690-912 |
7.14e-28 |
|
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: 112.97 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSnpereTAADSDARSRgpV 769
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID------GVDIS-----KIGLHDLRSR--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENItfeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 847 TNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03244 158 SKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
305-610 |
7.15e-28 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 115.39 E-value: 7.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 305 FRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVS--SQEFLGNAYvlavllflalllqrtflqasYYVAIE 382
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALaiLQGITVFQY--------------------SMAVSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 383 TGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALI 462
Cdd:cd18559 65 GGIFASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 463 GAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTSI 542
Cdd:cd18559 143 GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 543 SIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18559 223 AVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1327-1556 |
9.29e-28 |
|
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: 112.95 E-value: 9.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1327 GLLAPSLIpknwpdQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMvdmFEGRIIID 1405
Cdd:cd03248 1 GSLAPDHL------KGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF---YQPQGGQV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1406 GIDIAKLPLHT---LRSRLSIILQDPVLFSGTIRFNLD-PEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENF 1481
Cdd:cd03248 72 LLDGKPISQYEhkyLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1482 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 1556
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
381-934 |
1.23e-27 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 120.83 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 381 IETGINlrGAIQTKIYNKIMHL--------STSNLSMGEMTAGQICNLVAIDT-NQLMWFFFLCPNLWampvqiivgviL 451
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLG-----------L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAWENIFCSRVE 523
Cdd:TIGR03797 270 MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 524 MTRRKEM------TSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFkesdfspsVAFASLSlfhilvtplfllsSVV 597
Cdd:TIGR03797 350 LELSAQRienlltVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFN--------TAFGSFS-------------GAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 598 RSTVKALVSVqklseflssaeireeqcaprepapqgqagkYQAVPLkvVNRKRP---AREEVRDLLGPLQRLTPSMDgdA 674
Cdd:TIGR03797 409 TQLSNTLISI------------------------------LAVIPL--WERAKPileALPEVDEAKTDPGKLSGAIE--V 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 675 DNFCvqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPSnpe 754
Cdd:TIGR03797 455 DRVT-------FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFY------DGQDLA--- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 755 retAADSDA--RSRGPVAYASQkpwLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGG 832
Cdd:TIGR03797 519 ---GLDVQAvrRQLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGG 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 833 QRQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGT 667
|
570 580
....*....|....*....|..
gi 1274095655 913 LKDFQRSECQLFEhwktLMNRQ 934
Cdd:TIGR03797 668 YDELMAREGLFAQ----LARRQ 685
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
689-912 |
1.65e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 119.95 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ-----RVSGavfwnslpdsegedpsnpeRETAADSDA 763
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKING-------------------IELRELDPE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 764 RSRGPVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 842
Cdd:PRK11174 420 SWRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 843 LYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQA--LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
696-910 |
2.15e-27 |
|
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: 111.79 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEREtaadsdarsrgpVAYASQK 775
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD------GEPVTGPGPD------------RGYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 ----PWLlnaTVEENITFesPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 842
Cdd:cd03293 82 dallPWL---TVLDNVAL--GLElqgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 843 LYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM--KDGTIQRE 910
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQ-LQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
696-911 |
8.27e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 108.68 E-value: 8.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERETAADSdarsrgpVAYASQk 775
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD------GKDLASLSPKELARK-------IAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 pwllnatveenitfespfnkqrykmVIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQRISVARALYQHTNVVFLDD 854
Cdd:cd03214 81 -------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 855 PFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 911
Cdd:cd03214 124 PTSHLDIA-----HQIELLELLRRLARergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
694-958 |
1.02e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 117.12 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSegedpsnpereTAADSDARSRgpVAYAS 773
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-----------KLQLDSWRSR--LAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFL 852
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 853 DDPFSALDVHlSDHlmqaGILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKdfqrsecQLFEH--WK 928
Cdd:PRK10789 476 DDALSAVDGR-TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD-------QLAQQsgWY 543
|
250 260 270
....*....|....*....|....*....|
gi 1274095655 929 TLMNRQdQELEKETvmeRKAPEPSQGLPRA 958
Cdd:PRK10789 544 RDMYRY-QQLEAAL---DDAPEIREEAVDA 569
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
686-920 |
1.10e-26 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 117.92 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQRvsGAVFWNSLpDSEGEDPSNPEREtaadsda 763
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQH--GQVLVDGV-DLAIADPAWLRRQ------- 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 764 rsrgpVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRISVA 840
Cdd:TIGR01846 533 -----MGVVLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIA 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
693-907 |
1.59e-26 |
|
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: 109.12 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLATLGEMQRV-SGAVFwnslpdSEGEDPSN-PERETAADsdarSRGPVA 770
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKST-LLNILGGLDRPtSGEVR------VDGTDISKlSEKELAAF----RRRHIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPWLL-NATVEENI----TFESPFNKQRYKMVIEACslqpdidilphgDQTQIGERgIN-----LSGGQRQRISVA 840
Cdd:cd03255 86 FVFQSFNLLpDLTALENVelplLLAGVPKKERRERAEELL------------ERVGLGDR-LNhypseLSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
686-907 |
2.23e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.36 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgedpSNPEretaadsDARS 765
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA----MPPP-------EWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RgpVAYASQKPWLLNATVEENITF-----ESPFNKQRYKMVIEACSLQPDIdiLphgdQTQIGErginLSGGQRQRISVA 840
Cdd:COG4619 75 Q--VAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI--L----DKPVER----LSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEEL-LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1309-1579 |
3.09e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 115.71 E-value: 3.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1309 GAVKRIHTLLKTEAESYEGllAPSLIPKNWPDQgkIQIQNLSVR-YDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1387
Cdd:PRK11174 319 GAAESLVTFLETPLAHPQQ--GEKELASNDPVT--IEAEDLEILsPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1388 ------------SLaffrMVDMFEGriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWE 1452
Cdd:PRK11174 393 lnallgflpyqgSL----KINGIEL---------RELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQ 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1453 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 1532
Cdd:PRK11174 458 ALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT 537
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1533 VTIAHRVHTILSADLVMVLKRGAILE---FDKpeklLSQKDSVFASFVRA 1579
Cdd:PRK11174 538 LMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
696-919 |
3.60e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.61 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPsnpereTAADSDARSRgpVAYASQK 775
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL------GEDV------ARDPAEVRRR--IGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWL-LNATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARALYQHT 847
Cdd:COG1131 82 PALyPDLTVRENLRFfarlyglPRKEARERIDELLELFGLTDAAD-------RKVG----TLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 848 NVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKDFQRS 919
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
686-911 |
8.81e-26 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 106.83 E-value: 8.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEREtaadsdars 765
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID------GRDVTGVPPE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RGPVAYASQK----PWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQR 834
Cdd:cd03259 71 RRNIGMVFQDyalfPHL---TVAENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 835 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 911
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
691-903 |
1.55e-25 |
|
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: 106.08 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDsegedpsnperetaadsdARSRGPVA 770
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------------------EKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRISV 839
Cdd:cd03235 72 YVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALER---VGLSELADR-QIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 840 ARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILEL---LRDDKRTVVLVTHKL-QYLPHADWIIAMK 903
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPK-----TQEDIYELlreLRREGMTILVVTHDLgLVLEYFDRVLLLN 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1344-1558 |
2.41e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 104.32 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPlHTLRSRLSI 1423
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPVLFSGTIRFNLdpekkcsdstlwealeiaqlklvvkalpggldaiitegGENFSQGQRQLFCLARAFVRKTSIFI 1503
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1504 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILE 1558
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
389-890 |
2.42e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 112.45 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 389 GAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVA--IDTNQLMWFFFLCPNLWAMPVQIIV--GVILLYYILGVSALIGA 464
Cdd:TIGR02868 86 GALRVRVYERLARQALA--GRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVGAAAvaAIAVLSVPAALILAAGL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 465 AVIILLAPvqyFVATKLSQAQRSTLEYS-NERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTSIS 543
Cdd:TIGR02868 164 LLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 544 IFMNTAIPIAAVLITFVGHVSFFKESDFSPS----VAFASLSLFHilvtPLFLLSSVVRSTVKALVSVQKLSEFLSSAEI 619
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADGRLAPVtlavLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDAAGP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 620 REEQCAPREpapqgqagkyQAVPLKVVNRkrpareEVRDLLgplqrltpsmdgdadnfcvqiiggfFTWtPDGIPTLSNI 699
Cdd:TIGR02868 317 VAEGSAPAA----------GAVGLGKPTL------ELRDLS-------------------------AGY-PGAPPVLDGV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 700 TIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavfwnSLPDSEGEDPSNPERETAADSDARSRgPVAYASQKPWLL 779
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAG------------LLDPLQGEVTLDGVPVSSLDQDEVRR-RVSVCAQDAHLF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 780 NATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSA 858
Cdd:TIGR02868 422 DTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
490 500 510
....*....|....*....|....*....|....
gi 1274095655 859 LDVHLSDHLmqagiLELLRD--DKRTVVLVTHKL 890
Cdd:TIGR02868 502 LDAETADEL-----LEDLLAalSGRTVVLITHHL 530
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
696-920 |
4.72e-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: 105.28 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPSnperETAADSDARSRGPVAYASQK 775
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI------DGEDIS----GLSEAELYRLRRRMGMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 844
Cdd:cd03261 86 GALFDSlTVFENVAF--PLRehtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 845 QHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASG-----VIDDLIRSLKKelglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
.
gi 1274095655 920 E 920
Cdd:cd03261 228 D 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1344-1556 |
9.00e-25 |
|
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: 102.68 E-value: 9.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdmfegriiidgidiAKLPLHTLRsrlsi 1423
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTL----------------------ARLILGLLR----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ilqdPVlfSGTIRfnLDpekkCSDSTLWEALEIAQLklvVKALPGglDAIITEG--GEN-FSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03246 54 ----PT--SGRVR--LD----GADISQWDPNELGDH---VGYLPQ--DDELFSGsiAENiLSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1501 IFIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 1556
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
686-915 |
9.76e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 9.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllATLgeMQRvsgavFWNSlpdSEGE---DPSNPERETAADSd 762
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI--ANL--LTR-----FYDI---DEGEillDGHDLRDYTLASL- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 763 arsRGPVAYASQKPWLLNATVEENITFESpfnKQRY--KMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRI 837
Cdd:PRK11176 416 ---RNQVALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 838 SVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1339-1570 |
1.18e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.68 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1339 PDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSS-FSLaFFRMVDMFEGRIIIDGIDIAKLPLHTL 1417
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTlLQL-LTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1418 RSRLSIILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQL-KLVvkALPGGLDAIITEGGENFSQGQRQLFCLAR 1493
Cdd:PRK11160 413 RQAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLeKLL--EDDKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1494 AFVRKTSIFIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 1570
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
693-911 |
1.30e-24 |
|
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: 104.12 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPSNPEREtaadsDARSRGP-VAY 771
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF------DGKDLLKLSRR-----LRKIRRKeIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVI--EACSLQPDIDIL---PHGdqtqigerginLSGGQRQRIS 838
Cdd:cd03257 87 VFQDPMSsLNPrmTIGEQIAeplriHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKDGTIQREG 911
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKLQEelglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
693-910 |
3.15e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.81 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWNslpdseGEDPSnperetAADSDARSR--- 766
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLniLGGL---DRPtSGEVLID------GQDIS------SLSERELARlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 767 ---GpvaYASQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 835
Cdd:COG1136 86 rhiG---FVFQFFNLLpELTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 836 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 910
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
692-906 |
3.20e-24 |
|
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: 100.40 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERETAadsdarsRGPVAY 771
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID------GKDIAKLPLEEL-------RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVVF 851
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 852 LDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 906
Cdd:cd00267 104 LDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
685-912 |
3.24e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.84 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEREtaadSDAR 764
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD------GKDLTKLSRR----SLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 765 SRGPVAYASQKPWL-LNA--TVEENITfESPFN------KQRYKMV---IEACSLQPD-IDILPHGdqtqigerginLSG 831
Cdd:COG1123 340 LRRRVQMVFQDPYSsLNPrmTVGDIIA-EPLRLhgllsrAERRERVaelLERVGLPPDlADRYPHE-----------LSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 832 GQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKD 904
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvRYI--ADRVAVMYD 480
|
....*...
gi 1274095655 905 GTIQREGT 912
Cdd:COG1123 481 GRIVEDGP 488
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1312-1579 |
3.60e-24 |
|
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: 109.07 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1312 KRIHTLLKTEAESYEGLLAPslipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSfsLAf 1391
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLP-------RPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKST--LA- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1392 fRM----------------VDMFEGRIIIDGIDIAKLPlhtlrsrlsiilQDPVLFSGTI-----RF-NLDPEKkcsdst 1449
Cdd:COG4618 376 -RLlvgvwpptagsvrldgADLSQWDREELGRHIGYLP------------QDVELFDGTIaeniaRFgDADPEK------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1450 lweALEIAQL----KLVVKaLPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT 1525
Cdd:COG4618 437 ---VVAAAKLagvhEMILR-LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA 512
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1526 AFAD-RTVVTIAHRVHTILSADLVMVLKRGAILEFDKpekllsqKDSVFASFVRA 1579
Cdd:COG4618 513 LKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP-------RDEVLARLARP 560
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
445-912 |
6.50e-24 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 108.25 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 445 IIVGVILLYYILGV--SALIGAAVIILLAPVqYFVATKLSQAQRStleySNERLKQTN----EMLRGIKLLKLYAWENI- 517
Cdd:TIGR02204 145 MCIGGLIMMFITSPklTSLVLLAVPLVLLPI-LLFGRRVRKLSRE----SQDRIADAGsyagETLGAIRTVQAFGHEDAe 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 518 ---FCSRVEMTRRKEMTSLRAFAVYTSISIFMNTAipiAAVLITFVGhVSFFKESDFSPSV--AFASLSLFhiLVTPLFL 592
Cdd:TIGR02204 220 rsrFGGAVEKAYEAARQRIRTRALLTAIVIVLVFG---AIVGVLWVG-AHDVIAGKMSAGTlgQFVFYAVM--VAGSIGT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 593 LSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPREPAPQGQAgkyqAVPLKVVNRKRPAREEVrdllgplqrltpsmdg 672
Cdd:TIGR02204 294 LSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRG----EIEFEQVNFAYPARPDQ---------------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 673 dadnfcvqiiggfftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGeDPSn 752
Cdd:TIGR02204 354 ---------------------PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL-DPA- 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 753 peretaadsDARSRgpVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEAC-SLQPD--IDILPHGDQTQIGERGINL 829
Cdd:TIGR02204 411 ---------ELRAR--MALVPQDPVLFAASVMENIRYGRP--DATDEEVEAAArAAHAHefISALPEGYDTYLGERGVTL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 830 SGGQRQRISVARALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQR 909
Cdd:TIGR02204 478 SGGQRQRIAIARAILKDAPILLLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVA 554
|
...
gi 1274095655 910 EGT 912
Cdd:TIGR02204 555 QGT 557
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
690-919 |
8.81e-24 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 101.99 E-value: 8.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgEDPSnperetaadsdaRSRGPV 769
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPV------------ELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLL-NATVEENIT-------FESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRISV 839
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIAlvpkllkWPKEKIRERADELLALVGLDPAefADRYPH-----------ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 840 ARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQR 918
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
.
gi 1274095655 919 S 919
Cdd:cd03295 226 S 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
692-915 |
1.56e-23 |
|
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: 107.90 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERETAadsdarsRGPVAY 771
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN------GFSLKDIDRHTL-------RQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLLNATVEENITFESPFNKQRyKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 848
Cdd:TIGR01193 553 LPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 849 VVFLDDPFSALDVhlsdhLMQAGILE-LLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:TIGR01193 632 VLILDESTSNLDT-----ITEKKIVNnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
686-911 |
3.05e-23 |
|
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: 98.54 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDpsnperetaADSDArs 765
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK---------ALSSL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 rgpVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQ 845
Cdd:cd03247 77 ---ISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 846 HTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 911
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSL-IFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
686-919 |
4.35e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 100.26 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERetaadsdARS 765
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD------GRPVTRRRR-------KAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RGPVAYASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVIEACSLQPDI-DILPHgdqtQigerginLSGGQRQR 836
Cdd:COG1124 78 RRRVQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYPH----Q-------LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 837 ISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 911
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
....*...
gi 1274095655 912 TLKDFQRS 919
Cdd:COG1124 222 TVADLLAG 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
696-857 |
7.96e-23 |
|
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: 96.18 E-value: 7.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEREtaadsdaRSRGPVAYASQK 775
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD------GQDLTDDERK-------SLRKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLLNA-TVEENITFESPFnKQRYKMVIEAcslQPDIDI----LPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVV 850
Cdd:pfam00005 68 PQLFPRlTVRENLRLGLLL-KGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 1274095655 851 FLDDPFS 857
Cdd:pfam00005 144 LLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
694-907 |
8.00e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.90 E-value: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsLPDseGEDPSnperetAADSDARsRGPVAYAS 773
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV----RLD--GADIS------QWDPNEL-GDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVVFLD 853
Cdd:cd03246 83 QDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 854 DPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03246 122 EPNSHLDVEGERALNQA--IAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
690-917 |
8.15e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 99.18 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdsegeDPSNPERETAADSDARSRgpV 769
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID--------GTDINKLKGKALRQLRRQ--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLN-ATVEENI---------TFESPFN------KQRykmvieACSLQPDIDILPHGDQtqigeRGINLSGGQ 833
Cdd:cd03256 81 GMIFQQFNLIErLSVLENVlsgrlgrrsTWRSLFGlfpkeeKQR------ALAALERVGLLDKAYQ-----RADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 834 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGT 912
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL-LKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGP 228
|
....*
gi 1274095655 913 LKDFQ 917
Cdd:cd03256 229 PAELT 233
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
694-920 |
1.73e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 98.62 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNslpdseGEDPSNperetaADSDARSRgPVAY 771
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLsmISRLLPPD--SGEVLVD------GLDVAT------TPSRELAK-RLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWL-LNATVEENITF-ESPFNKQR-----YKMVIEAcslqpdIDILphgDQTQIGERGIN-LSGGQRQRISVARAL 843
Cdd:COG4604 80 LRQENHInSRLTVRELVAFgRFPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDK-RTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
690-907 |
3.33e-22 |
|
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: 97.16 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDpsnperetaadsdARSRGPV 769
Cdd:cd03248 25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH-------------KYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENITFESPfnKQRYKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 847 TNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03248 169 PQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
692-906 |
5.30e-22 |
|
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: 94.95 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERETAAdsdarSRGPVAY 771
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID------GEDLTDLEDELPP-----LRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLL-NATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVV 850
Cdd:cd03229 81 VFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 851 FLDDPFSALDVhlsdhLMQAGILELLRD----DKRTVVLVTHKLQYLPH-ADWIIAMKDGT 906
Cdd:cd03229 123 LLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
691-922 |
1.01e-21 |
|
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: 96.08 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEREtaadsdARSRgpVA 770
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID------GEDVRKEPRE------ARRQ--IG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPWL-LNATVEENITFESPFN-------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARA 842
Cdd:COG4555 78 VLPDERGLyDRLTVRENIRYFAELYglfdeelKKRIEELIELLGLEEFLDRRVGE-----------LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 843 LYQHTNVVFLDDPFSALDVhLSDHLMQaGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSEC 921
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDV-MARRLLR-EILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
.
gi 1274095655 922 Q 922
Cdd:COG4555 225 E 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
686-923 |
1.80e-21 |
|
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: 100.36 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQRVSGAVFWNslpdseGEDPsnpereTAADSD 762
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLD------GRDL------LELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 763 ARSRGpVAYASQKPW--LLNATVEENITfESPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGG 832
Cdd:COG1123 80 LRGRR-IGMVFQDPMtqLNPVTVGDQIA-EALENlglsraeaRARVLELLEAVGLERRLDRYPH-----------QLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 833 QRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQY-LPHADWIIAMKDGTI 907
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTT-----QAEILDLLRELQRergtTVLLITHDLGVvAEIADRVVVMDDGRI 221
|
250
....*....|....*.
gi 1274095655 908 QREGTLKDFQRSECQL 923
Cdd:COG1123 222 VEDGPPEEILAAPQAL 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1344-1568 |
5.14e-21 |
|
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: 98.82 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD---MFEGRIIIDGIDIAKLPLHTLRSR 1420
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1421 LSIILQDP--VLFSGTIRFNLD--PEKKCSDSTLWEALEIAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFV 1496
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 1497 RKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQ 1568
Cdd:COG1123 159 LDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1345-1554 |
9.97e-21 |
|
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: 90.38 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1345 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSII 1424
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1425 LQdpvlfsgtirfnldpekkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFIM 1504
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 1505 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTI-LSADLVMVLKRG 1554
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1344-1570 |
1.70e-20 |
|
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: 92.01 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAF------------FRMVDMfegriiidgidiAK 1411
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsgevlVDGKDI------------TK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1412 LPLHTLRSRLSIILQDPV--LFSGTIR---------FNLDPEkkcsdstlwEALEIAQ--LKLVvkalpgGLDAIITEGG 1478
Cdd:COG1122 68 KNLRELRRKVGLVFQNPDdqLFAPTVEedvafgpenLGLPRE---------EIRERVEeaLELV------GLEHLADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAI 1556
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
250
....*....|....
gi 1274095655 1557 LEFDKPEKLLSQKD 1570
Cdd:COG1122 213 VADGTPREVFSDYE 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
811-1581 |
2.47e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.56 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 811 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL 890
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 891 QYLPHADWIIAM----------------------------------------KDGTIQREGTLKDFQRSECQLFEH---- 926
Cdd:PTZ00265 641 STIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnNNNKINNAGSYIIEQGTHDALMKNkngi 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 927 WKTLMNRQ--------DQELEKETVMERKAPEPSQGLPRAmSSRDGLLLDEDEEEEEAAESEEDDNLSSVLHQRAKIPW- 997
Cdd:PTZ00265 721 YYTMINNQkvsskkssNNDNDKDSDMKSSAYKDSERGYDP-DEMNGNSKHENESASNKKSCKMSDENASENNAGGKLPFl 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 998 -RACTKYLSSAGVLLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECALDQ-----SVYAMVftvlc 1071
Cdd:PTZ00265 800 rNLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEAnsnkySLYILV----- 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1072 slgIALCLVTSVTVE-----WTGLKVAKRLHRSLLNRIILAPMRFFEttplgsilnrfsSDCNT---IDQHIPSTLECLS 1143
Cdd:PTZ00265 875 ---IAIAMFISETLKnyynnVIGEKVEKTMKRRLFENILYQEISFFD------------QDKHApglLSAHINRDVHLLK 939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1144 RSTllcVSALTVISYVTPVFLVALLplavvcyfIQKYFrvasrdlqqlddttqLPLLshfAETVEGLTTI--RAFRYEAR 1221
Cdd:PTZ00265 940 TGL---VNNIVIFTHFIVLFLVSMV--------MSFYF---------------CPIV---AAVLTGTYFIfmRVFAIRAR 990
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1222 F-QQKLLEYTDSNNIASLFLTAAN-------RWLEVRMEYIGACVV----------LIAAATSISNSLHRE---LSAGLV 1280
Cdd:PTZ00265 991 LtANKDVEKKEINQPGTVFAYNSDdeifkdpSFLIQEAFYNMNTVIiygledyfcnLIEKAIDYSNKGQKRktlVNSMLW 1070
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1281 GLGLTYALMVSNYLNWmvrnLADMEIQLGAV------KRIHTLLKTEaeSYEGLLA-----------------PSLIPKN 1337
Cdd:PTZ00265 1071 GFSQSAQLFINSFAYW----FGSFLIRRGTIlvddfmKSLFTFLFTG--SYAGKLMslkgdsenaklsfekyyPLIIRKS 1144
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1338 WPD---------------QGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDM---- 1397
Cdd:PTZ00265 1145 NIDvrdnggiriknkndiKGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndh 1224
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1398 ---------------------------------FEGRIIIDGIDIAKL-----------------PLHTLRSRLSIILQD 1427
Cdd:PTZ00265 1225 hivfknehtndmtneqdyqgdeeqnvgmknvneFSLTKEGGSGEDSTVfknsgkilldgvdicdyNLKDLRNLFSIVSQE 1304
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1428 PVLFSGTIRFNLDPEKKcsDSTLWE---ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIM 1504
Cdd:PTZ00265 1305 PMLFNMSIYENIKFGKE--DATREDvkrACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLL 1382
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1505 DEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILSADLVMVL----KRGAILEFDKP-EKLLSQKDSVFASFV 1577
Cdd:PTZ00265 1383 DEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAHGThEELLSVQDGVYKKYV 1462
|
....
gi 1274095655 1578 RADK 1581
Cdd:PTZ00265 1463 KLAK 1466
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
688-907 |
3.10e-20 |
|
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: 90.55 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 688 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpDSEGEDPSNPEREtaadsDARSRg 767
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI------EIDGIDISTIPLE-----DLRSS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 pVAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEACSlqpdidilphgdqtqIGERGINLSGGQRQRISVARALYQHT 847
Cdd:cd03369 84 -LTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 848 NVVFLDDPFSALDVHlSDHLMQAGILELLRDDkrTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03369 145 RVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
696-907 |
5.15e-20 |
|
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: 88.99 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEREtaadsdARSRgpVAYASQK 775
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL------GKDIKKEPEE------VKRR--IGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLL-NATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLDD 854
Cdd:cd03230 82 PSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 855 PFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:cd03230 122 PTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1344-1565 |
7.23e-20 |
|
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: 90.32 E-value: 7.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRII--------IDGIDIAKLPLH 1415
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDegevlldgKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1416 tLRSRLSIILQDPVLFSGTIRFNLD--------PEKKCSDSTLWEALEIAQLKLVVKALPGGLDaiiteggenFSQGQRQ 1487
Cdd:cd03260 79 -LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1488 LFCLARAFVRKTSIFIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKL 1565
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
691-912 |
9.32e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.83 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNslpdseGEDpsnperetAADSDARSRGp 768
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrmIAGLEDPT--SGEILIG------GRD--------VTDLPPKDRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLL-NATVEENITF------ESPfnKQRYKMVIEAcslqpdIDILphgdqtQIGE----RGINLSGGQRQRI 837
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFplklrkVPK--AEIDRRVREA------AELL------GLEDlldrKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 838 SVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQREG 911
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVE-MRAEIKRLHRRLGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQVG 216
|
.
gi 1274095655 912 T 912
Cdd:COG3839 217 T 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
690-914 |
1.15e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDPSnperetaadsdarSRGPV 769
Cdd:TIGR00958 492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY-------------LHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENITFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 848
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMaAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 849 VVFLDDPFSALDVHlSDHLMQagilELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 914
Cdd:TIGR00958 638 VLILDEATSALDAE-CEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
696-920 |
1.92e-19 |
|
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: 89.27 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGED-PSNPERETAAdsdARSRgpVAYASQ 774
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD------GQDiTGLSEKELYE---LRRR--IGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 775 KPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARAL 843
Cdd:COG1127 90 GGALFDSlTVFENVAF--PLRehtdlseaeiRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLS---DHLmqagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSaviDEL----IRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
.
gi 1274095655 920 E 920
Cdd:COG1127 233 D 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
696-926 |
2.53e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.36 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgEMQRvSGAVFWNslpdseGEDpsnpereTAADSDARSRGpVAYAS 773
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLriIAGL-ETPD-SGRIVLN------GRD-------LFTNLPPRERR-VGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLL-NATVEENITF----ESPFNKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQ 845
Cdd:COG1118 82 QHYALFpHMTVAENIAFglrvRPPSKAEIRARVeelLELVQLEGLADRYPS-----------QLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 846 HTNVVFLDDPFSALDVHLSDHLMQaGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDfqrsecqLF 924
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRR-WLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDE-------VY 222
|
..
gi 1274095655 925 EH 926
Cdd:COG1118 223 DR 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
696-888 |
2.66e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 87.92 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPsnperetaADSDARSRGPVAYASQK 775
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN------GEPI--------RDAREDYRRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLLNA-TVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHTNV 849
Cdd:COG4133 84 DGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1274095655 850 VFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTH 888
Cdd:COG4133 153 WLLDEPFTALDAAGVALL--AELIAAHLARGGAVLLTTH 189
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
686-925 |
3.89e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.04 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPdsegEDPSNPEretaadsDARS 765
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA----ITDDNFE-------KLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RGPVAYASQKPWLLNATVEENITFESPFNKQRY-KMVIEACSLQPDIDILPHGD-QTQigergiNLSGGQRQRISVARAL 843
Cdd:PRK13648 84 HIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYdEMHRRVSEALKQVDMLERADyEPN------ALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQL 923
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
..
gi 1274095655 924 FE 925
Cdd:PRK13648 237 TR 238
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
691-890 |
5.74e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.52 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpdsegedpsnpERETAAdsdarsrgPVA 770
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------------RRAGGA--------RVA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQK---PWLLNATVEENITF-----ESPFNKQRY--KMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISVA 840
Cdd:NF040873 59 YVPQRsevPDSLPLTVRDLVAMgrwarRGLWRRLTRddRAAVDDALERVGLADLAG---RQLGE----LSGGQRQRALLA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTHKL 890
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDL 179
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
686-912 |
1.59e-18 |
|
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: 91.93 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLgeMQRVSGAVFWNSLPDSEgedpsnPERETAADSda 763
Cdd:TIGR03796 485 FGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIakLVAGL--YQPWSGEILFDGIPREE------IPREVLANS-- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 764 rsrgpVAYASQKPWLLNATVEENITFESPFNKQryKMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISVA 840
Cdd:TIGR03796 555 -----VAMVDQDIFLFEGTVRDNLTLWDPTIPD--ADLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:TIGR03796 628 RALVRNPSILILDEATSALDP-----ETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
673-907 |
1.86e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 90.90 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 673 DADNFCV--QIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGeMQRVSGAVFWNslpdseGEDP 750
Cdd:COG4172 277 EARDLKVwfPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFD------GQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 751 SNpeRETAADSDARSRGPVA----YASQKPWLlnaTVEENIT------FESPFNKQRYKMVIEACS---LQPD-IDILPH 816
Cdd:COG4172 350 DG--LSRRALRPLRRRMQVVfqdpFGSLSPRM---TVGQIIAeglrvhGPGLSAAERRARVAEALEevgLDPAaRHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 817 gdqtqigErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHKLQ- 891
Cdd:COG4172 425 -------E----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV-----QAQILDLLRDlqREHglAYLFISHDLAv 488
|
250
....*....|....*...
gi 1274095655 892 --YLphADWIIAMKDGTI 907
Cdd:COG4172 489 vrAL--AHRVMVMKDGKV 504
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
691-912 |
2.13e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.62 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSN--PERetaadsdarsRgP 768
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD------GRDVTGlpPEK----------R-N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRI 837
Cdd:COG3842 79 VGMVFQDyalfPHL---TVAENVAFglrmrgVPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 838 SVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKlQY--LPHADWIIAMKDGTIQREGT 912
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREE-MREELRRLQRELGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1344-1568 |
2.23e-18 |
|
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: 86.45 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPLHtLRS 1419
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMLAGLLKpdsgSILIDGEDVRKEPRE-ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1420 RLSIILQDPVLFSG-TIRFNLD---PEKKCSDSTLWEALEIaqlklVVKALpgGLDAIITEGGENFSQGQRQLFCLARAF 1495
Cdd:COG4555 75 QIGVLPDERGLYDRlTVRENIRyfaELYGLFDEELKKRIEE-----LIELL--GLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1496 VRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQ 1568
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
696-891 |
2.48e-18 |
|
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: 85.70 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWnslpdsEGEDPSNPEretaaDSDARSRGPVA 770
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLL------DGKDIYDLD-----VDVLELRRRVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPWLLNATVEENITF------ESPfNKQRYKMVIEACS---LQPDIDILPHGDQtqigerginLSGGQRQRISVAR 841
Cdd:cd03260 85 MVFQKPNPFPGSIYDNVAYglrlhgIKL-KEELDERVEEALRkaaLWDEVKDRLHALG---------LSGGQQQRLCLAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELlrDDKRTVVLVTHKLQ 891
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQ 201
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
686-912 |
2.60e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.65 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATlgemqRvsgavFWNslPDSeGEDPSNpERETAADSDAR 764
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLqLLT-----R-----AWD--PQQ-GEILLN-GQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 765 SRGPVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDIlPHGDQTQIGERGINLSGGQRQRISVARAL 843
Cdd:PRK11160 412 LRQAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQ-----ILELLAEhaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
692-907 |
3.54e-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: 83.25 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWNslpdseGEdpsnpERETAADSDARSRGpV 769
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMkiLS--GLYKPDSGEILVD------GK-----EVSFASPRDARRAG-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNV 849
Cdd:cd03216 78 AMVYQ------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 850 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:cd03216 104 LILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1345-1554 |
3.66e-18 |
|
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: 84.83 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1345 QIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSII 1424
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1425 LQDP--VLFSGTIR---------FNLDPEKkcSDSTLWEALEIAQLKLVVKALPggldaiiteggENFSQGQRQLFCLAR 1493
Cdd:cd03225 81 FQNPddQFFGPTVEeevafglenLGLPEEE--IEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 1494 AFVRKTSIFIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILS-ADLVMVLKRG 1554
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
691-902 |
6.31e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRvsGAVFWnslpdsEGEDPS--NPERetaadsdarSR 766
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLkiVASLISPTS--GTLLF------EGEDIStlKPEI---------YR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 767 GPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQ----PDidilphgdqtQIGERGIN-LSGGQRQRISVAR 841
Cdd:PRK10247 81 QQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLErfalPD----------TILTKNIAeLSGGEKQRISLIR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 902
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
654-906 |
6.67e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 654 EEVRDLLGPLQRLTPSMDGD--ADNFCVQiiggfftwTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ 731
Cdd:COG4178 343 EAADALPEAASRIETSEDGAlaLEDLTLR--------TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 732 RVSGAVfwnSLPDSEGedpsnperetaadsdarsrgpVAYASQKPWLLNATVEENITF---ESPFNKQRYKMVIEACSLQ 808
Cdd:COG4178 415 YGSGRI---ARPAGAR---------------------VLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 809 pdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTH 888
Cdd:COG4178 471 ---HLAERLDEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--TTVISVGH 542
|
250
....*....|....*...
gi 1274095655 889 KLQYLPHADWIIAMKDGT 906
Cdd:COG4178 543 RSTLAAFHDRVLELTGDG 560
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
694-912 |
9.99e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.11 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNslpdseGEDPsnpeRETAADSDARSRGPVAy 771
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRILID------GQDI----RDVTQASLRAAIGIVP- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 asQKPWLLNATVEENItfespfnkqRY----------KMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 841
Cdd:COG5265 439 --QDTVLFNDTIAYNI---------AYgrpdaseeevEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSR-TERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
703-911 |
1.45e-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: 82.93 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 703 IPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDpsnperETAADSDARsrgPVAYASQKPWLL-NA 781
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN------GVD------VTAAPPADR---PVSMLFQENNLFaHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 782 TVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALYQHTNVVFLDD 854
Cdd:cd03298 86 TVEQNVGLGlspglklTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 855 PFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 911
Cdd:cd03298 155 PFAALDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
692-916 |
2.33e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 82.87 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDpsnperETAADSDARSRGPVAY 771
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF------DGRD------ITGLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLL-NATVEENITF-ESPFNKQRYKMVIE-ACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVARALYQHTN 848
Cdd:cd03224 80 VPEGRRIFpELTVEENLLLgAYARRRAKRKARLErVYELFPRL-------KERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 849 VVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 916
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEA--IRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
695-920 |
4.09e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.11 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 695 TLSNITIR-----------IPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDpsnperETAADSDA 763
Cdd:COG3840 3 RLDDLTYRygdfplrfdltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN------GQD------LTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 764 RsrgPVAYASQK----PWLlnaTVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgDQtqigerginLSGG 832
Cdd:COG3840 71 R---PVSMLFQEnnlfPHL---TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 833 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 911
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPALRQE-MLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADG 212
|
....*....
gi 1274095655 912 TLKDFQRSE 920
Cdd:COG3840 213 PTAALLDGE 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
691-912 |
5.80e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 82.00 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDpsnperetAADSDARSRGpVA 770
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG------GED--------ATDVPVQERN-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 838
Cdd:cd03296 78 FVFQHYALFrHMTVFDNVAFglrvkprsERPPEaeiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKEL-RRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
698-919 |
7.06e-17 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 86.10 E-value: 7.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQRVSGAVFWNSLPDseGEDPSNPERETAadsdarsRGPVAYASQKPW 777
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLI----NLLQRVYDPTVGQILID--GIDINTVTRESL-------RKSIATVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 778 LLNATVEENITF--ESPFNKQRYKMViEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDP 855
Cdd:TIGR01192 420 LFNRSIRENIRLgrEGATDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 856 FSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:TIGR01192 499 TSALDVETEARVKNA--IDALRKN-RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
698-920 |
7.29e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPsnpeRETAADSDARSRGPVAYasqkpw 777
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL------DGEHI----QHYASKEVARRIGLLAQ------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 778 llNATVEENITFESPFNKQRYKMvieacslQP--------DIDILPHGDQ----TQIGERGIN-LSGGQRQRISVARALY 844
Cdd:PRK10253 89 --NATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 845 QHTNVVFLDDPFSALDVhlsDHlmQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:PRK10253 160 QETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
.
gi 1274095655 920 E 920
Cdd:PRK10253 235 E 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
690-915 |
1.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.20 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPdsegedpsnpeRETAADSDARSRGPV 769
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-----------IDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISV 839
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSF-GAVNlklpedevRKRVDNALKRTGIEHLKDKPTHC-----------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 840 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL-LVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
691-911 |
1.28e-16 |
|
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: 80.38 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDpsnperetAADSDARSRGpVA 770
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG------GRD--------VTDLPPKDRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPWLL-NATVEENITFESPFNKQRyKMVIE------ACSLQpdIDILPHGDQTQigerginLSGGQRQRISVARAL 843
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVP-KDEIDervrevAELLQ--IEHLLDRKPKQ-------LSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 911
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1336-1551 |
1.38e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.24 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1336 KNWPDQGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAK-LP 1413
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1414 LHTLRSRLSIILQDPVLFSGTIRFN----------------------------LDPEKKC--------------SDSTLW 1451
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdlealsnyynedgndsqenKNKRNSCrakcagdlndmsntTDSNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1452 -------------EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1515
Cdd:PTZ00265 535 iemrknyqtikdsEVVDVSKKVLIhdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270
....*....|....*....|....*....|....*...
gi 1274095655 1516 ENILQKVV--MTAFADRTVVTIAHRVHTILSADLVMVL 1551
Cdd:PTZ00265 615 EYLVQKTInnLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1361-1509 |
1.39e-16 |
|
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: 78.46 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1361 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL 1439
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1440 -------DPEKKCSDSTLWEALEiaqlKLvvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1509
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALE----KL---GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
696-891 |
1.69e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.37 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFW--NSLPDSEgEDPSnperetaadsDARSRgp 768
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFhgKNLYAPD-VDPV----------EVRRR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLLNATVEENITFESPFNKQRYKM--VIEACSLQPdidILPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIAYGARINGYKGDMdeLVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1274095655 847 TNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHKLQ 891
Cdd:PRK14243 170 PEVILMDEPCSAL-----DPISTLRIEELMHELKEqyTIIIVTHNMQ 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
686-915 |
2.08e-16 |
|
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: 80.32 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMQRvSGAVFWNslpdseGED---PSNPERETAads 761
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrCINGLERPT-SGSVLVD------GTDltlLSGKELRKA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 762 daRSRgpVAYASQKPWLLNA-TVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQ 833
Cdd:cd03258 81 --RRR--IGMIFQHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 834 RQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQ 908
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
....*..
gi 1274095655 909 REGTLKD 915
Cdd:cd03258 221 EEGTVEE 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
690-888 |
2.64e-16 |
|
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: 79.37 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNpERETAADSDARSRGpV 769
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN------GQDVSD-LRGRAIPYLRRKIG-V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKpWLLNATVEENITF------ESPFN-KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARA 842
Cdd:cd03292 83 VFQDFR-LLPDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1274095655 843 LYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD-DKR--TVVLVTH 888
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTT-----WEIMNLLKKiNKAgtTVVVATH 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
691-915 |
2.82e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.97 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPSN---PERetaadsdarsrg 767
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL------DGKDITNlppHKR------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVAYASQKPWLL-NATVEENITF-----ESPFNKQRYKmVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRISVA 840
Cdd:cd03300 73 PVNTVFQNYALFpHLTVFENIAFglrlkKLPKAEIKER-VAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSDHlMQagiLELLRDDKR---TVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKD-MQ---LELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
698-912 |
3.17e-16 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 80.77 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPSNperetAADSDARS--RGPVAYASQK 775
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI------DGQDIAA-----MSRKELRElrRKKISMVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLL-NATVEENITF------ESPFNKQRYKM-VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHT 847
Cdd:cd03294 111 FALLpHRTVLENVAFglevqgVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 848 NVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03294 180 DILLMDEAFSALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
711-912 |
3.35e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 81.77 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 711 IVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSN--PERetaadsdaRSRGPV--AYAsqkpWLLNATVEEN 786
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLD------GEDVTNvpPHL--------RHINMVfqSYA----LFPHMTVEEN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 787 ITFESPFNK----QRYKMVIEACSLqpdidilphgdqTQIGERG----INLSGGQRQRISVARALYQHTNVVFLDDPFSA 858
Cdd:TIGR01187 63 VAFGLKMRKvpraEIKPRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 859 LDVHLSDhLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 912
Cdd:TIGR01187 131 LDKKLRD-QMQLELKTIQEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
689-888 |
4.14e-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: 77.58 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnSLPDSEGedpsnperetaadsdarsrgp 768
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGED--------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidILPHGDqtqigergiNLSGGQRQRISVARALYQHTN 848
Cdd:cd03223 66 LLFLPQRPYLPLGTLREQL-------------------------IYPWDD---------VLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1274095655 849 VVFLDDPFSALDVHLSDHLMQagileLLRDDKRTVVLVTH 888
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGH 146
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1344-1559 |
4.61e-16 |
|
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: 79.09 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD------MFEGRIIIDGIDIAKLPLh 1415
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiIFDGKDLLKLSRRLRKIR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1416 tlRSRLSIILQDPvlFSgtirfNLDPEKKCSDStLWEALEI--------AQLKLVVKALPG-GLDAII-----TEggenF 1481
Cdd:cd03257 81 --RKEIQMVFQDP--MS-----SLNPRMTIGEQ-IAEPLRIhgklskkeARKEAVLLLLVGvGLPEEVlnrypHE----L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1482 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVMVLKRGAI 1556
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
...
gi 1274095655 1557 LEF 1559
Cdd:cd03257 225 VEE 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
694-888 |
5.34e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.91 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavFwnsLPDSEGEDPSNPERETAADSDarsRGPVAyas 773
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAG---------F---LAPSSGEITLDGVPVTGPGAD---RGVVF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QK----PWLlnaTVEENITFESPFNK----QRYKMVIEACSLqpdIDiLPHGDQTQIGErginLSGGQRQRISVARALYQ 845
Cdd:COG4525 83 QKdallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VG-LADFARRRIWQ----LSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1274095655 846 HTNVVFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTH 888
Cdd:COG4525 152 DPRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
686-902 |
6.21e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.29 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---RVSGAVFWNslpdseGED--PSNPERetaad 760
Cdd:COG4136 7 LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLN------GRRltALPAEQ----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 761 sdarsRGpVAYASQKPWLL-NATVEENITF---ESPFNKQRYKMVIEAcsLQpDIDiLPHgdqtqIGERGIN-LSGGQRQ 835
Cdd:COG4136 76 -----RR-IGILFQDDLLFpHLSVGENLAFalpPTIGRAQRRARVEQA--LE-EAG-LAG-----FADRDPAtLSGGQRA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 836 RISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 902
Cdd:COG4136 141 RVALLRALLAEPRALLLDEPFSKLDAALRAQ-FREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
696-936 |
6.85e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlatlgemQRVSGAVFWNSLPDSEGEDPSNP-ERETAADSDAR-SRGPVAYAS 773
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKSAGSHIELLGRTvQREGRLARDIRkSRANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLLNA-TVEENITF----ESPFNKQRYKMVIEAcSLQPDIDILphgdqTQIG------ERGINLSGGQRQRISVARA 842
Cdd:PRK09984 93 QQFNLVNRlSVLENVLIgalgSTPFWRTCFSWFTRE-QKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 843 LYQHTNVVFLDDPFSALDVHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDFQ 917
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVM-----DTLRDinqnDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFD 241
|
250
....*....|....*....
gi 1274095655 918 RSEcqlFEHWKTLMNRQDQ 936
Cdd:PRK09984 242 NER---FDHLYRSINRVEE 257
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
694-912 |
8.18e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.70 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQRV----SGAVfwnsLPDseGEDPSNPERETAadsdarsRGPV 769
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQRVfdpqSGRI----LID--GTDIRTVTRASL-------RRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENITFESPfNKQRYKMVIEACSLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 847
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 848 NVVFLDDPFSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAA--LDELMKG-RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1344-1555 |
9.76e-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: 78.14 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRI--IIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIIL--QDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1499
Cdd:cd03290 80 SVAYaaQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 1500 SIFIMDEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVMVLKRGA 1555
Cdd:cd03290 160 NIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
706-911 |
1.02e-15 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 77.72 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 706 GQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWNslpDSEGEDPSNPERetaadsdarsRGpVAYASQKPWLL- 779
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLrciagLEKPDGGTIVLNGTVLF---DSRKKINLPPQQ----------RK-IGLVFQQYALFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 780 NATVEENITFESPFNKQRYKMVIEAcslqpdiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTNVVFLDDPFSA 858
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 859 LDVHLSDHLMQAgILELLRDDKRTVVLVTHKL---QYLphADWIIAMKDGTIQREG 911
Cdd:cd03297 162 LDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
693-912 |
1.15e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQRVSGAVFWNSLPD--SEGEDPSNPERE------------ 756
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVmsLLMRFYDLKNDHHIVFKNEHTNdmTNEQDYQGDEEQnvgmknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 757 TAADSDARS-------------------------RGPVAYASQKPWLLNATVEENITF-ESPFNKQRYKMVIEACSLQPD 810
Cdd:PTZ00265 1261 TKEGGSGEDstvfknsgkilldgvdicdynlkdlRNLFSIVSQEPMLFNMSIYENIKFgKEDATREDVKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 811 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKL 890
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
250 260
....*....|....*....|....*..
gi 1274095655 891 QYLPHADWIIAM----KDGT-IQREGT 912
Cdd:PTZ00265 1420 ASIKRSDKIVVFnnpdRTGSfVQAHGT 1446
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
696-912 |
1.50e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.13 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGED-------------PSNPERETAadsd 762
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqlarrlallpqhHLTPEGITV---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 763 arsRGPVAYAsQKPWLlnatveeniTFESPFNKQRYKMVIEACslqpdidilphgDQTQIGE----RGINLSGGQRQRIS 838
Cdd:PRK11231 94 ---RELVAYG-RSPWL---------SLWGRLSAEDNARVNQAM------------EQTRINHladrRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
696-907 |
1.97e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.18 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDpsnperetaaDS-----DARsrgpva 770
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE----------DTrlmfqDAR------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 yasQKPWllnATVEENITFESPFN-KQRYKMVIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQHTNV 849
Cdd:PRK11247 92 ---LLPW---KKVIDNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 850 VFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 907
Cdd:PRK11247 155 LLLDEPLGALDA-LTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
696-889 |
2.02e-15 |
|
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: 77.31 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---RVSGAVFWNSLPdsegedpsnPERETAADSdarsrgpVAYA 772
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQP---------RKPDQFQKC-------VAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 773 SQKPWLL-NATVEENITFESPF-------NKQRYKMVieacslqpDIDILPHGDQTQIGERGI-NLSGGQRQRISVARAL 843
Cdd:cd03234 87 RQDDILLpGLTVRETLTYTAILrlprkssDAIRKKRV--------EDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHK 889
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
690-915 |
2.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.20 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPdsegedpsnperetaADSDARS---- 765
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP---------------IKYDKKSllev 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 835
Cdd:PRK13639 77 RKTVGIVFQNPddQLFAPTVEEDVAF-GPLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 836 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLK 914
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPK 222
|
.
gi 1274095655 915 D 915
Cdd:PRK13639 223 E 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
691-912 |
2.64e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.30 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavfwnSLPDSEGE---DpsnpERETAADSDARSRG 767
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG------------YYPLTEGEirlD----GRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 847
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 848 NVVFLDDPFSALDVHLSDHLMQAgiLELLRdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQA--LAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
696-909 |
2.76e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQRVSGAVFWNSlpdseGEDPSNPERETAAdsdARSRGPVAYASQK 775
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDKPTSGTYRVA-----GQDVATLDADALA---QLRREHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLL-NATVEENITFESPF-------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHT 847
Cdd:PRK10535 95 YHLLsHLTAAQNVEVPAVYaglerkqRLLRAQELLQRLGLEDRVEYQPS-----------QLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 848 NVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQR 909
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
696-915 |
3.88e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 76.61 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSN--PERETaadsdarsrgpVAYAS 773
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN------GKDITNlpPEKRD-----------ISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLL-NATVEENITF----ESPFNKQRYKMVIE-ACSLqpDIDILPHGDQTqigergiNLSGGQRQRISVARALYQHT 847
Cdd:cd03299 78 QNYALFpHMTVYKNIAYglkkRKVDKKEIERKVLEiAEML--GIDHLLNRKPE-------TLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 848 NVVFLDDPFSALDVHLSDHLMqagilELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLR-----EELKKIRKefgvTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
696-920 |
4.89e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.37 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpdSEGEDPSNPERETAADSDARSRgpVAYASQK 775
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-------TIGERVITAGKKNKKLKPLRKK--VGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 P--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALYQ 845
Cdd:PRK13634 94 PehQLFEETVEKDICF-GPMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 846 HTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLKD-FQRSE 920
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEM-FYKLHKEKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREiFADPD 238
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1340-1570 |
8.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.57 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1340 DQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRS 1419
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1420 RLSIILQDP-VLFSGT-----IRFNLdpEKKCSDSTLWEALeIAQLKLVVkalpgGLDAIITEGGENFSQGQRQLFCLAR 1493
Cdd:PRK13632 84 KIGIIFQNPdNQFIGAtveddIAFGL--ENKKVPPKKMKDI-IDDLAKKV-----GMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 1494 AFVRKTSIFIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKD 1570
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
687-911 |
8.44e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 75.28 E-value: 8.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 687 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLpDSEGEDPSnperetaadsdarsR 766
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ-SHTGLAPY--------------Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 767 GPVAYASQKPWLL-NATVEENITFE-SPFNK----QRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRIS 838
Cdd:TIGR01277 70 RPVSMLFQENNLFaHLTVRQNIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRVA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 911
Cdd:TIGR01277 139 LARCLVRPNPILLLDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
694-912 |
8.82e-15 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 75.23 E-value: 8.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDsegedpsNPERETAadsdarsRGPVAYAS 773
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-------RTDRKAA-------RQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QK---PWLLnaTVEENITFESPF---NKQRYKMVIEA----CSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARAL 843
Cdd:cd03263 82 QFdalFDEL--TVREHLRFYARLkglPKSEIKEEVELllrvLGLTDKAN-------KRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRddKRTVVLVTHKLQ---YLphADWIIAMKDGTIQREGT 912
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDL-ILEVRK--GRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
686-916 |
1.38e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---RVSGAV-FWNSlpdsegedpSNPERETAA 759
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELEsevRVEGRVeFFNQ---------NIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 760 DsdaRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKM----VIEACSLQPDI-DILPHgdqtQIGERGINLSGGQR 834
Cdd:PRK14258 84 N---RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLwDEIKH----KIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 835 QRISVARALYQHTNVVFLDDPFSALDVHLS---DHLMQAGILEllrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 911
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVSRLSDFTAFFKGNENRIG 232
|
....*
gi 1274095655 912 TLKDF 916
Cdd:PRK14258 233 QLVEF 237
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
683-910 |
1.59e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 75.61 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 683 GGFFtWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPS--NPERETAAD 760
Cdd:TIGR02769 15 GGLF-GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF------RGQDLYqlDRKQRRAFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 761 SDARSRGPVAYASQKP-----WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQR 834
Cdd:TIGR02769 88 RDVQLVFQDSPSAVNPrmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 835 QRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQR 909
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
.
gi 1274095655 910 E 910
Cdd:TIGR02769 232 E 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
692-920 |
1.86e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWNslpdseGE--DPSNPeretaadSDARSRG 767
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMkiLS--GVYQPDSGEILLD------GEpvRFRSP-------RDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 pVAYASQKPWLL-NATVEENITFESPFNK----QRYKMVIEACSL--QPDIDILPHgdqTQIGErginLSGGQRQRISVA 840
Cdd:COG1129 81 -IAIIHQELNLVpNLSVAENIFLGREPRRggliDWRAMRRRARELlaRLGLDIDPD---TPVGD----LSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAELTED 230
|
.
gi 1274095655 920 E 920
Cdd:COG1129 231 E 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1344-1568 |
2.89e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 77.64 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLK---PVLKHVNALIAPGQKIGICGRTGSGKSSFSLA------------FFRMVDMfegriiidgID 1408
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLllgllrptsgsiLFDGKDL---------TK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1409 IAKLPLHTLRSRLSIILQDPvlFSGtirfnLDPEKKCSDStLWEALEIAQL-------KLVVKAL------PGGLDAIIT 1475
Cdd:COG1123 332 LSRRSLRELRRRVQMVFQDP--YSS-----LNPRMTVGDI-IAEPLRLHGLlsraerrERVAELLervglpPDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1476 EggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLV 1548
Cdd:COG1123 404 E----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRV 475
|
250 260
....*....|....*....|
gi 1274095655 1549 MVLKRGAILEFDKPEKLLSQ 1568
Cdd:COG1123 476 AVMYDGRIVEDGPTEEVFAN 495
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
689-888 |
3.04e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 75.47 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQRVSGAVFWnslpdsEGEDPSN-PERETAAdsdA 763
Cdd:COG0444 13 TRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILF------DGEDLLKlSEKELRK---I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 764 RSRGpVAYASQKPwlLNA-----TVEENITfESPFN------KQRYKMVIEA---CSLQPDIDIL---PHgdqtqigerg 826
Cdd:COG0444 84 RGRE-IQMIFQDP--MTSlnpvmTVGDQIA-EPLRIhgglskAEARERAIELlerVGLPDPERRLdryPH---------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 827 iNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTH 888
Cdd:COG0444 150 -ELSGGMRQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITH 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
696-888 |
3.91e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.98 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnSLPDSEGEDPSNPERetaadsdarsrgpVAYASQ- 774
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI---KLDGGDIDDPDVAEA-------------CHYLGHr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 775 ---KPWLlnaTVEENITFESPFNKQRYKMV---IEACSLQPDIDiLPHGdqtqigergiNLSGGQRQRISVARALYQHTN 848
Cdd:PRK13539 82 namKPAL---TVAENLEFWAAFLGGEELDIaaaLEAVGLAPLAH-LPFG----------YLSAGQKRRVALARLLVSNRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1274095655 849 VVFLDDPFSALDVH--------LSDHLMQAGIlellrddkrtVVLVTH 888
Cdd:PRK13539 148 IWILDEPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
691-888 |
4.79e-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: 72.39 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDpsNPEREtaadsdarsrgpVA 770
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD--EPHEN------------IL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPWLLNA-TVEENITFESPFNKQRYKMVIEACslqpdidilphgdqTQIGERGIN------LSGGQRQRISVARAL 843
Cdd:TIGR01189 77 YLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARLW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 844 YQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 888
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
692-911 |
4.93e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnslpdSEGEDPSnperetAADSDARSRgPVAY 771
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL------VAGDDVE------ALSARAASR-RVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWL-LNATVEENITFESPFNKQRYKMVIEACSLQPDiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTNV 849
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 850 VFLDDPFSALDVHlsdHLMQAgiLELLR---DDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 911
Cdd:PRK09536 161 LLLDEPTASLDIN---HQVRT--LELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAG 221
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1082-1314 |
6.98e-14 |
|
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: 74.00 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1082 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYV-- 1159
Cdd:cd18552 60 TYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdw 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1160 --TPVFLVALLPLAVVCYFIQKYFRVASRDLQ-QLDDttqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSN--- 1233
Cdd:cd18552 140 klTLIALVVLPLAALPIRRIGKRLRKISRRSQeSMGD-----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLrrl 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1234 NIASLFLTAANRWLevrMEYIGACVVLIAAATSISNSLHRELSAG-LVGLgLTYALMVSNYLnwmvRNLADM--EIQ--L 1308
Cdd:cd18552 215 SMKIARARALSSPL---MELLGAIAIALVLWYGGYQVISGELTPGeFISF-ITALLLLYQPI----KRLSNVnaNLQrgL 286
|
....*.
gi 1274095655 1309 GAVKRI 1314
Cdd:cd18552 287 AAAERI 292
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
690-911 |
7.02e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSN-PERETAAdsdARSR-G 767
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN------GQDLSRlKRREIPY---LRRRiG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVAyasQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 839
Cdd:COG2884 83 VVF---QDFRLLpDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 840 ARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPHADW-IIAMKDGTIQREG 911
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSW-----EIMELLEEINRrgtTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
686-912 |
7.64e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.68 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMqrvsgavfwnsLPDSegedpsNPERETAADS---- 761
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL-----------LPDD------NPNSKITVDGitlt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 762 -----DARSRGPVAYASQKPWLLNATVEENITFESPfNKQ--RYKMVIEACSLQPDIDILPHGDQTQIgergiNLSGGQR 834
Cdd:PRK13640 76 aktvwDIREKVGIVFQNPDNQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 835 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL-IRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
691-888 |
7.67e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.26 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPSN--PEREtaadsdarsrgP 768
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML------DGVDLSHvpPYQR-----------P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLL-NATVEENITFESPFNK-------QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVA 840
Cdd:PRK11607 93 INMMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH 888
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDR-MQLEVVDILERVGVTCVMVTH 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
691-891 |
8.94e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnSLPDSEGEDPSnPERETAADSDARSrgpva 770
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI---TLDGKPVEGPG-AERGVVFQNEGLL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 yasqkPWLlnaTVEENITFespfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTNV 849
Cdd:PRK11248 83 -----PWR---NVQDNVAF-----GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1274095655 850 VFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 891
Cdd:PRK11248 150 LLLDEPFGALDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
684-902 |
1.31e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.85 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 684 GFFTwTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQRVSGAVFWNslpdseGEDPSNPERETAADsd 762
Cdd:PRK11308 20 GLFK-PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIE-TPTGGELYYQ------GQDLLKADPEAQKL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 763 ARSR------GPvaYASQKP-WLLNATVEE----NITFESPFNKQRYKMVIEACSLQPD-IDILPHgdqtqigergiNLS 830
Cdd:PRK11308 90 LRQKiqivfqNP--YGSLNPrKKVGQILEEplliNTSLSAAERREKALAMMAKVGLRPEhYDRYPH-----------MFS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 831 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 902
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQelglSYVFISHDLSVVEHiADEVMVM 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1341-1569 |
1.56e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.25 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1341 QGKIQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMF-----EGRIIIDGIDIAKLPLH 1415
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1416 TLRSRLSIILQDP------VLFSGT---IRFN-LDPEKKCSDSTLWEALEIAQLKLVVKalpGGLDAiiteGGENFSQGQ 1485
Cdd:PRK14247 79 ELRRRVQMVFQIPnpipnlSIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVK---DRLDA----PAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1486 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtilsADLVMVLKRGAILE- 1558
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEw 226
|
250
....*....|....*..
gi 1274095655 1559 ------FDKPEKLLSQK 1569
Cdd:PRK14247 227 gptrevFTNPRHELTEK 243
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
690-912 |
1.64e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.71 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnslpdSEGEDPSNPERETAAdsdarsRGPV 769
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL------VSGIDTGDFSKLQGI------RKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKP--WLLNATVEENITFeSPFNkqrykmvieACslQPDIDILPHGDQTqIGERGI---------NLSGGQRQRIS 838
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAF-GPEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
696-892 |
2.21e-13 |
|
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: 70.27 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWNSLPDSEGEdpsnperetaadsdarSRGPVAYAS 773
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLnaLAGRRTGLGVSGEVLINGRPLDKRS----------------FRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLL-NATVEENITFespfnkqrykmvieACSLQpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFL 852
Cdd:cd03213 89 QDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1274095655 853 DDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY 892
Cdd:cd03213 136 DEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSS 173
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1063-1314 |
2.51e-13 |
|
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: 72.58 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1063 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1142
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1143 SRSTLLCVSALTVISYVTPV-FLVALLPLAVVCYFIQKYF---RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1218
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWKlTLVALLLLPLYVLILRYFRrriRKASREVRESLAE----LSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1219 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELSAGlvglGLTYALMVSNYLNWMV 1298
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG----ELVAFLAYLGMLFGPI 272
|
250 260
....*....|....*....|
gi 1274095655 1299 RNLADM--EIQ--LGAVKRI 1314
Cdd:cd07346 273 QRLANLynQLQqaLASLERI 292
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
694-907 |
2.53e-13 |
|
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: 71.86 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnslpdSEGEDPSNPERETAadsdaRSRgpVAYAS 773
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV------IDGIDISKLPLHTL-----RSR--LSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLD 853
Cdd:cd03288 102 QDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 854 DPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03288 182 EATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
696-918 |
3.26e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.81 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPEretaadsdARSRgPVAYASQK 775
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH------GTDVSRLH--------ARDR-KVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPhgdqTQigerginLSGGQRQRISVARAL 843
Cdd:PRK10851 83 YALFrHMTVFDNIAFgltvlprrERPNAaaiKAKVTQLLEMVQLAHLADRYP----AQ-------LSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQR 918
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKEL-RRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
696-907 |
3.66e-13 |
|
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: 70.25 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNslpdseGEDPSNPERETAAdsdARSRgpVAYAS 773
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTIIID------GLKLTDDKKNINE---LRQK--VGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLL-NATVEENITfESP---FNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNV 849
Cdd:cd03262 83 QQFNLFpHLTVLENIT-LAPikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 850 VFLDDPFSALDVHlsdhlMQAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:cd03262 157 MLFDEPTSALDPE-----LVGEVLDVMKDlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
691-915 |
3.97e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSN--PEREtaadsdarsrgP 768
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD------GQDITHvpAENR-----------H 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLL-NATVEENITF-----ESPfNKQRYKMVIEA---CSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 839
Cdd:PRK09452 88 VNTVFQSYALFpHMTVFENVAFglrmqKTP-AAEITPRVMEAlrmVQLEEFAQRKPH-----------QLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 840 ARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQ-MQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
687-890 |
4.07e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 687 TWTpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgedpsnperetaadsdARSR 766
Cdd:PRK15056 15 TWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----------------ALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 767 GPVAYASQKP---WLLNATVEENIT---------FESPfnKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQR 834
Cdd:PRK15056 78 NLVAYVPQSEevdWSFPVLVEDVVMmgryghmgwLRRA--KKRDRQIVTAALARVDMVEFRH---RQIGE----LSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 835 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL 890
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNL 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1344-1567 |
4.24e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSL------------AFFRMVDMFEgriiidgidIAK 1411
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALhlngllrpqkgkVLVSGIDTGD---------FSK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1412 LPlhTLRSRLSIILQDP-VLFSG-TIRFNL--DPEKKCSDSTlwealEIAqlKLVVKALPG-GLDAIITEGGENFSQGQR 1486
Cdd:PRK13644 72 LQ--GIRKLVGIVFQNPeTQFVGrTVEEDLafGPENLCLPPI-----EIR--KRVDRALAEiGLEKYRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1487 QLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKL 1565
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
..
gi 1274095655 1566 LS 1567
Cdd:PRK13644 223 LS 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
696-891 |
4.52e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.84 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEM------QRVSGAVFWNslpdseGEDPSNPERETAAdsdARSRgpV 769
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLL-RCLNRMndlipgARVEGEILLD------GEDIYDPDVDVVE---LRRR--V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENITFESPFNKQRYKMVIEA--------CSLQPDI-DILphgdqtqiGERGINLSGGQRQRISVA 840
Cdd:COG1117 95 GMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVkDRL--------KKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD--DKRTVVLVTHKLQ 891
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPIST-----AKIEELILElkKDYTIVIVTHNMQ 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
818-911 |
6.16e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.77 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 818 DQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-A 896
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvS 219
|
90
....*....|....*
gi 1274095655 897 DWIIAMKDGTIQREG 911
Cdd:PRK10619 220 SHVIFLHQGKIEEEG 234
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1059-1314 |
7.12e-13 |
|
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: 71.05 E-value: 7.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1059 DQSVYAMVFTVLCSLGIALCLVTSVTV---EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHI 1135
Cdd:cd18557 31 DLDVLNELALILLAIYLLQSVFTFVRYylfNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1136 PSTLECLSRSTLLCVSA---LTVISY-VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQlddttQLPLLSHFA-ETVEGL 1210
Cdd:cd18557 111 TDNLSQLLRNILQVIGGliiLFILSWkLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQD-----ALAKAGQVAeESLSNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1211 TTIRAF---RYE-ARFQQKLLEYTDSnNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSlhrELSAGLVGLGLTY 1286
Cdd:cd18557 186 RTVRSFsaeEKEiRRYSEALDRSYRL-ARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSG---QLTVGELTSFILY 261
|
250 260
....*....|....*....|....*...
gi 1274095655 1287 ALMVSNYLNWMVRNLADMEIQLGAVKRI 1314
Cdd:cd18557 262 TIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1344-1567 |
7.20e-13 |
|
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: 70.22 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSL--KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPvlfsgtiRFNLDPEKKCsDSTLWEALEIAQLKLVVKALPGGLDAIiteG-GENF--------SQGQRQLFCLA 1492
Cdd:COG1124 82 QMVFQDP-------YASLHPRHTV-DRILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1493 RAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1344-1568 |
1.02e-12 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrLSI 1423
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKS------------------------------TL---LKA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 IL--QDPVlfSGTIRFNLDPEKKCSDStlwealeIA---QLKLVVKALP--------GGLD--------------AIITE 1476
Cdd:COG1121 52 ILglLPPT--SGTVRLFGKPPRRARRR-------IGyvpQRAEVDWDFPitvrdvvlMGRYgrrglfrrpsradrEAVDE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1477 -----GGENF--------SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI 1542
Cdd:COG1121 123 alervGLEDLadrpigelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAV 202
|
250 260
....*....|....*....|....*..
gi 1274095655 1543 LS-ADLVMVLKRGaILEFDKPEKLLSQ 1568
Cdd:COG1121 203 REyFDRVLLLNRG-LVAHGPPEEVLTP 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1345-1556 |
1.30e-12 |
|
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: 68.71 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1345 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRM-----------VDMFEGRIIIDGIDIAKLP 1413
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTL----LKAilgllkptsgsIRVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1414 LHTLRSRLS-IILQDPVLFSGTIRFNLDPEKKCSDstlWEALEIAqLKLVvkalpgGLDAI----ITEggenFSQGQRQL 1488
Cdd:cd03235 75 QRRSIDRDFpISVRDVVLMGLYGHKGLFRRLSKAD---KAKVDEA-LERV------GLSELadrqIGE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1489 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-SADLVMVLKRGAI 1556
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLeYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
676-911 |
1.36e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.76 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 676 NFCVQIIGGFFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG--EMQRVSGAVFwnslpdsegedpsnp 753
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiyLPQRGRVKVM--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 754 ERETAADSDARSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqig 823
Cdd:PRK13647 66 GREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAF-GPVNmgldkdevERRVEEALKAVRMWDFRDKPPY------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 824 ergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAM 902
Cdd:PRK13647 138 ----HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVL 211
|
....*....
gi 1274095655 903 KDGTIQREG 911
Cdd:PRK13647 212 KEGRVLAEG 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1345-1557 |
1.59e-12 |
|
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: 67.46 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1345 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLRSRLSII 1424
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKS------------------------------TLLKTLAGL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1425 LQdpvLFSGTIRFNLDPEKKcsdstlWEALEIAQLKLVV----KALpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03214 49 LK---PSSGEILLDGKDLAS------LSPKELARKIAYVpqalELL--GLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1501 IFIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILSADLVMVLKRGAIL 1557
Cdd:cd03214 118 ILLLDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1339-1538 |
1.78e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.15 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1339 PDQGKIQIQNLSVRyDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKLPLH--- 1415
Cdd:COG4178 358 SEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAI--------------AGLWPYgsg 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1416 --TLRSRLSIIL--QDPVLFSGTIRFNL---DPEKKCSDSTLWEALEIAQLKlvvkALPGGLDAIiTEGGENFSQGQRQL 1488
Cdd:COG4178 419 riARPAGARVLFlpQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLG----HLAERLDEE-ADWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1489 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1538
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1328-1563 |
1.92e-12 |
|
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: 71.64 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1328 LLA--PSLIPKNWPDQGK--IQIQNLSVRYD---SSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRM 1394
Cdd:COG4172 256 LLAaePRGDPRPVPPDAPplLEARDLKVWFPikrGLFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1395 VD-----MFEGRIIIDGIDIAKLPlhtLRSRLSIILQDPvlFSgtirfNLDPEKKCSDsTLWEALEIAQLKL-------- 1461
Cdd:COG4172 336 IPsegeiRFDGQDLDGLSRRALRP---LRRRMQVVFQDP--FG-----SLSPRMTVGQ-IIAEGLRVHGPGLsaaerrar 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1462 VVKAL------PGGLDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFA------- 1528
Cdd:COG4172 405 VAEALeevgldPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehg 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 1529 --------DRTVV-TIAHRvhtilsadlVMVLKRGAILE-------FDKPE 1563
Cdd:COG4172 477 laylfishDLAVVrALAHR---------VMVMKDGKVVEqgpteqvFDAPQ 518
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
691-888 |
2.01e-12 |
|
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: 67.90 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDpsnperetaadSDARSrgpVA 770
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-----------SIARG---LL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPWLLNA-TVEENITFESPFNKQrykmviEACslqpdIDILPHGDQTQIGERGIN-LSGGQRQRISVARALYQHTN 848
Cdd:cd03231 77 YLGHAPGIKTTlSVLENLRFWHADHSD------EQV-----EEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1274095655 849 VVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 888
Cdd:cd03231 146 LWILDEPTTALDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1344-1553 |
2.32e-12 |
|
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: 68.27 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSS--LKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAKlPLHTLRSRL 1421
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLERPTSGEVLVDGE-PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFS-GTIRFN--LDPEKKCSDSTlwEALEIAQ--LKLVvkalpgGLdaiitEGGENF-----SQGQRQLFCL 1491
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGLELQGVPKA--EARERAEelLELV------GL-----SGFENAyphqlSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1492 ARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILSADLVMVLKR 1553
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
673-912 |
2.87e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.64 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 673 DADNFCVQIiggfftwtpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnSLPDSEGEDPSN 752
Cdd:PRK13548 4 EARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV---RLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 753 PERetaadsdARSRgpvAYASQK-----PWllnaTVEENITF-ESPF--NKQRYKMVIEACSLQPDIDILPHGDQTQige 824
Cdd:PRK13548 72 AEL-------ARRR---AVLPQHsslsfPF----TVEEVVAMgRAPHglSRAEDDALVAAALAQVDLAHLAGRDYPQ--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 825 rginLSGGQRQRISVARALYQHTN------VVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL---- 890
Cdd:PRK13548 135 ----LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLA---H--QHHVLRLARQlaheRGLAVIVVLHDLnlaa 205
|
250 260
....*....|....*....|..
gi 1274095655 891 QYlphADWIIAMKDGTIQREGT 912
Cdd:PRK13548 206 RY---ADRIVLLHQGRLVADGT 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-929 |
3.23e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.40 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWnslpdsEGEDPSNPERetaadSDARSRGPVA 770
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVYL------DGQDIFKMDV-----IELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPwLLNATVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVAR 841
Cdd:PRK14247 88 FQIPNP-IPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDdkRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKD-F 916
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD--MTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREvF 233
|
250
....*....|...
gi 1274095655 917 QRSECQLFEHWKT 929
Cdd:PRK14247 234 TNPRHELTEKYVT 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
683-902 |
3.31e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 69.38 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 683 GGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPSNPERETAADsd 762
Cdd:COG4608 21 GGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF------DGQDITGLSGRELRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 763 ARSR------GPvaYASqkpwlLNA--TVEENItfESPF-------NKQRYKMV---IEACSLQPD-IDILPHgdqtqig 823
Cdd:COG4608 93 LRRRmqmvfqDP--YAS-----LNPrmTVGDII--AEPLrihglasKAERRERVaelLELVGLRPEhADRYPH------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 824 ErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADW 898
Cdd:COG4608 157 E----FSGGQRQRIGIARALALNPKLIVCDEPVSALDV--S---IQAQVLNLLEDLQDelglTYLFISHDLSVVRHiSDR 227
|
....
gi 1274095655 899 IIAM 902
Cdd:COG4608 228 VAVM 231
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1063-1314 |
3.55e-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: 68.72 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1063 YAMVFTVLCSLGIALC-LVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC 1141
Cdd:cd18572 37 RAVLLLLLLSVLSGLFsGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1142 LSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLpllshfAETVEGL-TTIRA 1215
Cdd:cd18572 117 FLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQDaLAEANQV------AEEALSNiRTVRS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1216 F---RYEA-RFQQKLLEYTDSN---NIASLFLTAANRWLevrmEYIGACVVLIAAATSIsnsLHRELSAG-LVGLGLtYA 1287
Cdd:cd18572 191 FateEREArRYERALDKALKLSvrqALAYAGYVAVNTLL----QNGTQVLVLFYGGHLV---LSGRMSAGqLVTFML-YQ 262
|
250 260
....*....|....*....|....*..
gi 1274095655 1288 LMVSNYLNWMVRNLADMEIQLGAVKRI 1314
Cdd:cd18572 263 QQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
696-913 |
3.58e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgedpsnpeRETAADSDARSRgPVAYASQK 775
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK--------LSSAAKAELRNQ-KLGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLL-NATVEENITFESPFNKQRYKMVIEACSlqpdiDILPH-GDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLD 853
Cdd:PRK11629 96 HHLLpDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 854 DPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 913
Cdd:PRK11629 171 EPTGNLDARNADSIFQL-LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1344-1567 |
4.36e-12 |
|
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: 68.15 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKL----------- 1412
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTL----LRAL--------------AGLlkpssgevlld 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1413 --PLHTLRSR-----LSIILQDPVL-FSGTIR--------------FNLDPE-KKCSDSTLwEALEIAQLKlvvkalpgg 1469
Cdd:COG1120 62 grDLASLSRRelarrIAYVPQEPPApFGLTVRelvalgryphlglfGRPSAEdREAVEEAL-ERTGLEHLA--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1470 lDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILS 1544
Cdd:COG1120 132 -DRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARY 204
|
250 260
....*....|....*....|...
gi 1274095655 1545 ADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:COG1120 205 ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
695-891 |
5.18e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.88 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 695 TLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---RVSGAVFWNslpdseGEDPSNPERETAadsdaRSRGPV 769
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsINRMNDLNpevTITGSIVYN------GHNIYSPRTDTV-----DLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLLNATVEENITFESPFN----KQRYKMVIEACSLQPDI-----DILpHgdqtqigERGINLSGGQRQRISVA 840
Cdd:PRK14239 89 GMVFQQPNPFPMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdevkDRL-H-------DSALGLSGGQQQRVCIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 841 RALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELlrDDKRTVVLVTHKLQ 891
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQ 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
699-902 |
5.34e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGED----PSNPERETAADSDARSRGPVAyaSQ 774
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL------GKDllgmKDDEWRAVRSDIQMIFQDPLA--SL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 775 KPWLlnaTVEENI-----TFESPFNKQ----RYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVARALY 844
Cdd:PRK15079 112 NPRM---TIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 845 QHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 902
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
689-915 |
6.48e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSS-------LLLATlgemqrvSGAVFWNSLPDSEGEDPSNPERETAAD- 760
Cdd:PRK13651 16 LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPD-------TGTIEWIFKDEKNKKKTKEKEKVLEKLv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 761 ------------SDARSRGPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLqpDIDILPHGDqt 820
Cdd:PRK13651 89 iqktrfkkikkiKEIRRRVGVVFQFAEYQLFEQTIEKDIIF-GPVSmgvskeeaKKRAAKYIELVGL--DESYLQRSP-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 821 qigergINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWI 899
Cdd:PRK13651 164 ------FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRT 235
|
250 260
....*....|....*....|
gi 1274095655 900 IAMKDGTIQREG----TLKD 915
Cdd:PRK13651 236 IFFKDGKIIKDGdtydILSD 255
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
699-919 |
7.68e-12 |
|
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: 68.60 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN--SLPDSEGEDPSNPERETaadsdarsrgpVAYASQKP 776
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrTLFDSRKGIFLPPEKRR-----------IGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 777 WLL-NATVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHTNVV 850
Cdd:TIGR02142 85 RLFpHLSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 851 FLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1359-1555 |
7.91e-12 |
|
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: 67.96 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1359 PVLKHVNALIAPGQKIGICGRTGSGKSSFslaffRMVDMFEGRIIIDGIDiaklplHTlrSRLSIILQDPVLFSGTIRFN 1438
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSL-----LMLILGELEPSEGKIK------HS--GRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1439 LDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEN- 1517
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 1274095655 1518 ILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGA 1555
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1344-1568 |
8.11e-12 |
|
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: 66.84 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLK--PVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFE-------GRIIIDGIDIAKLPL 1414
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsgsvLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1415 HTLRSRLSIILQDPVLFS-----GTIRFNLD---PEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQR 1486
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1487 QLFCLARAFVRKTSIFIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKP 1562
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 1274095655 1563 EKLLSQ 1568
Cdd:cd03258 226 EEVFAN 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
692-920 |
9.51e-12 |
|
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: 66.69 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDpsnperETAADSDARSRGPVAY 771
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD------GED------ITGLPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLL-NATVEENI----------TFESPFNKQRYKMVIEACSlqpdiDILphgDQTQIGERG----INLSGGQRQR 836
Cdd:cd03219 80 TFQIPRLFpELTVLENVmvaaqartgsGLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 837 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKD 915
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDE 229
|
....*
gi 1274095655 916 FQRSE 920
Cdd:cd03219 230 VRNNP 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1344-1560 |
1.11e-11 |
|
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: 66.00 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPLHtlRS 1419
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLERpdsgEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1420 RLSIILQDPVLFS-----GTIRFNLD----PEKKCSDSTLwEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1490
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKlrgvPKAEIRARVR-ELLELVGLEGLLNRYPHEL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 1491 LARAFVRKTSIFIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFD 1560
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
687-890 |
1.34e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 687 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDpsnpERETAAdsdarSR 766
Cdd:PRK10771 8 TWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN------GQD----HTTTPP-----SR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 767 GPVAYASQKPWLLN-ATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 838
Cdd:PRK10771 71 RPVSMLFQENNLFShLTVAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHKL 890
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDPAL-----RQEMLTLVSQvcQERqlTLLMVSHSL 190
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
694-915 |
1.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.65 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKS-------SLLLATlgemqrvSGAVFwnslpdSEGEDPSNPERETaadsDARSR 766
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKStiakhmnALLIPS-------EGKVY------VDGLDTSDEENLW----DIRNK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 767 GPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 838
Cdd:PRK13633 87 AGMVFQNPDNQIVATIVEEDVAF-GPENlgippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 839 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1344-1565 |
1.66e-11 |
|
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: 65.99 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLA----------FFRMVDMFEGRIIIdgidiak 1411
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLlrLIVgllrpdsgevLIDGEDISGLSEAE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1412 lpLHTLRSRLSIILQDPVLFSG-TIR----FNLDPEKKCSDSTLweaLEIAQLKLVVKALPGGLDAIITEggenFSQGQR 1486
Cdd:cd03261 72 --LYRLRRRMGMLFQSGALFDSlTVFenvaFPLREHTRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE----LSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1487 QLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPE 1563
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
..
gi 1274095655 1564 KL 1565
Cdd:cd03261 223 EL 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
686-915 |
1.89e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNSLpdsegedpsnperETAADSDA 763
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIskILTGLLKPQ--SGEIKIDGI-------------TISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 764 RSRGPVAYASQKP--WLLNATVEENITFeSPFNKQ--RYKM--VIEACSLQPDI-DILPHGDQtqigergiNLSGGQRQR 836
Cdd:PRK13632 80 EIRKKIGIIFQNPdnQFIGATVEDDIAF-GLENKKvpPKKMkdIIDDLAKKVGMeDYLDKEPQ--------NLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 837 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKI-MVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
694-926 |
2.60e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgedpsnperETAADSdarsRGPVAYAS 773
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE---------ETVWDV----RRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKP--WLLNATVEENITF--EspfNKQ--RYKMV------IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 841
Cdd:PRK13635 88 QNPdnQFVGATVQDDVAFglE---NIGvpREEMVervdqaLRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKR-TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKdfqrse 920
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVL--ETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPE------ 225
|
....*.
gi 1274095655 921 cQLFEH 926
Cdd:PRK13635 226 -EIFKS 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1344-1554 |
2.62e-11 |
|
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: 63.96 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdmfegriiidgidiaklplhTLRSRLSI 1423
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTT-----------------------------LIKIILGL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDpvlfSGTIR-FNLDPEKkcsdstlwealEIAQLKLVVKALPGGlDAIITE--GGEN--FSQGQRQLFCLARAFVRK 1498
Cdd:cd03230 50 LKPD----SGEIKvLGKDIKK-----------EPEEVKRRIGYLPEE-PSLYENltVRENlkLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1499 TSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILS-ADLVMVLKRG 1554
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
697-897 |
2.66e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 697 SNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgeMQRVSGAVFWNSLPdsegedpsnperetaadsdaRSRGPVAYASQ 774
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLriLAGL--ARPDAGEVLWQGEP--------------------IRRQRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 775 KPWL--LNA-----TVEENITFespfnkqrykmvieACSLQPDIDilphGDQT-----QIGERGI------NLSGGQRQR 836
Cdd:PRK13538 76 LLYLghQPGiktelTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQRR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 837 ISVARALYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTHklQYLPHAD 897
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH--QDLPVAS 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
829-934 |
3.56e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
90 100
....*....|....*....|....*..
gi 1274095655 908 QREGTLKdfqrsecQLFEHWKTLMNRQ 934
Cdd:PRK11264 223 VEQGPAK-------ALFADPQQPRTRQ 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
689-912 |
3.70e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdsegeDPSNPERETAADSDARSRGP 768
Cdd:PRK13645 20 TPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG--------DYAIPANLKKIKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKP--WLLNATVEENITFeSPFN-----KQRYKMVIEACSLQPdidiLPhgdQTQIGERGINLSGGQRQRISVAR 841
Cdd:PRK13645 92 IGLVFQFPeyQLFQETIEKDIAF-GPVNlgenkQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
698-924 |
4.66e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.28 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnslpdSEGEDpsnperetAADSDARSRGpVAYASQKPW 777
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF------IDGED--------VTHRSIQQRD-ICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 778 LL-NATVEENITF-------ESPFNKQRYKmviEACSLqpdIDILPHGDQ--TQIgerginlSGGQRQRISVARALYQHT 847
Cdd:PRK11432 89 LFpHMSLGENVGYglkmlgvPKEERKQRVK---EALEL---VDLAGFEDRyvDQI-------SGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 848 NVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLF 924
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-929 |
4.69e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAV--FWNSLPdSEGEDPSNPERETaadsdarsrGP 768
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVrlFGRNIY-SPDVDPIEVRREV---------GM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 V-AYASQKPWLlnaTVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRIS 838
Cdd:PRK14267 90 VfQYPNPFPHL---TIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 839 VARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHK-LQYLPHADWIIAMKDGTIQREG-TLK 914
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANI-----DPVGTAKIEELLFELKKeyTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpTRK 234
|
250
....*....|....*
gi 1274095655 915 DFQRSECQLFEHWKT 929
Cdd:PRK14267 235 VFENPEHELTEKYVT 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1344-1538 |
4.70e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.94 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKL-PLHT------ 1416
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRAL--------------AGLwPWGSgrigmp 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1417 LRSRLSIILQDPVLFSGTIRfnldpekkcsdstlwealeiaqlklvvkalpgglDAIITEGGENFSQGQRQLFCLARAFV 1496
Cdd:cd03223 62 EGEDLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1274095655 1497 RKTSIFIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1538
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
698-911 |
5.03e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVF-----WNSLPDSEgedpsnperetaadsdaRSRGPV--A 770
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekrMNDVPPAE-----------------RGVGMVfqS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQkPWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARAL 843
Cdd:PRK11000 84 YALY-PHL---SVAENMSFglklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 911
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1344-1554 |
5.45e-11 |
|
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: 62.97 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG------RIIIDGIDIAKLPLHTL 1417
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAGLEEpdsgsiLIDGEDLTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1418 RSRLSIILQDPVLFSG-TIRFNLdpekkcsdstlwealeiaqlklvvkALPggldaiiteggenFSQGQRQLFCLARAFV 1496
Cdd:cd03229 75 RRRIGMVFQDFALFPHlTVLENI-------------------------ALG-------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 1497 RKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVMVLKRG 1554
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
696-916 |
6.02e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 64.24 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNslpdseGEDPSNPERETAAdsdARSRgpVAYAS 773
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTITVD------GEDLTDSKKDINK---LRRK--VGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QK----PwllNATVEENITfESP-----FNKQrykmviEACSLQpdIDILphgDQTQIGERG----INLSGGQRQRISVA 840
Cdd:COG1126 84 QQfnlfP---HLTVLENVT-LAPikvkkMSKA------EAEERA--MELL---ERVGLADKAdaypAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 916
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELV-----GEVLDVMRDlakEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
696-913 |
6.15e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 62.73 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEmqrvSGAVFWNSlpdsegeDPSNPEREtaadsdarsrgPVAYASQk 775
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLIS-------FLPKFSRN-----------KLIFIDQ- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 pwlLNATVEENITFespfnkqrykmvieacslqpdidiLPHGDQTQigergiNLSGGQRQRISVARALYQHT-NVVF-LD 853
Cdd:cd03238 68 ---LQFLIDVGLGY------------------------LTLGQKLS------TLSGGELQRVKLASELFSEPpGTLFiLD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 854 DPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 913
Cdd:cd03238 115 EPSTGLHQQDINQLL--EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKV 172
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1344-1568 |
7.02e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.82 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVDMF----EGRIIIDGIDIAKLPLHTL-- 1417
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLINGLllpdDNPNSKITVDGITLTAKTVwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1418 -RSRLSIILQDP-VLFSGT-----IRFNLD----PEKKcsdstlwealeiaQLKLVVKALP--GGLDAIITEGgENFSQG 1484
Cdd:PRK13640 82 iREKVGIVFQNPdNQFVGAtvgddVAFGLEnravPRPE-------------MIKIVRDVLAdvGMLDYIDSEP-ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1485 QRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKP 1562
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
....*.
gi 1274095655 1563 EKLLSQ 1568
Cdd:PRK13640 228 VEIFSK 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1344-1562 |
1.10e-10 |
|
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: 63.74 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP---LHTLRSR 1420
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1421 LSIILQDpvlfsgtirFNLDPEK---------KCSDSTLWEAL-------EIAQ----LKLVvkalpgGLDAIITEGGEN 1480
Cdd:cd03256 80 IGMIFQQ---------FNLIERLsvlenvlsgRLGRRSTWRSLfglfpkeEKQRalaaLERV------GLLDKAYQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1481 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILS-ADLVMVLKR 1553
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKD 220
|
....*....
gi 1274095655 1554 GAILeFDKP 1562
Cdd:cd03256 221 GRIV-FDGP 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
696-915 |
1.47e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.91 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNperETAADSDARSRgpVAYASQK 775
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID------GVDITD---KKVKLSDIRKK--VGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 P--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDI--DILPhgdqtqigergINLSGGQRQRISVARAL 843
Cdd:PRK13637 92 PeyQLFEETIEKDIAF-GPINlglseeeiENRVKRAMNIVGLDYEDykDKSP-----------FELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1344-1512 |
1.53e-10 |
|
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: 62.50 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMV----DMFEGRIIIDGIDIAKLPLHtLRS 1419
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1420 RLSIILQDPVLFSG-TIRFNLD-----PEKKCSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLFCLAR 1493
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALAR 144
|
170
....*....|....*....
gi 1274095655 1494 AFVRKTSIFIMDEATASID 1512
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALD 163
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1067-1314 |
1.54e-10 |
|
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: 64.04 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1067 FTVLCSLGIALCLVTSV---TVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1143
Cdd:cd18575 39 FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1144 RSTLLCVSALTVISYVTP---VFLVALLPLAVV-CYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAFRY 1218
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQdRLADLS-----AFAEETLSAIKTVQAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1219 EARFQQKLLEYTDSNniaslfLTAANRWLEVRMEYIGACVVLIAAATS------ISNSLHRELSAGLVGLGLTYALMVSN 1292
Cdd:cd18575 194 EDAERQRFATAVEAA------FAAALRRIRARALLTALVIFLVFGAIVfvlwlgAHDVLAGRMSAGELSQFVFYAVLAAG 267
|
250 260
....*....|....*....|..
gi 1274095655 1293 YLNWMVRNLADMEIQLGAVKRI 1314
Cdd:cd18575 268 SVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1066-1226 |
1.66e-10 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 64.07 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1066 VFTV--LCSLGIALCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1143
Cdd:cd18573 50 VFVVgaAANFGRVYLLRIA------GERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1144 RSTLLCVSALTVISYVTP-VFLVALL---PLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPllshfAETVEGLTTIRAF-- 1216
Cdd:cd18573 124 RSLVSGVGGIGMMLYISPkLTLVMLLvvpPIAVGAVFYGRYVRKLSKQVQDaLADATKVA-----EERLSNIRTVRAFaa 198
|
170
....*....|..
gi 1274095655 1217 -RYE-ARFQQKL 1226
Cdd:cd18573 199 eRKEvERYAKKV 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
689-923 |
1.86e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgedpsnpereTAADSDARS-RG 767
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH----------KTKDKYIRPvRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVAYASQKP--WLLNATVEENITFeSPFNkqrYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARALY 844
Cdd:PRK13646 86 RIGMVFQFPesQLFEDTVEREIIF-GPKN---FKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 845 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSECQL 923
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRL-LKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
689-912 |
2.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAV----FWNSlPDSEGEDPSNPERETAADSDAR 764
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIG-DKKNNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 765 SRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQ 833
Cdd:PRK13631 114 LRRRVSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 834 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagileLLRDDK---RTVVLVTHKL-QYLPHADWIIAMKDGTIQR 909
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-----LILDAKannKTVFVITHTMeHVLEVADEVIVMDKGKILK 256
|
...
gi 1274095655 910 EGT 912
Cdd:PRK13631 257 TGT 259
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
378-610 |
2.01e-10 |
|
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: 63.72 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 378 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYIL 456
Cdd:cd07346 61 YLAARLGQRVVFDLRRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIGALVILFYLN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 457 GVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWE----NIFCSRVEMTRRKEMTS 532
Cdd:cd07346 139 WKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 533 LRAFAVYTSISIFMNTaipIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd07346 219 ARLSALFSPLIGLLTA---LGTALVLLYG-GYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1344-1537 |
2.80e-10 |
|
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: 60.15 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdmfegriiidgidiaklplhtlrsrLSI 1423
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPVLFSGTIRFNldpekkcsdstlwEALEIAQLklvvkalpggldaiiteggENFSQGQRQLFCLARAFVRKTSIFI 1503
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 1274095655 1504 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1537
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
698-915 |
3.28e-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: 63.58 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLL--LATL-----GEMqRVSGAVFWNS-----LPdsegedpsnPERetaadsdars 765
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLraIAGLerpdsGRI-RLGGEVLQDSargifLP---------PHR---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 766 RgPVAYASQK----PWLlnaTVEENITF---ESPFNKQRYKM--VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQR 836
Cdd:COG4148 77 R-RIGYVFQEarlfPHL---SVRGNLLYgrkRAPRAERRISFdeVVELLGIGHLLDRRPA-----------TLSGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 837 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKL---QYLphADWIIAMKDGTIQREGT 912
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDLARKAEILP--YLERLRDELDIpILYVSHSLdevARL--ADHVVLLEQGRVVASGP 217
|
...
gi 1274095655 913 LKD 915
Cdd:COG4148 218 LAE 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1269-1558 |
5.06e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1269 NSLHRELSAGLvglgltyaLMVSNYLNwMVRNLAD--MEIQLGAV---KRIHTLLKTEAESY-EGLLA--PSLIPKNWPD 1340
Cdd:PRK15134 200 RELQQELNMGL--------LFITHNLS-IVRKLADrvAVMQNGRCveqNRAATLFSAPTHPYtQKLLNsePSGDPVPLPE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1341 QGK--IQIQNLSV---------RYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD-----MFEGRIII 1404
Cdd:PRK15134 271 PASplLDVEQLQVafpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINsqgeiWFDGQPLH 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1405 DGIDIAKLPlhtLRSRLSIILQDPvlfSGTIRFNLDPEKkcsdsTLWEALEIAQLKL--------VVKALPG-GLDAII- 1474
Cdd:PRK15134 351 NLNRRQLLP---VRHRIQVVFQDP---NSSLNPRLNVLQ-----IIEEGLRVHQPTLsaaqreqqVIAVMEEvGLDPETr 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1475 ----TEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVHTIL 1543
Cdd:PRK15134 420 hrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY-----LFISHDLHVVR 490
|
330
....*....|....*.
gi 1274095655 1544 S-ADLVMVLKRGAILE 1558
Cdd:PRK15134 491 AlCHQVIVLRQGEVVE 506
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
689-917 |
5.36e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEgedpSNPERETAAdsdARSRGP 768
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS----TSKQKEIKP---VRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLLNATVEENITFeSPFNKQRYKMVIEACSLQpDIDILphGDQTQIGERG-INLSGGQRQRISVARALYQHT 847
Cdd:PRK13643 88 VVFQFPESQLFEETVLKDVAF-GPQNFGIPKEKAEKIAAE-KLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 848 NVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQ 917
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDvFQ 233
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
689-889 |
6.47e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.00 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLATLGEMQRVSGAVFwnSLPdsegedpsnperetaadsdarSRGP 768
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGRL--TKP---------------------AKGK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLLNATVEENITF-ESPFNKQRYKMvieacSLQPDIDILPHGDQTQIGERGIN----------LSGGQRQRI 837
Cdd:TIGR00954 517 LFYVPQRPYMTLGTLRDQIIYpDSSEDMKRRGL-----SDKDLEQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 838 SVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHK 889
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVD-----VEGYMYRLCREFGITLFSVSHR 638
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1344-1569 |
8.31e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------- 1416
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpdvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1417 LRSRLSIILQDPVLFSG-TIRFN----------LDPEKKCSDSTLWeALEIAQLKLVVKALpggldaiITEGGENFSQGQ 1485
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNvaigvklnglVKSKKELDERVEW-ALKKAALWDEVKDR-------LNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1486 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILSADLVMVLKRGAILE------ 1558
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgptrk 234
|
250
....*....|..
gi 1274095655 1559 -FDKPEKLLSQK 1569
Cdd:PRK14267 235 vFENPEHELTEK 246
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1344-1574 |
8.89e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM------------VDMFEGRIIIDgidiaK 1411
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesevrvegrVEFFNQNIYER-----R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1412 LPLHTLRSRLSIILQDPVLFSGTI---------------RFNLDP--EKKCSDSTLWEalEIAQlKLVVKALpggldaii 1474
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVydnvaygvkivgwrpKLEIDDivESALKDADLWD--EIKH-KIHKSAL-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1475 teggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTILS-ADLVM 1549
Cdd:PRK14258 150 -----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQVSRlSDFTA 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 1274095655 1550 VLKR-----GAILEFDKPEKLLSQ------KDSVFA 1574
Cdd:PRK14258 223 FFKGnenriGQLVEFGLTKKIFNSphdsrtREYVLS 258
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
696-926 |
1.02e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERETAAD---------SDArsr 766
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR------GEPLAKLNRAQRKAfrrdiqmvfQDS--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 767 gPVAYASQKP--WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVARAL 843
Cdd:PRK10419 99 -ISAVNPRKTvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRPP-----------QLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 844 YQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLkdfqr 918
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQqfgtACLFITHDLRLVERfCQRVMVMDNGQIVETQPV----- 236
|
....*...
gi 1274095655 919 SECQLFEH 926
Cdd:PRK10419 237 GDKLTFSS 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1344-1556 |
1.39e-09 |
|
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: 58.59 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrLSI 1423
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKS------------------------------TL---MKI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 I--LQDPVlfSGTIRFNldpEKKCSDSTLWEALE-----IAQLklvvkalpggldaiiteggenfSQGQRQLFCLARAFV 1496
Cdd:cd03216 46 LsgLYKPD--SGEILVD---GKEVSFASPRDARRagiamVYQL----------------------SVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 1497 RKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRGAI 1556
Cdd:cd03216 99 RNARLLILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
696-888 |
1.45e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.63 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWNslpdseGEDPSN-PERETAAdsdARSRgpVAY 771
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLL---ERPtSGSVLVD------GVDLTAlSERELRA---ARRK--IGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLLNA-TVEENITFesPF------NKQRYKMVIEACSLqpdIDILPHGDQ--TQigerginLSGGQRQRISVARA 842
Cdd:COG1135 87 IFQHFNLLSSrTVAENVAL--PLeiagvpKAEIRKRVAELLEL---VGLSDKADAypSQ-------LSGGQKQRVGIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1274095655 843 LYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTH 888
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTR-----SILDLLKDINRelglTIVLITH 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1344-1566 |
1.55e-09 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 60.48 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF-SLAFFRM-----------------VDMFEgriiid 1405
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLpptygndvrlfgerrggEDVWE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1406 gidiaklplhtLRSRLSII---LQDPVLFSGTIR-------FnldpekkcsDST-LWEALEIAQLKLVVKALPG-GLDAI 1473
Cdd:COG1119 76 -----------LRKRIGLVspaLQLRFPRDETVLdvvlsgfF---------DSIgLYREPTDEQRERARELLELlGLAHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1474 ItegGENF---SQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILSA- 1545
Cdd:COG1119 136 A---DRPFgtlSQGEQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGi 210
|
250 260
....*....|....*....|.
gi 1274095655 1546 DLVMVLKRGAILEFDKPEKLL 1566
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
696-912 |
1.69e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 60.32 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQRVSGAVFWNSL----PDSEGEDP-SNPER 755
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLEHIDKVividQSPIGRTPrSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 756 ETAADSDARS------RGP--------VAYASQK-PWLLNATVEENITFESPFNKQRYKmvieacsLQPDIDIlphG-DQ 819
Cdd:cd03271 91 YTGVFDEIRElfcevcKGKrynretleVRYKGKSiADVLDMTVEEALEFFENIPKIARK-------LQTLCDV---GlGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 820 TQIGERGINLSGGQRQRISVARALYQ---HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHA 896
Cdd:cd03271 161 IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLE--VLQRLVDKGNTVVVIEHNLDVIKCA 238
|
250 260
....*....|....*....|..
gi 1274095655 897 DWIIAM------KDGTIQREGT 912
Cdd:cd03271 239 DWIIDLgpeggdGGGQVVASGT 260
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
696-920 |
1.77e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.57 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQrvsgavfwnslPDSEGEDPSNPERETAADSDARSRgPVAYASQK 775
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQ-----------PPSEGEILLDAQPLESWSSKAFAR-KVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 -PWLLNATVEENITF-ESP-------FNKQRYKMVIEACSLqpdIDILPhgdqtqIGERGIN-LSGGQRQRISVARALYQ 845
Cdd:PRK10575 94 lPAAEGMTVRELVAIgRYPwhgalgrFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 846 HTNVVFLDDPFSALDV-HLSDHLmqAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:PRK10575 165 DSRCLLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1063-1225 |
2.26e-09 |
|
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: 60.48 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1063 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1142
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1143 SRSTLLCVSALTVISYV----TPVFLVALLPLAVVCYFIQKYFRVASRDL-QQLDDttqlpLLSHFAETVEGLTTIRAFR 1217
Cdd:cd18544 123 IGDLLLLIGILIAMFLLnwrlALISLLVLPLLLLATYLFRKKSRKAYREVrEKLSR-----LNAFLQESISGMSVIQLFN 197
|
....*...
gi 1274095655 1218 YEARFQQK 1225
Cdd:cd18544 198 REKREFEE 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
693-910 |
2.35e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsEGEDPSNPERETAADSDARSRGPVAYA 772
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL------VGQPLHQMDEEARAKLRAKHVGFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 773 SQKPWLLNATveENITFESPFNKQRykmviEACSLQPDIDILphgDQTQIGER----GINLSGGQRQRISVARALYQHTN 848
Cdd:PRK10584 97 FMLIPTLNAL--ENVELPALLRGES-----SRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 849 VVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 910
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADL-LFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
691-920 |
2.66e-09 |
|
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: 59.23 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPsnpereTAADSDARSRGPVA 770
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD------GEDI------TGLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQK----PWLlnaTVEENIT--FESPFNKQRYKMVIEACslqpdIDILPhgdqtQIGER----GINLSGGQRQRISVA 840
Cdd:COG0410 82 YVPEGrrifPSL---TVEENLLlgAYARRDRAEVRADLERV-----YELFP-----RLKERrrqrAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFE--IIRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLAD 226
|
.
gi 1274095655 920 E 920
Cdd:COG0410 227 P 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
691-949 |
3.17e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.36 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWN----------SLPDSEGE---------- 748
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvLRGMDQYEPTSGRIIYHvalcekcgyvERPSKVGEpcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 749 -------DPSNPERetaadsdARSRGPVAYASQKPWLL--NATVEENITfeSPFNKQRYKmviEACSLQPDIDILphgDQ 819
Cdd:TIGR03269 91 peevdfwNLSDKLR-------RRIRKRIAIMLQRTFALygDDTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 820 TQIGER----GINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhLMQAGILELLRDDKRTVVLVTHKLQYLPH 895
Cdd:TIGR03269 156 VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 896 -ADWIIAMKDGTIQREGTLKDFQRSECQLFEhwktlmnrqdqELEKETVMERKAP 949
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEVVAVFMEGVS-----------EVEKECEVEVGEP 278
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
696-911 |
3.95e-09 |
|
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: 58.36 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGqLTMIVGQVGCGKSSLL--LATLgeMQRVSGAVFWNslpdseGEDPSNPERETaadsdarsRGPVAYAS 773
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMriLATL--TPPSSGTIRID------GQDVLKQPQKL--------RRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKP-WLLNATVEENITF-------ESPFNKQRYKMVIEAcslqpdIDILPHGDQtQIGErginLSGGQRQRISVARALYQ 845
Cdd:cd03264 79 QEFgVYPNFTVREFLDYiawlkgiPSKEVKARVDEVLEL------VNLGDRAKK-KIGS----LSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 846 HTNVVFLDDPFSALD----VHLSDHLMQAGilellrdDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 911
Cdd:cd03264 148 DPSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1082-1229 |
4.21e-09 |
|
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: 59.42 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1082 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP 1161
Cdd:cd18576 57 IYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1162 ---VFLVALLP-LAVVCYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAF---RYEA-RFQQKLLEY 1229
Cdd:cd18576 137 kltLLMLATVPvVVLVAVLFGRRIRKLSKKVQdELAEAN-----TIVEETLQGIRVVKAFtreDYEIeRYRKALERV 208
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1090-1226 |
4.21e-09 |
|
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: 59.77 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1090 LKVAKRLHRSLL----NRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPST-LECLSRSTLLCVSALTVISYVTPVFL 1164
Cdd:cd18570 67 LKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1165 VALLPL---AVVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFRYEARFQQKL 1226
Cdd:cd18570 146 ITLLIIplyILIILLFNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKKI 206
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
830-907 |
4.35e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 830 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL---QYLPHAdwIIAM 902
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225
|
....*
gi 1274095655 903 KDGTI 907
Cdd:PRK11701 226 KQGRV 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
688-907 |
4.43e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 58.60 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 688 WTPDGIPT-LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWNslpdseGEDPsnpereTAADSDA 763
Cdd:COG4181 19 GTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLglLAGL---DRPtSGTVRLA------GQDL------FALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 764 RSR------GPVAYASQkpwLLNA-TVEENITFESPFN-----KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSG 831
Cdd:COG4181 84 RARlrarhvGFVFQSFQ---LLPTlTALENVMLPLELAgrrdaRARARALLERVGLGHRLDHYPAQ-----------LSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 832 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQ-----IIDLLFELNRergtTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
830-912 |
5.08e-09 |
|
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: 58.15 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 830 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDG 905
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHG 208
|
....*..
gi 1274095655 906 TIQREGT 912
Cdd:cd03265 209 RIIAEGT 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
696-920 |
5.97e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ--------RVSGAVFWNslpdseGEdpsnPERETAADSDARSRG 767
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN------GE----PLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVAYASQKPWLLnaTVEENITFespfnkQRYKMVIEACSL-QPDIDILPH-----GDQTQIGERGINLSGGQRQRISVAR 841
Cdd:PRK13547 87 VLPQAAQPAFAF--SAREIVLL------GRYPHARRAGALtHRDGEIAWQalalaGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 842 ALYQ---------HTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 911
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLA-HQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVAHG 237
|
....*....
gi 1274095655 912 TLKDFQRSE 920
Cdd:PRK13547 238 APADVLTPA 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
685-907 |
6.03e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.94 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAtlgemqrVSGAVfwnsLPDS-----EGEDPSN-PERETA 758
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA-------IAGSL----PPDSgsiliDGKDVTKlPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 759 ADsdarsrgpVAYASQKPwLL----NATVEENI----------TFESPFNKQRYKMVIEACSlqpDIDI-LPHGDQTQIG 823
Cdd:COG1101 80 KY--------IGRVFQDP-MMgtapSMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLA---TLGLgLENRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 824 ergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagiL--ELLRDDKRTVVLVTHKLQY-LPHADWII 900
Cdd:COG1101 148 ----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRLI 220
|
....*..
gi 1274095655 901 AMKDGTI 907
Cdd:COG1101 221 MMHEGRI 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
829-916 |
6.95e-09 |
|
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: 60.47 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL----QYlphADWII 900
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLgvvrRF---ADRVA 228
|
90
....*....|....*.
gi 1274095655 901 AMKDGTIQREGTLKDF 916
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
696-927 |
7.78e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMQR-----VSGAVFwnslpdsegedpsNPERETAADSDARSRGPV 769
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLrVLNLLEMPRsgtlnIAGNHF-------------DFSKTPSDKAIRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQK----PWLlnaTVEENITfESPFN---------KQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQRQR 836
Cdd:PRK11124 85 GMVFQQynlwPHL---TVQQNLI-EAPCRvlglskdqaLARAEKLLERLRLKPYADRFP-----------LHLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 837 ISVARALYQHTNVVFLDDPFSALD-------VHLSDHLMQAGIlellrddkrTVVLVTHKLQYLPH-ADWIIAMKDGTIQ 908
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETGI---------TQVIVTHEVEVARKtASRVVYMENGHIV 220
|
250
....*....|....*....
gi 1274095655 909 REGTLKDFQRSECQLFEHW 927
Cdd:PRK11124 221 EQGDASCFTQPQTEAFKNY 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1344-1542 |
8.23e-09 |
|
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: 57.42 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP---LHTLRSR 1420
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1421 LSIILQDpvlfsgtirFNLDPEKKCSDSTLWeALEIAQL--KLVVKALPGGLDAIITEGGEN-----FSQGQRQLFCLAR 1493
Cdd:cd03292 80 IGVVFQD---------FRLLPDRNVYENVAF-ALEVTGVppREIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1494 AFVRKTSIFIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRVHTI 1542
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHRVIAL 209
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
696-905 |
1.21e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 57.93 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSL--LLAtlGEMQRVSGAVFWNSLPDSEG-------------EDPS---NPeret 757
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLakMLA--GIIEPTSGEILINGHKLEYGdykyrckhirmifQDPNtslNP---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 758 aadsdarsRGPVAYASQKPWLLNATVEEnitfespfnKQRYKMVIEACS---LQPD-IDILPHgdqtqigergiNLSGGQ 833
Cdd:COG4167 103 --------RLNIGQILEEPLRLNTDLTA---------EEREERIFATLRlvgLLPEhANFYPH-----------MLSSGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 834 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINL-MLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1348-1554 |
1.23e-08 |
|
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: 56.41 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1348 NLSVRYDSSL----KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVdmfEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03213 8 NLTVTVKSSPsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTG---LGVSGEVLINGRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFsgtirfnldpekkcSDSTLWEALEI-AQLKlvvkalpgGLdaiiteggenfSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03213 85 GYVPQDDILH--------------PTLTVRETLMFaAKLR--------GL-----------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1501 IFIMDEATASIDMATENILQKVVMtAFAD--RTVVTIAHRVHTIL--SADLVMVLKRG 1554
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
699-911 |
1.59e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 56.61 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpDSEGEDPSNPEREtaadsdARSRGPVAYASQK--P 776
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKEPAE------ARRRLGFVSDSTGlyD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 777 WLlnaTVEENITFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARALYQHTNV 849
Cdd:cd03266 92 RL---TARENLEYFAGLYglkgdelTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 850 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 911
Cdd:cd03266 158 LLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1344-1558 |
1.67e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRY---DSSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP- 1413
Cdd:PRK10261 314 LQVRNLVTRFplrSGLLNRVTREVHAVekvsfdLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1414 --LHTLRSRLSIILQDPVLfsgtirfNLDPEKKCSDSTLwEALEIAQLkLVVKALPGGLDAIITEGG----------ENF 1481
Cdd:PRK10261 394 gkLQALRRDIQFIFQDPYA-------SLDPRQTVGDSIM-EPLRVHGL-LPGKAAAARVAWLLERVGllpehawrypHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1482 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NI---LQKVVMTAFA----DRTVVT-IAHRVHTILSADLVM 1549
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLlldLQRDFGIAYLfishDMAVVErISHRVAVMYLGQIVE 544
|
....*....
gi 1274095655 1550 VLKRGAILE 1558
Cdd:PRK10261 545 IGPRRAVFE 553
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
696-907 |
1.77e-08 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 55.90 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGED--PSNPeretaadSDARSRGpVAYAS 773
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD------GKPvtRRSP-------RDAIRAG-IAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 ----QKPWLLNATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQHTNV 849
Cdd:cd03215 82 edrkREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 850 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
696-915 |
2.03e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEdpsnpERETaadsdarsRGPVAYASQK 775
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN-----IREV--------RKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 P--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQ 845
Cdd:PRK13652 87 PddQIFSPTVEQDIAF-GPINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 846 HTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEE 224
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
696-902 |
2.04e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 56.50 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL-GEMQR-----VSGAV--FWNSLPDS-----EGEDPS-NPERETAADS 761
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyAEGQRryvesLSAYArqFLGQMDKPdvdsiEGLSPAiAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 762 DARSRGPVAYASQKPWLLNATVeeNItfespfnKQRYKMVIEacslqpdidilphgdqtqIG------ERGIN-LSGGQR 834
Cdd:cd03270 91 PRSTVGTVTEIYDYLRLLFARV--GI-------RERLGFLVD------------------VGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 835 QRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 902
Cdd:cd03270 144 QRIRLATQIgSGLTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
692-954 |
2.31e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.89 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQRVSGAVFWNslpdseGEDPsnpereTAADSDA--RSRGP 768
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrCINLLE-RPTSGRVLVD------GQDL------TALSEKElrKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLLNA-TVEENITFespfnkqrykmvieacSLQpdidiLPHGDQTQIGER--------GI---------NLS 830
Cdd:PRK11153 84 IGMIFQHFNLLSSrTVFDNVAL----------------PLE-----LAGTPKAEIKARvtellelvGLsdkadrypaQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 831 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVIDAG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 906 TIQREGTLKDfqrsecqLFEHWKTLMNRQ------DQELEkETVMERKAPEPSQG 954
Cdd:PRK11153 218 RLVEQGTVSE-------VFSHPKHPLTREfiqstlHLDLP-EDYLARLQAEPTTG 264
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1343-1568 |
2.36e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.33 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1343 KIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVD-MFEGRIIIDGIDIAKLPLHT---LR 1418
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLA----KLLNgLLLPEAGTITVGGMVLSEETvwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1419 SRLSIILQDP-VLFSGT-----IRFNLDpEKKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1492
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGAtvqddVAFGLE-NIGVPREEMVERVDQA-LRQV------GMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1493 RAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQ 1568
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
696-920 |
2.79e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpdsegedPSNPERETAADS-DARSRGPVAYASQ 774
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV------------KIDGELLTAENVwNLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 775 KPWLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHTNVV 850
Cdd:PRK13642 91 DNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDF-----KTREPAR---LSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 851 FLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 920
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRV-IHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSElFATSE 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
698-919 |
3.24e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQrVSGAVFWNSLpDSEGED---PSNPERETAADSDarsrgpVAYASQ 774
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKL-EFNGQDlqrISEKERRNLVGAE------VAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 775 KPWL-LNA--TVEENI-----TFESPFNKQRYKMVIEACSLQ--PD----IDILPHgdqtqigergiNLSGGQRQRISVA 840
Cdd:PRK11022 97 DPMTsLNPcyTVGFQImeaikVHQGGNKKTRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELL----RDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 915
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDV-----TIQAQIIELLlelqQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHD 240
|
....
gi 1274095655 916 FQRS 919
Cdd:PRK11022 241 IFRA 244
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
694-917 |
3.40e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.70 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPsnPERETAADSDARSRGPVAYAS 773
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD------GENI--PAMSRSRLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 qKPWLLNATVEENITF--------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQ 845
Cdd:PRK11831 93 -GALFTDMNVFDNVAYplrehtqlPAPLLHSTVMMKLEAVGLRGAAKLMPS-----------ELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 846 HTNVVFLDDPFSALD-------VHLSDHLMQA-GIlellrddkrTVVLVTHKL-QYLPHAD--WIIAmkDGTIQREGTLK 914
Cdd:PRK11831 161 EPDLIMFDEPFVGQDpitmgvlVKLISELNSAlGV---------TCVVVSHDVpEVLSIADhaYIVA--DKKIVAHGSAQ 229
|
...
gi 1274095655 915 DFQ 917
Cdd:PRK11831 230 ALQ 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
694-920 |
3.59e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnslpdSEGEdpsnperETAADSDARSRGPVAYAS 773
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII------IDGD-------LLTEENVWDIRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKP--WLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHT 847
Cdd:PRK13650 88 QNPdnQFVGATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDF-----KEREPAR---LSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 848 NVVFLDDPFSALDvhlsdhlmQAGILELLRDDKR-------TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRS 919
Cdd:PRK13650 160 KIIILDEATSMLD--------PEGRLELIKTIKGirddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSRG 231
|
.
gi 1274095655 920 E 920
Cdd:PRK13650 232 N 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1344-1581 |
3.60e-08 |
|
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: 56.15 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPVLFSG-TIRFN--LDP--EKkcsdstlWEALEIAQ-----LKLVvkalpgGLDaiITEGGENF----SQGQRQLF 1489
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPklLK-------WPKEKIREradelLALV------GLD--PAEFADRYphelSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1490 CLARAFVRKTSIFIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILSADLVMVLKRGAILEFDKP 1562
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTP 220
|
250 260
....*....|....*....|
gi 1274095655 1563 EKLL-SQKDSVFASFVRADK 1581
Cdd:cd03295 221 DEILrSPANDFVAEFVGADR 240
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1363-1556 |
3.85e-08 |
|
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: 55.58 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1363 HVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAKLPLHTLRSR--LSIILQDPVLFSG-TIRFNL 1439
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL----LNLIAGFETPQSGRVLINGVDVTAAPPADrpVSMLFQENNLFAHlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1440 D----PEKKCSdstlwealEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1515
Cdd:cd03298 92 GlglsPGLKLT--------AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1274095655 1516 ENILQKVVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRGAI 1556
Cdd:cd03298 164 RAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-912 |
4.08e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ----RVSGAVFWNslpdseGEDpsnperetAADSDA-RSRGP 768
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYdskiKVDGKVLYF------GKD--------IFQIDAiKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKP-WLLNATVEENITFesPF------NKQRYKMVIEACSLQPDIDILPHgdqTQIGERGINLSGGQRQRISVAR 841
Cdd:PRK14246 92 VGMVFQQPnPFPHLSIYDNIAY--PLkshgikEKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELlrDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 912
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDI-VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1344-1537 |
5.09e-08 |
|
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: 55.19 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrL 1421
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS------------------------------TL---L 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SII--LQDPVlfSGTIRFNLDPEKKCSDSTLWE--------------------ALEIAQLKLVVKALPG----------- 1468
Cdd:cd03255 48 NILggLDRPT--SGEVRVDGTDISKLSEKELAAfrrrhigfvfqsfnllpdltALENVELPLLLAGVPKkerreraeell 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 1469 ---GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAH 1537
Cdd:cd03255 126 ervGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTH 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
696-912 |
5.27e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQRvsGAVFWNSLPDSEGEDpsnperetaADSDARSRGPVAYAS 773
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMvrLLNRLIEPTR--GQVLIDGVDIAKISD---------AELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLL-NATVEENITFESPFN----KQRYKMVIEACSlQPDIDILPHGDQTQigerginLSGGQRQRISVARALYQHTN 848
Cdd:PRK10070 113 QSFALMpHMTVLDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 849 VVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
691-906 |
5.97e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 53.22 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSlpdsegedpsnperetaadsdarsRGPVA 770
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVV 850
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 851 FLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGT 906
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEA-----LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1344-1537 |
6.57e-08 |
|
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: 54.84 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDpvlfsgtirFNLDPE--------------KKCSDStlwEALEIAQ--LKLVvkalpgGLDAIITEGGENFSQGQ 1485
Cdd:cd03262 79 GMVFQQ---------FNLFPHltvlenitlapikvKGMSKA---EAEERALelLEKV------GLADKADAYPAQLSGGQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 1486 RQLFCLARAFVRKTSIFIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAH 1537
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTH 193
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1344-1557 |
6.64e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 55.07 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdmfegriiidgidiaklplhTLRSRL 1421
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTT-----------------------------TLRMLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDP--VLFSGtIRFNLDP-EKK-----CSDS-------TLWEALEI---------AQLKLVVKALPGGLD--AIIT 1475
Cdd:cd03266 53 GLLEPDAgfATVDG-FDVVKEPaEARrrlgfVSDStglydrlTARENLEYfaglyglkgDELTARLEELADRLGmeELLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1476 EGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKR 1553
Cdd:cd03266 132 RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHR 211
|
....
gi 1274095655 1554 GAIL 1557
Cdd:cd03266 212 GRVV 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
696-890 |
6.89e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSL--LLAtlGEMQRVSGAVFWNslpdseGE--DPSNPeretaadSDARSRGpVAY 771
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLmkILY--GLYQPDSGEILID------GKpvRIRSP-------RDAIALG-IGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLLNA-TVEENI------TFESPFNKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISVARALY 844
Cdd:COG3845 85 VHQHFMLVPNlTVAENIvlglepTKGGRLDRKAARARIRELSERYGLDVDPD---AKVED----LSVGEQQRVEILKALY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1274095655 845 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL 890
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKL 201
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1572 |
8.30e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.53 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPV-LFSGTI-----RFNLD----PEKKCSdSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLAR 1493
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLEnhavPYDEMH-RRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1494 AFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDS 1571
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
.
gi 1274095655 1572 V 1572
Cdd:PRK13648 236 L 236
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
691-860 |
8.74e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLA---TLGEMQRVSGAVFWNSLPdsegedpsnperetAADSDARSRG 767
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYNGIP--------------YKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVAYASQK----PWLlnaTVEENITFespfnkqrykmvieACSLQpdidilphGDQTQigeRGInlSGGQRQRISVARAL 843
Cdd:cd03233 84 EIIYVSEEdvhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEAL 133
|
170
....*....|....*..
gi 1274095655 844 YQHTNVVFLDDPFSALD 860
Cdd:cd03233 134 VSRASVLCWDNSTRGLD 150
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1358-1569 |
9.30e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.05 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1358 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIA------KLPLHTLRSRLSIILQDPVLF 1431
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1432 SG-TIRFNLD-PEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1509
Cdd:PRK14246 103 PHlSIYDNIAyPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1510 SIDMATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILE-------FDKPEKLLSQK 1569
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKNELTEK 250
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
829-911 |
9.92e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.71 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
|
....
gi 1274095655 908 QREG 911
Cdd:PRK09493 215 AEDG 218
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
696-912 |
1.10e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.95 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQRVSGA------VFWNSLPdsEGEDP-SNP 753
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanrlngaktvpGRYTSIEGLehldkvIHIDQSP--IGRTPrSNP 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 754 ERET----------AADSDARSRGpvaYaSQKPWLLNA--------------TVEEN------ITFES----PFNKQ--- 796
Cdd:TIGR00630 702 ATYTgvfdeirelfAETPEAKVRG---Y-TPGRFSFNVkggrceacqgdgviKIEMHflpdvyVPCEVckgkRYNREtle 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 797 -RYK---------MVI-EACSLQPDIDILPHGDQT---------QIGERGINLSGGQRQRISVARALYQ---HTNVVFLD 853
Cdd:TIGR00630 778 vKYKgkniadvldMTVeEAYEFFEAVPSISRKLQTlcdvglgyiRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILD 857
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 854 DPFSALdvHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPHADWII------AMKDGTIQREGT 912
Cdd:TIGR00630 858 EPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTVVASGT 920
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1344-1558 |
1.15e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.29 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSF---------------SLAFFRMVDMfegriiidgiD 1408
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLlkllygeerptsgqvLVNGQDLSRL----------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1409 IAKLPLhtLRSRLSIILQDpvlfsgtirFNLDPEKkcsdsTLWE----ALEIAQ-------------LKLV-----VKAL 1466
Cdd:COG2884 71 RREIPY--LRRRIGVVFQD---------FRLLPDR-----TVYEnvalPLRVTGksrkeirrrvrevLDLVglsdkAKAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1467 PGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTI 1542
Cdd:COG2884 135 PHEL-----------SGGEQQRVAIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELV 200
|
250
....*....|....*..
gi 1274095655 1543 LSADL-VMVLKRGAILE 1558
Cdd:COG2884 201 DRMPKrVLELEDGRLVR 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
688-909 |
1.21e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 54.86 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 688 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATL------GEMQrVSGaVFWNSLPDSEGedpsnperetaads 761
Cdd:cd03289 12 YTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQ-IDG-VSWNSVPLQKW-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 762 darsRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 841
Cdd:cd03289 76 ----RKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 842 ALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQR 909
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
692-911 |
1.31e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEdpsnpERETAADSDARSRGpVAY 771
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID------GQ-----EMRFASTTAALAAG-VAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLL-NATVEENI---TFESPFNKQRYKMVIEACSLQPD---IDILPhgdQTQIGErginLSGGQRQRISVARALY 844
Cdd:PRK11288 84 IYQELHLVpEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEhlgVDIDP---DTPLKY----LSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 845 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLqylphaDWIIAMKDG-TIQREG 911
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1091-1225 |
1.41e-07 |
|
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: 55.10 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1091 KVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-LVALL- 1168
Cdd:cd18547 75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtLIVLVt 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 1169 -PLAVVC-YFI----QKYFRVASRDLQQLDdttqlpllSHFAETVEGLTTIRAFRYEARFQQK 1225
Cdd:cd18547 155 vPLSLLVtKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEE 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
689-920 |
1.80e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnSLPDSEgedpsnpERETAADSDARS-RG 767
Cdd:PRK13649 16 TPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV---RVDDTL-------ITSTSKNKDIKQiRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVAYASQKP--WLLNATVEENITFeSPFNKQRYKmvIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 845
Cdd:PRK13649 86 KVGLVFQFPesQLFEETVLKDVAF-GPQNFGVSQ--EEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 846 HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRSE 920
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDiFQDVD 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1344-1570 |
1.92e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.35 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVD-MFEGRIIIDGIDIAKLPLHT---LR 1418
Cdd:PRK13650 5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDgLLEAESGQIIIDGDLLTEENvwdIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1419 SRLSIILQDP-VLFSGT-----IRFNLDpEKKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1492
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGAtveddVAFGLE-NKGIPHEEMKERVNEA-LELV------GMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1493 RAFVRKTSIFIMDEATASID--------MATENILQKVVMtafadrTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEK 1564
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQM------TVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
....*.
gi 1274095655 1565 LLSQKD 1570
Cdd:PRK13650 227 LFSRGN 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
693-919 |
2.59e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDPSNPERETAADSDARSRGP-VAY 771
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRGAdMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWL-LNA--TVEENITfESPFNKQ---RYKMVIEACSLQPDIDIlPHGdQTQIGERGINLSGGQRQRISVARALYQ 845
Cdd:PRK10261 109 IFQEPMTsLNPvfTVGEQIA-ESIRLHQgasREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 846 HTNVVFLDDPFSALDVhlsdhLMQAGILELLR----DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:PRK10261 186 RPAVLIADEPTTALDV-----TIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
696-941 |
3.37e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.69 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWNS------LPDSEGEDPSNPERETAADSDARSRG 767
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLkiLA--GELEPDSGEVSIPKglrigyLPQEPPLDDDLTVLDTVLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 768 PVA---YASQKPWLLNATVEENITFESPFNkqrykmVIEACSLQPDIDI------LPHGDQTQ-IGErginLSGGQRQRI 837
Cdd:COG0488 92 LEAeleELEAKLAEPDEDLERLAELQEEFE------ALGGWEAEARAEEilsglgFPEEDLDRpVSE----LSGGWRRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 838 SVARALYQHTNVVFLDDPFSALDVHlsdhlmqaGIL---ELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ 908
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLE--------SIEwleEFLKNYPGTVLVVSHdryfldRV-----ATRILELDRGKLT 228
|
250 260 270
....*....|....*....|....*....|....
gi 1274095655 909 R-EGTLKDFQRSECQLFEHWKTLMNRQDQELEKE 941
Cdd:COG0488 229 LyPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKE 262
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
694-918 |
4.73e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEM----QRVSGAVFWNSLPdsegedpsnperetAADSDARSRgPV 769
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKP--------------VAPCALRGR-KI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPwllnatveenitfESPFNKQRyKM---VIEAC---SLQPDIDILPH-------GDQTQIGER-GINLSGGQRQ 835
Cdd:PRK10418 82 ATIMQNP-------------RSAFNPLH-TMhthARETClalGKPADDATLTAaleavglENAARVLKLyPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 836 RISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRT----VVLVTHKLQYLPH-ADWIIAMKDGTIQRE 910
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDV-----VAQARILDLLESIVQKralgMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
....*....
gi 1274095655 911 GTLKD-FQR 918
Cdd:PRK10418 223 GDVETlFNA 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
829-915 |
4.81e-07 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 52.78 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP----HAdwiIAMKD 904
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL-LDKLAAEGAPTLVLVTHHVEEIPpgitHV---LLLKD 218
|
90
....*....|.
gi 1274095655 905 GTIQREGTLKD 915
Cdd:COG1119 219 GRVVAAGPKEE 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1361-1567 |
4.82e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.88 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1361 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRS----RLSIILQDpvlfsgtir 1436
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1437 FNLDPEKKCSDSTLWeALEIAQLKLVVKAlPGGLDAIITEGGENF--------SQGQRQLFCLARAFVRKTSIFIMDEAT 1508
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 1509 ASID--MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1344-1567 |
5.09e-07 |
|
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: 54.42 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFsLAFFRMVDMFEGRIIIDGIDIAKLP---------- 1413
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEPTSGRIIYHVALCEkcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1414 --------------------------LHTLRSRLSIILQDPvlfsgtirFNLDPEKKCSDSTLwEALEIAQLKlVVKALP 1467
Cdd:TIGR03269 78 vgepcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRT--------FALYGDDTVLDNVL-EALEEIGYE-GKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1468 GGLDAI--------ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH 1537
Cdd:TIGR03269 148 RAVDLIemvqlshrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSH 227
|
250 260 270
....*....|....*....|....*....|.
gi 1274095655 1538 RVHTILS-ADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:TIGR03269 228 WPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1343-1565 |
7.74e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1343 KIQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIdgidiAKLPLH------- 1415
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVE-----GKVTFHgknlyap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1416 -----TLRSRLSIILQDPVLFSGTI-------------RFNLDP--EKKCSDSTLWEALEiAQLKlvvkalpggldaiit 1475
Cdd:PRK14243 83 dvdpvEVRRRIGMVFQKPNPFPKSIydniaygaringyKGDMDElvERSLRQAALWDEVK-DKLK--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1476 EGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVHTI---LSAD 1546
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMtafFNVE 226
|
250 260
....*....|....*....|
gi 1274095655 1547 LVMVLKR-GAILEFDKPEKL 1565
Cdd:PRK14243 227 LTEGGGRyGYLVEFDRTEKI 246
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
696-905 |
8.11e-07 |
|
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: 51.51 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPdsegedpsnperetaADSDARSRgpVAYASQK 775
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP---------------LDIAARNR--IGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWL-LNATVEENITFESpfnkQRYKMVIEACSLQPD-----IDILPHGDQtQIGErginLSGGQRQRISVARALYQHTNV 849
Cdd:cd03269 79 RGLyPKMKVIDQLVYLA----QLKGLKKEEARRRIDewlerLELSEYANK-RVEE----LSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 850 VFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDV-IRE-LARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
829-912 |
9.55e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTI 907
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
....*
gi 1274095655 908 QREGT 912
Cdd:PRK11650 214 EQIGT 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
691-911 |
9.80e-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: 50.99 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEM--QRVSGAVFWnslpdsEGEDpsnperetaadsdarsrgp 768
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILF------KGED------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 vayasqkpwLLNATVEEN------ITFESPfnkqrykMVIEACSLqpdIDILphgdqtqigeRGIN--LSGGQRQRISVA 840
Cdd:cd03217 66 ---------ITDLPPEERarlgifLAFQYP-------PEIPGVKN---ADFL----------RYVNegFSGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 841 RALYQHTNVVFLDDPFSALDVhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADWIIAMKDGTIQREG 911
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSG 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
830-893 |
1.01e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 1.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 830 SGGQRQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRtvvlvTHKLQYL 893
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSL-----DKTVQAQILALLKSLQQ-----KHQLAYL 480
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1344-1572 |
1.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYD-SSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 1422
Cdd:PRK13642 5 LEVENLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1423 IILQDP------VLFSGTIRFNLDPEKKCSDSTLweaLEIAQLKLVVKALPggldaIITEGGENFSQGQRQLFCLARAFV 1496
Cdd:PRK13642 85 MVFQNPdnqfvgATVEDDVAFGMENQGIPREEMI---KRVDEALLAVNMLD-----FKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 1497 RKTSIFIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSV 1572
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
692-920 |
1.32e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQRVSGAVfwnsLPDSeGEDPSNPERET-AADSDARSRGpVA 770
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTL-------MKIIAGIV----PPDS-GTLEIGGNPCArLTPAKAHQLG-IY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 771 YASQKPWLL-NATVEENITFESPFNKQRYKMVIE-----ACSLQPDIdilphgdqtQIGergiNLSGGQRQRISVARALY 844
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDS---------SAG----SLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 845 QHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDD 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
691-918 |
1.55e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.76 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQrvsgavfwnslPDSeGEdpsnperetaadsdaRSRGP-- 768
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE-----------PDS-GT---------------VKLGEtv 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 -VAYASQKPWLL--NATVEENItfeSPFNKQRYKMVIEACsLQpdiDILPHGDQ--TQIGergiNLSGGQRQRISVARAL 843
Cdd:COG0488 379 kIGYFDQHQEELdpDKTVLDEL---RDGAPGGTEQEVRGY-LG---RFLFSGDDafKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 844 YQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ-REGTLKDF 916
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHdryfldRV-----ATRILEFEDGGVReYPGGYDDY 517
|
..
gi 1274095655 917 QR 918
Cdd:COG0488 518 LE 519
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
644-890 |
1.96e-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: 53.09 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 644 KVVNRKRPAREEVRDLLGP-------LQRLTPsmdGDADNFCVQIIGGFFTwtPDGIPTLSNITIRIPRGQLTMIVGQVG 716
Cdd:TIGR01257 892 RALEKTEPLTEEMEDPEHPegindsfFERELP---GLVPGVCVKNLVKIFE--PSGRPAVDRLNITFYENQITAFLGHNG 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 717 CGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPsnperETAADSDARSRGpvaYASQKPWLLN-ATVEENITFESPFNK 795
Cdd:TIGR01257 967 AGKTTTLSILTGLLPPTSGTVLVG------GKDI-----ETNLDAVRQSLG---MCPQHNILFHhLTVAEHILFYAQLKG 1032
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 796 QRYkmviEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILEL 875
Cdd:TIGR01257 1033 RSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY-----SRRSIWDL 1103
|
250
....*....|....*..
gi 1274095655 876 LRDDK--RTVVLVTHKL 890
Cdd:TIGR01257 1104 LLKYRsgRTIIMSTHHM 1120
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
691-905 |
2.04e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQRVSGAVFWNSLpdsEGEDPSNPERETAAD-SDARSRGpV 769
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTL-------MKVLSGVYPHGTY---EGEIIFEGEELQASNiRDTERAG-I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPWLL-NATVEENItF---E-SPFNKQRY-KMVIEACSL--QPDIDILPHgdqTQIGergiNLSGGQRQRISVAR 841
Cdd:PRK13549 85 AIIHQELALVkELSVLENI-FlgnEiTPGGIMDYdAMYLRAQKLlaQLKLDINPA---TPVG----NLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHLSDHLmqagiLELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVL-----LDIIRDLKAhgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1058-1245 |
2.06e-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: 51.27 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1058 LDQSVYAMVFTVLCSLGIALCL------VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTI 1131
Cdd:cd18554 37 LDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1132 DQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVA---LLPLAVVC-YFIQKYFRVASRDLQQLDDTTQlpllSHFAETV 1207
Cdd:cd18554 117 KDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFYILAvKYFFGRLRKLTKERSQALAEVQ----GFLHERI 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 1274095655 1208 EGLTTIRAFRYEARFQQkllEYTDSNNiasLFLTAANR 1245
Cdd:cd18554 193 QGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
693-891 |
2.11e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 50.79 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPSNPERETAAdsdarsRGPVAYA 772
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA------GLVPWKRRKKFLR------RIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 773 --SQKPWLLNA----TVEENITFESPFnkqRYKMVIEACSlqpdiDILPHGDQTQIGERgiNLSGGQRQRISVARALYQH 846
Cdd:cd03267 102 qkTQLWWDLPVidsfYLLAAIYDLPPA---RFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1274095655 847 TNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQ 891
Cdd:cd03267 172 PEILFLDEPTIGLDVV-AQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1346-1387 |
2.15e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.37 E-value: 2.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1274095655 1346 IQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1387
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL 40
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
705-888 |
2.17e-06 |
|
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: 48.91 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 705 RGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDPSNPEretaadsdarsrgpvayasqkpwllnatve 784
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 785 enitfespfnkqrykmvieacslqpdidilphgdQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLS 864
Cdd:smart00382 51 ----------------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
170 180
....*....|....*....|....*...
gi 1274095655 865 DHLMQAGILELL----RDDKRTVVLVTH 888
Cdd:smart00382 97 ALLLLLEELRLLlllkSEKNLTVILTTN 124
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1358-1567 |
2.21e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1358 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------LRSRLSIILQDPVLF 1431
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyrdvleFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1432 SGTIRFN---------LDPEKkcsdstlwEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 1502
Cdd:PRK14271 114 PMSIMDNvlagvrahkLVPRK--------EFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1503 IMDEATASIDMATENILQKVVMTaFADR-TVVTIAHRV-HTILSADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
703-899 |
2.25e-06 |
|
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: 50.83 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 703 IPR-GQLTMIVGQVGCGKSSLLLATLGEMQ----RVSGAVFWNSLPD----SEGEDpsnpERETAADSDARSRGPVAYAS 773
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKpnlgKFDDPPDWDEILDefrgSELQN----YFTKLLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 QKPWLLNATVEENITFESPFNKQRYkmVIEACSLQPdidilphgdqtqIGERGI-NLSGGQRQRISVARALYQHTNVVFL 852
Cdd:cd03236 98 LIPKAVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1274095655 853 DDPFSALDVHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWI 899
Cdd:cd03236 164 DEPSSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
696-888 |
2.31e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.34 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDpsnperETAADSDARsRGPVAYASQk 775
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGRE------ASLIDAIGR-KGDFKDAVE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 pwLLNAT-VEENITFESPFNkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLDD 854
Cdd:COG2401 118 --LLNAVgLSDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 1274095655 855 PFSALDVHLSdHLMQAGILELLRDDKRTVVLVTH 888
Cdd:COG2401 163 FCSHLDRQTA-KRVARNLQKLARRAGITLVVATH 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1579 |
2.72e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.89 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDP--VLFSGTI-------RFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARA 1494
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1495 FVRKTSIFIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEkLLSQ 1568
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTD 227
|
250
....*....|.
gi 1274095655 1569 KDSVFASFVRA 1579
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
829-905 |
2.74e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 903
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 1274095655 904 DG 905
Cdd:PRK15134 232 NG 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
691-905 |
2.81e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWnslpdsEGEdpsnpERETAADSDARSRGP 768
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYW------SGS-----PLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 769 VAYASQKPWLLNATVEENI----TFESPFNKQRYKMVIEACS---LQPDIDILPhgDQTQIGERGinlsGGQRQRISVAR 841
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKnllRELQLDADN--VTRPVGDYG----GGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETE-----ILLDIIRDLKAhgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
706-915 |
2.94e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.56 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 706 GQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSLPDSEGEDPSNPERETAADSD-ARSRGPVAYASQkpwLLNATVE 784
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpSTSLNPRQRISQ---ILDFPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 785 ENITFESPFNKQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHL 863
Cdd:PRK15112 116 LNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 864 SDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 915
Cdd:PRK15112 185 RSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1479-1577 |
3.27e-06 |
|
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: 50.03 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVMVLKRG 1554
Cdd:cd03299 128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNG 206
|
90 100
....*....|....*....|....
gi 1274095655 1555 AILEFDKPEKLLSQKDSVF-ASFV 1577
Cdd:cd03299 207 KLIQVGKPEEVFKKPKNEFvAEFL 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1344-1537 |
4.04e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.16 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------- 1416
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSprtdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1417 LRSRLSIILQDPVLFSGTI--------RFNLDPEKKCSDSTLWEALEIAQLKLVVKAlpggldaIITEGGENFSQGQRQL 1488
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1274095655 1489 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1537
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
696-888 |
4.80e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.20 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATlgeMQRvsgavfwnSLPDSEGeDPS---NPERETAADSDARSrgpvAYA 772
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL---AFR--------SPKGVKG-SGSvllNGMPIDAKEMRAIS----AYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 773 SQKPWLLNA-TVEENITFESPF----------NKQRYKMVIEACSLQPDIDILphgdqTQIGERGINLSGGQRQRISVAR 841
Cdd:TIGR00955 105 QQDDLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCANTR-----IGVPGRVKGLSGGERKRLAFAS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTH 888
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1067-1572 |
5.12e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1067 FTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID---QHIPStlecLS 1143
Cdd:PRK10522 54 FLGLLLLLMAVTLGSQLALTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITiafVRLPE----LV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1144 RSTLLCVSALTVISYVTP-VFLVALLPLAVVcyFIQKYFRVAS-----RDLQQLDDTtqlpLLSHFAETVEG-----LTT 1212
Cdd:PRK10522 130 QGIILTLGSAAYLAWLSPkMLLVTAIWMAVT--IWGGFVLVARvykhmATLRETEDK----LYNDYQTVLEGrkeltLNR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1213 IRA-FRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMeyigacvvliaaatsisnslhrelsAGLVGLgltyALMVS 1291
Cdd:PRK10522 204 ERAeYVFENEYEPDAQEYRHHIIRADTFHLSAVNWSNIMM-------------------------LGAIGL----VFYMA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1292 NYLNWmvrnlADMEIQ--------------LGAVKRIHTLL----------KTEAESYEGLLAPSLIPKNWPdqgKIQIQ 1347
Cdd:PRK10522 255 NSLGW-----ADTNVAatysltllflrtplLSAVGALPTLLsaqvafnklnKLALAPYKAEFPRPQAFPDWQ---TLELR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1348 NLSVRYDS---SLKPVlkhvNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSII 1424
Cdd:PRK10522 327 NVTFAYQDngfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1425 LQDPVLFSGTirfnLDPEKKCSDSTLWEA-LEIAQLKlvvkalpgglDAIITEGGE----NFSQGQRQLFCLARAFVRKT 1499
Cdd:PRK10522 403 FTDFHLFDQL----LGPEGKPANPALVEKwLERLKMA----------HKLELEDGRisnlKLSKGQKKRLALLLALAEER 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 1500 SIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSV 1572
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1268-1568 |
5.16e-06 |
|
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: 50.96 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1268 SNSLHRELSAGLVGLGLTyaLMVSNYLNWMVRNLADMEIQL--GAVKRIHTLLKTEAESYEGllAPSLIPKNWPDQGK-- 1343
Cdd:TIGR03269 204 AKLVHNALEEAVKASGIS--MVLTSHWPEVIEDLSDKAIWLenGEIKEEGTPDEVVAVFMEG--VSEVEKECEVEVGEpi 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPVLKHVNAL---IAPGQKIGICGRTGSGKSSFS--LA----------FFRM----VDMFEgriii 1404
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSkiIAgvleptsgevNVRVgdewVDMTK----- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1405 dgidiaklPLHTLRSR----LSIILQDPVLFsgtirfnldPEKKCSDStLWEAL------EIAQLKLVVKALPGGLD--- 1471
Cdd:TIGR03269 355 --------PGPDGRGRakryIGILHQEYDLY---------PHRTVLDN-LTEAIglelpdELARMKAVITLKMVGFDeek 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1472 --AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-AD 1546
Cdd:TIGR03269 417 aeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCD 496
|
330 340
....*....|....*....|..
gi 1274095655 1547 LVMVLKRGAILEFDKPEKLLSQ 1568
Cdd:TIGR03269 497 RAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1069-1239 |
5.97e-06 |
|
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: 50.10 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1069 VLCSLGIALCLVTS-VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTL 1147
Cdd:cd18541 47 LLLALLIGIFRFLWrYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1148 LCVSALTVISYVTPVF-LVALLPL---AVVCYFIQKYFRVASRDLQQ----LDDTTQlpllshfaETVEGLTTIRAF--- 1216
Cdd:cd18541 127 LGVLVLVMMFTISPKLtLIALLPLpllALLVYRLGKKIHKRFRKVQEafsdLSDRVQ--------ESFSGIRVIKAFvqe 198
|
170 180
....*....|....*....|....*...
gi 1274095655 1217 -RYEARFQQKLLEYTDSNN----IASLF 1239
Cdd:cd18541 199 eAEIERFDKLNEEYVEKNLrlarVDALF 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
693-912 |
6.52e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.11 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSlPDSEGEDPSNPERETAAdsdARSRGPVAYA 772
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG-KDITDWQTAKIMREAVA---IVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 773 SQkpwllnaTVEENITFESPF-NKQRYKMVIEACslqpdIDILPHGDQTQIgERGINLSGGQRQRISVARALYQHTNVVF 851
Cdd:PRK11614 94 RM-------TVEENLAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 852 LDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFD--TIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
696-915 |
6.66e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.83 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpDSEGEDpSNPERETAADSDARSRGPVAYASQK 775
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI------TIAGYH-ITPETGNKNLKKLRKKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALYQHT 847
Cdd:PRK13641 96 AQLFENTVLKDVEF-GPKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 848 NVVFLDDPFSALDVHLSDHLMQagileLLRDDKR---TVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQ-----LFKDYQKaghTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKE 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
683-881 |
8.35e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 683 GGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN-----SLPDSEGE----DPSNP 753
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridTLSPGKLQalrrDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 754 ERETAADSDARSrgPVAYASQKPWLLNATVEENITfespfnKQRYKMVIEACSLQPDIDI-LPHgdqtqigergiNLSGG 832
Cdd:PRK10261 407 FQDPYASLDPRQ--TVGDSIMEPLRVHGLLPGKAA------AARVAWLLERVGLLPEHAWrYPH-----------EFSGG 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1274095655 833 QRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR 881
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSI-----RGQIINLLLDLQR 511
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1344-1567 |
9.60e-06 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 48.58 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTlRSRLSI 1423
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 IL--QDPVLFSG-TIRfnldpekkcsdstlwEALEIAQLKLVVKALPGGLDAII-----------TEGGeNFSQGQRQLF 1489
Cdd:cd03224 78 GYvpEGRRIFPElTVE---------------ENLLLGAYARRRAKRKARLERVYelfprlkerrkQLAG-TLSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1490 CLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1344-1574 |
9.63e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.70 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYD------------SSLKPVlKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAK 1411
Cdd:PRK15079 9 LEVADLKVHFDikdgkqwfwqppKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1412 L---PLHTLRSRLSIILQDPvLFSgtirfnLDPEKKCSD------STLWEALEIAQLKLVVKAL---PGGLDAIITEGGE 1479
Cdd:PRK15079 88 MkddEWRAVRSDIQMIFQDP-LAS------LNPRMTIGEiiaeplRTYHPKLSRQEVKDRVKAMmlkVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1480 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHR---VHTIlsADLVMVLK 1552
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNLLQQ--LQREMGLSLIFIAHDlavVKHI--SDRVLVMY 236
|
250 260
....*....|....*....|..
gi 1274095655 1553 RGAILEfdkpeklLSQKDSVFA 1574
Cdd:PRK15079 237 LGHAVE-------LGTYDEVYH 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
692-915 |
1.03e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdsegedpsNPERETAADSDARSRGpVAY 771
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-----------NINYNKLDHKLAAQLG-IGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLLNA-TVEENI--------------TFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQR 836
Cdd:PRK09700 85 IYQELSVIDElTVLENLyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 837 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 915
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSD 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1344-1387 |
1.14e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.06 E-value: 1.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1387
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1082-1302 |
1.28e-05 |
|
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: 49.00 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1082 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP 1161
Cdd:cd18545 61 IYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1162 VF-LVAL--LP-LAVVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYE----ARFQQKLLEYTDSN 1233
Cdd:cd18545 141 RLaLVTLavLPlLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSFAREdeneEIFDELNRENRKAN 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 1234 NIASLFLTAANRWLEVrMEYIGACVVLIAAATSIsnsLHRELSAGLVGLGLTYA-------LMVSNYLNWMVRNLA 1302
Cdd:cd18545 217 MRAVRLNALFWPLVEL-ISALGTALVYWYGGKLV---LGGAITVGVLVAFIGYVgrfwqpiRNLSNFYNQLQSAMA 288
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1057-1242 |
1.40e-05 |
|
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: 48.64 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1057 ALDQSVYAMVFTVL--CSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILA--------PMRFFETTPLGSILNRFSS 1126
Cdd:cd18546 25 GIDSGVRAGDLGVLllAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRvfahlqrlSLDFHERETSGRIMTRMTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1127 DCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFiqkyFRVASRDLQQLDDTTQLPLLSH 1202
Cdd:cd18546 105 DIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRW----FRRRSSRAYRRARERIAAVNAD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1274095655 1203 FAETVEGLTTIRAFRYEARFQQKLLEYTDSN---NIASLFLTA 1242
Cdd:cd18546 181 LQETLAGIRVVQAFRRERRNAERFAELSDDYrdaRLRAQRLVA 223
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1060-1232 |
1.49e-05 |
|
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: 48.58 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1060 QSVYAMVFTVLcsLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1139
Cdd:cd18551 37 GLLALLVALFL--LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1140 ECLSRSTLLCVSALTVISYVTPV-FLVAL--LPLAVVC-YFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1214
Cdd:cd18551 115 PQLVTGVLTVVGAVVLMFLLDWVlTLVTLavVPLAFLIiLPLGRRIRKASKRAQD-----ALGELSAALErALSAIRTVK 189
|
170
....*....|....*...
gi 1274095655 1215 AFRYEARFQQKLLEYTDS 1232
Cdd:cd18551 190 ASNAEERETKRGGEAAER 207
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
830-890 |
1.54e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 1.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 830 SGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTHKL 890
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1342-1577 |
1.56e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 48.92 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1342 GKIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdmfegriiidgidiaklplhTLRsrl 1421
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKST-----------------------------LLR--- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 sII--LQDPVlfSGTIRFN------LDPEK-----------------------------KCS----DSTLWEALEIAQLK 1460
Cdd:COG3839 48 -MIagLEDPT--SGEILIGgrdvtdLPPKDrniamvfqsyalyphmtvyeniafplklrKVPkaeiDRRVREAAELLGLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1461 LVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVVMTafadrTV 1532
Cdd:COG3839 125 DLLDRKPKQL-----------SGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TI 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 1533 -VTiahrvH------TIlsADLVMVLKRGAILEFDKPEKLLSQKDSVF-ASFV 1577
Cdd:COG3839 189 yVT-----HdqveamTL--ADRIAVMNDGRIQQVGTPEELYDRPANLFvAGFI 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
696-860 |
2.20e-05 |
|
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: 47.54 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPsnpereTAADSDARSRGPVAYASQK 775
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD------GQDI------TKLPMHKRARLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLL-NATVEENI--TFESpFNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVFL 852
Cdd:cd03218 84 ASIFrKLTVEENIlaVLEI-RGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLL 157
|
....*...
gi 1274095655 853 DDPFSALD 860
Cdd:cd03218 158 DEPFAGVD 165
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
824-920 |
2.50e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.24 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 824 ERGIN-LSGGQRQRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWII 900
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGL--HQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|....*.
gi 1274095655 901 AM------KDGTIQREGTLKDFQRSE 920
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILANP 586
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1064-1278 |
2.76e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 47.84 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1064 AMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECLS 1143
Cdd:cd18567 45 AIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1144 RSTLLCVSALTVI-SYVTPVFLVALlpLAVVCYFI-----QKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 1217
Cdd:cd18567 124 LDGLMAILTLVMMfLYSPKLALIVL--AAVALYALlrlalYPPLRRATEEQIVASAKEQ----SHFLETIRGIQTIKLFG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1218 YEARFQQKLLE-YTDSNN------IASLFLTAANRWLeVRMEYIgacVVLIAAATSIsnsLHRELSAG 1278
Cdd:cd18567 198 REAEREARWLNlLVDAINadirlqRLQILFSAANGLL-FGLENI---LVIYLGALLV---LDGEFTVG 258
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1452-1577 |
2.79e-05 |
|
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: 48.26 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1452 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVV 1523
Cdd:TIGR01187 83 EALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkTIQEQLG 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 1524 MtafadrTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQKDSVF-ASFV 1577
Cdd:TIGR01187 152 I------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
696-860 |
4.08e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQR----VSGAVFWNSLPDSEGEDpsnperetaadsdaRSRGPVAY 771
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhigVEGVITYDGITPEEIKK--------------HYRGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQK----PWLlnaTVEENITF----ESPFNkqRYKMVIEACSLQPDIDI------LPHGDQTQIGE---RGInlSGGQR 834
Cdd:TIGR00956 143 NAETdvhfPHL---TVGETLDFaarcKTPQN--RPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRGV--SGGER 215
|
170 180
....*....|....*....|....*.
gi 1274095655 835 QRISVARALYQHTNVVFLDDPFSALD 860
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1344-1571 |
4.26e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 46.67 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslkpVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVD---MFEGRIIIDGIDIAKLPLhtlr 1418
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLnlIAGFLPPDsgrILWNGQDLTALPPAERPV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1419 srlSIILQDPVLFSG-TIRFN----LDPEKKCSD---STLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1490
Cdd:COG3840 74 ---SMLFQENNLFPHlTVAQNiglgLRPGLKLTAeqrAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1491 LARAFVRKTSIFIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
....
gi 1274095655 1568 QKDS 1571
Cdd:COG3840 220 GEPP 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
827-888 |
4.38e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.41 E-value: 4.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1274095655 827 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTH 888
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE-----GILRLFEEFNRvgvTVLMATH 195
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1361-1570 |
4.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.13 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1361 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV----DMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGT 1434
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpssGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1435 IRFNLDPEKKCSDSTLWEALEIAqLKLVVKAlpGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-M 1513
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKA-LKWLKKV--GLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1514 ATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQKD 1570
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1452-1578 |
4.66e-05 |
|
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: 46.87 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1452 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-- 1529
Cdd:cd03294 143 EALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElq 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 1530 RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQ-KDSVFASFVR 1578
Cdd:cd03294 212 KTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNpANDYVREFFR 262
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1344-1558 |
4.75e-05 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 46.58 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDS--SLKPVLKHVNALIAPGQKIGICGRTGSGKSSF----------------------------SLAFFR 1393
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnilggldrptsgevlidgqdisslserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1394 mvdmfegriiidgidiaklplhtlRSRLSIILQDpvlfsgtirFNLDPE-----------------KKCSDSTLWEALEI 1456
Cdd:COG1136 85 ------------------------RRHIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLER 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1457 AQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFAD---RTV 1532
Cdd:COG1136 132 VGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTI 198
|
250 260
....*....|....*....|....*.
gi 1274095655 1533 VTIAHRVHTILSADLVMVLKRGAILE 1558
Cdd:COG1136 199 VMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1057-1225 |
5.93e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 46.86 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1057 ALDQSVYAMVFTVLcsLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIP 1136
Cdd:cd18780 40 ALNQAVLILLGVVL--IGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1137 STLECLSRSTLLCVSALTVISYV----TPVFLVALLPLAVVCYFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLT 1211
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTswklTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQD-----ALAAASTVAEeSISNIR 192
|
170
....*....|....
gi 1274095655 1212 TIRAFRYEARFQQK 1225
Cdd:cd18780 193 TVRSFAKETKEVSR 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
698-888 |
7.50e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 46.72 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnSLPDSegedpSNPEREtaadSDARSRGPVA--YASQK 775
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI---SLCGE-----PVPSRA----RHARQRVGVVpqFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PwllNATVEENI-TFESPFN------KQRYKMVIEACSLQPDIDilphgdqTQIGErginLSGGQRQRISVARALYQHTN 848
Cdd:PRK13537 93 P---DFTVRENLlVFGRYFGlsaaaaRALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVNDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1274095655 849 VVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 888
Cdd:PRK13537 159 VLVLDEPTTGLDPQ-ARHLMWERLRSLLARGK-TILLTTH 196
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
819-911 |
7.97e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 819 QTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD--DKRTVVLVTHKL-QYLPH 895
Cdd:PRK14271 154 KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-----IEEFIRSlaDRLTVIIVTHNLaQAARI 228
|
90
....*....|....*.
gi 1274095655 896 ADWIIAMKDGTIQREG 911
Cdd:PRK14271 229 SDRAALFFDGRLVEEG 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1344-1556 |
8.33e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVDMFEGRIIIDGIDIAKlPLHTLRSRL 1421
Cdd:PRK15439 12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLFSG-TIRFNL--------DPEKKCSDstLWEALEiAQLKLVVKAlpGGLDAiiteggenfsqGQRQLFCLA 1492
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENIlfglpkrqASMQKMKQ--LLAALG-CQLDLDSSA--GSLEV-----------ADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 1493 RAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAI 1556
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
698-915 |
8.72e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGED--PSNPeretaadSDARSRGpVAYASQK 775
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN------GKDisPRSP-------LDAVKKG-MAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 P----WLLNATVEENITFESPFNKQRYKMVI----------EACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVAR 841
Cdd:PRK09700 347 RrdngFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 842 ALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLR---DDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVG-----AKAEIYKVMRqlaDDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1087-1314 |
9.35e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 46.35 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1087 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-LV 1165
Cdd:cd18563 69 RLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLaLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1166 ALLPLAVVCYFIQKYFRVASRDLQQL----DDTTqlpllSHFAETVEGLTTIRAF---RYE-ARFQQKLLEYTDSNNIAS 1237
Cdd:cd18563 149 VLIPVPLVVWGSYFFWKKIRRLFHRQwrrwSRLN-----SVLNDTLPGIRVVKAFgqeKREiKRFDEANQELLDANIRAE 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1238 LFLTAANRWLEVRMEyIGACVVLIAAATSIsnsLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1314
Cdd:cd18563 224 KLWATFFPLLTFLTS-LGTLIVWYFGGRQV---LSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
699-907 |
1.08e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsLPDSEGEDPSNPERETAAD-----SDARSRGPVAYAS 773
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV----YLDGKPIDIRSPRDAIRAGimlcpEDRKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 774 qkpwllnatVEENITFESPFNKQRYKMVI----EACSLQPDIDIL----PHGDQtQIGergiNLSGGQRQRISVARALYQ 845
Cdd:PRK11288 348 ---------VADNINISARRHHLRAGCLInnrwEAENADRFIRSLniktPSREQ-LIM----NLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 846 HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 907
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYN--VIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1344-1567 |
1.09e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 46.37 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDPVL---FSG-----------TIRFnlDPEKKCSDSTLWEALEiaqlklvvkalPGGLDAIITEGGENFSQGQRQLF 1489
Cdd:PRK09536 82 VPQDTSLsfeFDVrqvvemgrtphRSRF--DTWTETDRAAVERAME-----------RTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1490 CLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLSA---DLVMVLKRGAILEFDKPEKL 1565
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPPADV 226
|
..
gi 1274095655 1566 LS 1567
Cdd:PRK09536 227 LT 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
692-891 |
1.19e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 45.65 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSlpdsegEDPSnperetAADSDARSRGPVAY 771
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD------EDIS------LLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWL---------LNATVE--ENITFESpfNKQRYKMVIEACSLQPDIDILphgdqtqigerGINLSGGQRQRISVA 840
Cdd:PRK10895 83 LPQEASIfrrlsvydnLMAVLQirDDLSAEQ--REDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 841 RALYQHTNVVFLDDPFSALD-VHLSDhlmQAGILELLRDDKRTVVLVTHKLQ 891
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
827-913 |
1.26e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 827 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVL-VTHKLQYLPH-ADWIIAMKD 904
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQ 204
|
....*....
gi 1274095655 905 GTIQREGTL 913
Cdd:PRK11144 205 GKVKAFGPL 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1344-1577 |
1.28e-04 |
|
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: 45.31 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAK----LPLHtlRS 1419
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFETPTSGEILLDGKditnLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1420 RLSIILQDPVLF-----SGTIRFNLDpEKKCSDSTLWEALEiAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARA 1494
Cdd:cd03300 73 PVNTVFQNYALFphltvFENIAFGLR-LKKLPKAEIKERVA-EALDLV------QLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1495 FVRKTSIFIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILSADLVMVLKRGAILEFDKPEKLLSQKD 1570
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
....*...
gi 1274095655 1571 SVF-ASFV 1577
Cdd:cd03300 224 NRFvADFI 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
711-910 |
1.67e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.16 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 711 IVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGE--DPSNPeretaadSDARSRGpVAYAS----QKPWLLNATVE 784
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLD------GKpvRIRSP-------RDAIRAG-IAYVPedrkGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 785 ENITFeSPFNKQRYKMVI-------EACSLQPDIDILPHGDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFS 857
Cdd:COG1129 349 ENITL-ASLDRLSRGGLLdrrreraLAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 858 ALDVhlsdhlmqaG----ILELLR---DDKRTVVLVThklQYLP----HADWIIAMKDGTIQRE 910
Cdd:COG1129 424 GIDV---------GakaeIYRLIRelaAEGKAVIVIS---SELPellgLSDRILVMREGRIVGE 475
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
827-890 |
1.73e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 1.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 827 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL 890
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA-IRRLSEEGKKTALVVEHDL 132
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1334-1577 |
2.34e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.21 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1334 IPKNWPDQGK-----IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGID 1408
Cdd:PRK11607 5 IPRPQAKTRKaltplLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1409 IAKLPLHT--LRSRLSIILQDPVLF-----SGTIRFNLDPEKKCSD---STLWEALEIAQLKLVVKALPGGLdaiitegg 1478
Cdd:PRK11607 79 DGVDLSHVppYQRPINMMFQSYALFphmtvEQNIAFGLKQDKLPKAeiaSRVNEMLGLVHMQEFAKRKPHQL-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1479 enfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKV----VMTAFADRTVVTIAHRvhtilsad 1546
Cdd:PRK11607 151 ---SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrMQLEvvDILERVgvtcVMVTHDQEEAMTMAGR-------- 219
|
250 260 270
....*....|....*....|....*....|..
gi 1274095655 1547 lVMVLKRGAILEFDKPEKLLSQKDSVF-ASFV 1577
Cdd:PRK11607 220 -IAIMNRGKFVQIGEPEEIYEHPTTRYsAEFI 250
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1368-1514 |
2.38e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.57 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1368 IAPGQKIGICGRTGSGKSSF-SL-AFFRMVD---MFEGRIIIDGIDIAKLPLhtlrsrlSIILQDPVLFSG-TIRFN--- 1438
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLlNLiAGFLTPAsgsLTLNGQDHTTTPPSRRPV-------SMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1439 -LDPEKKCSDSTLWEALEIAQ---LKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA 1514
Cdd:PRK10771 95 gLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1570 |
2.64e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.79 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1424 ILQDP--VLFS---------GTIRFNLDPEkkcsdsTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1492
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEE------TVAHRVSSA-LHML------GLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1493 RAFVRKTSIFIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 1274095655 1568 QKD 1570
Cdd:PRK13652 228 QPD 230
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1086-1233 |
2.80e-04 |
|
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: 44.73 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1086 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-L 1164
Cdd:cd18542 64 EKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLtL 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 1165 VALLPLAVVCYFIQKYFRVASRDLQQLDDttQLPLLSHFA-ETVEGLTTIRAF---RYE-ARFQQKLLEYTDSN 1233
Cdd:cd18542 144 ISLAIIPFIALFSYVFFKKVRPAFEEIRE--QEGELNTVLqENLTGVRVVKAFareDYEiEKFDKENEEYRDLN 215
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1059-1289 |
2.92e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1059 DQSVYAMVFTVLCSLGIALCL-----VTSVTVEWTGLKVAKRLHRSLLNRIIlapmRFFETTPLGSILNRFSSDCNTIDQ 1133
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAgirggLFTLAMARLNIRIRNLLFRSIVSQEI----GFFDTVKTGDITSRLTSDTTTMSD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1134 HIPSTLECLSRSTllcVSALTVIsyvtpVFLVAL-----------LPL-AVVCYFIQKYFRVASRDLQqlddtTQLPLLS 1201
Cdd:cd18784 109 TVSLNLNIFLRSL---VKAIGVI-----VFMFKLswqlslvtligLPLiAIVSKVYGDYYKKLSKAVQ-----DSLAKAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1202 HFA-ETVEGLTTIRAF--------RYEARFQQ-------KLLEYTDSNNIASLFLTAanrwLEVRMEYIGACVVLIAAAT 1265
Cdd:cd18784 176 EVAeETISSIRTVRSFanedgeanRYSEKLKDtyklkikEALAYGGYVWSNELTELA----LTVSTLYYGGHLVITGQIS 251
|
250 260
....*....|....*....|....*....
gi 1274095655 1266 S---ISNSLHR-ELSAGLVGLGLTYA-LM 1289
Cdd:cd18784 252 GgnlISFILYQlELGSCLESVGSVYTgLM 280
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
829-888 |
2.94e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 44.82 E-value: 2.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 888
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
782-860 |
3.25e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.25 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 782 TVEENI-----TFESPFNKQRYKMVieacSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVFLDDPF 856
Cdd:COG1137 94 TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
....
gi 1274095655 857 SALD 860
Cdd:COG1137 165 AGVD 168
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
829-903 |
4.04e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 4.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 829 LSGGQRQRISVARAL----YQHTNVVFLDDPFSALDvhLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMK 903
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLD--PRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1343-1573 |
4.64e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 43.85 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1343 KIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 1422
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1423 IILQDPVLFSG-TIRfNLDPEKKCSDSTLWEALEIAQLKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:PRK11231 80 LLPQHHLTPEGiTVR-ELVAYGRSPWLSLWGRLSAEDNARVNQAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1501 IFIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLSQK--DSVF 1573
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPGllRTVF 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1370-1563 |
4.97e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.36 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1370 PGQKIGICGRTGSGKSSFSLAFFRMVDmfegriiidgidiaklplhtlRSRLSIILQDPVLFSGTIRFNLdpekkcsdst 1449
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG---------------------PPGGGVIYIDGEDILEEVLDQL---------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1450 lwealeiaqlklvvkalpggLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAF-- 1527
Cdd:smart00382 50 --------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1274095655 1528 -----ADRTVVTIAHRVHTILSADLVMVLKRgaILEFDKPE 1563
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRRRFDR--RIVLLLIL 148
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
711-899 |
4.98e-04 |
|
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: 44.54 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 711 IVGQVGCGKSSLLLATLGEMQrvsgavfwnslpDSEGEdpsnperetAADSDARSRGpvaYASQKPWL-LNATVEENI-- 787
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDK------------DFNGE---------ARPQPGIKVG---YLPQEPQLdPTKTVRENVee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 788 -----------------TFESP---FNKQRYKM-----VIEAC---SLQPDIDI------LPHGDQtQIGergiNLSGGQ 833
Cdd:TIGR03719 92 gvaeikdaldrfneisaKYAEPdadFDKLAAEQaelqeIIDAAdawDLDSQLEIamdalrCPPWDA-DVT----KLSGGE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 834 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWI 899
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPGTVVAVTHDRYFLDNvAGWI 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
692-905 |
5.36e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnslpdsegedpSNPERETAADSDARSRGPVAY 771
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-----------QGKEIDFKSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 772 ASQKPWLLNATVEENITF-----ESPFNKQRyKMVIEACSL--QPDIDILPHgdqtqigERGINLSGGQRQRISVARALY 844
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLgryptKGMFVDQD-KMYRDTKAIfdELDIDIDPR-------AKVATLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 845 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDG 905
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1469-1557 |
6.28e-04 |
|
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: 43.19 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1469 GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-AD 1546
Cdd:cd03219 132 GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlAD 211
|
90
....*....|.
gi 1274095655 1547 LVMVLKRGAIL 1557
Cdd:cd03219 212 RVTVLDQGRVI 222
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
708-888 |
8.37e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 42.64 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 708 LTMIVGQVGCGKSSLLLAtlgemqrVSGAVFwnslpdsegedpsnpeRETAADSDARSRGPVAyasqkpwllnATVEE-- 785
Cdd:cd03279 30 LFLICGPTGAGKSTILDA-------ITYALY----------------GKTPRYGRQENLRSVF----------APGEDta 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 786 NITFESPFNKQRYKmVIEACSLQPD----IDILPHGDQTQIGERGI-NLSGGQRQRISVARAL------YQHTNVV---- 850
Cdd:cd03279 77 EVSFTFQLGGKKYR-VERSRGLDYDqftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevlQNRGGARleal 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1274095655 851 FLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTH 888
Cdd:cd03279 156 FIDEGFGTLDPEALEAVATA--LELIRTENRMVGVISH 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
696-892 |
8.92e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnslpdsegedpsnpERETAADsdarsrgpVAYASQK 775
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----------------HCGTKLE--------VAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 776 PWLLNA--TVEENITfESpfnKQ------RYKMVIEacSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQHT 847
Cdd:PRK11147 391 RAELDPekTVMDNLA-EG---KQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1274095655 848 NVVFLDDPFSALDVHLSDHLMqagilELLRDDKRTVVLVTHKLQY 892
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLE-----ELLDSYQGTVLLVSHDRQF 499
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
445-561 |
9.41e-04 |
|
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: 43.27 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 445 IIVGVILLYY--ILGVSALIGAAVIILLApvqYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAW 514
Cdd:cd18555 130 VIYLIYMLYYspLLTLIVLLLGLLIVLLL---LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKslgsekniYKKW 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1274095655 515 ENIFCSRVEMTRRKEMTSlrafAVYTSISIFMNTAIPIaavLITFVG 561
Cdd:cd18555 207 ENLFKKQLKAFKKKERLS----NILNSISSSIQFIAPL---LILWIG 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1344-1385 |
9.43e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.76 E-value: 9.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274095655 1344 IQIQNLSVRY------DSSLK--------------PVLKHVNALIAPGQKIGICGRTGSGKS 1385
Cdd:COG1134 5 IEVENVSKSYrlyhepSRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKS 66
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1344-1570 |
1.10e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 42.73 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSL---KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFR---------MVDMFEGRIIidgidiaK 1411
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkptsgkiIIDGVDITDK-------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1412 LPLHTLRSRLSIILQDP--VLFSGT----IRF---NLDPEKKCSDSTLWEALEIAQLKlvvkalpggLDAIITEGGENFS 1482
Cdd:PRK13637 76 VKLSDIRKKVGLVFQYPeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1483 QGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEF 1559
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQ 226
|
250
....*....|.
gi 1274095655 1560 DKPEKLLSQKD 1570
Cdd:PRK13637 227 GTPREVFKEVE 237
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1358-1572 |
1.17e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1358 KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDMFEGRIIIDGIDIAKlplHTLRsRLSIILQDPVLFSG-T 1434
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYPHlT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1435 IRFNLdpeKKCSDSTLWEALEiAQLKLVVKalpgglDAIITEGG----EN----------FSQGQRQLFCLARAFVRKTS 1500
Cdd:PLN03211 157 VRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1501 IFIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILsaDLVMVLKRGAILEFDKPEKLLSQKDSV 1572
Cdd:PLN03211 227 LLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1344-1387 |
1.20e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 42.45 E-value: 1.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1387
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTL 44
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1344-1577 |
1.23e-03 |
|
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: 42.33 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAK-LPLHTLRSR-L 1421
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAGLERPDSGTILFGGEdATDVPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDPVLF-----SGTIRFNLDPEKKcsdSTLWEALEIAQ-----LKLVvkalpgGLDAIITEGGENFSQGQRQLFCL 1491
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRVKPR---SERPPEAEIRAkvhelLKLV------QLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1492 ARAFVRKTSIFIMDEATASIDMATENILQKVVmTAFADRTVVT---IAHRVHTILS-ADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 1274095655 1568 QKDSVF-ASFV 1577
Cdd:cd03296 227 HPASPFvYSFL 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
696-889 |
1.23e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlgemQRVSGAVFwnslpdSEGEDPSN-PERETaadSDARSRGPVayA 772
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLnvLA-----ERVTTGVI------TGGDRLVNgRPLDS---SFQRSIGYV--Q 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 773 SQKPWLLNATVEENITFE---------SPFNKQRY-KMVIEACSLQPDIDILphgdqtqIGERGINLSGGQRQRISVARA 842
Cdd:TIGR00956 843 QQDLHLPTSTVRESLRFSaylrqpksvSKSEKMEYvEEVIKLLEMESYADAV-------VGVPGEGLNVEQRKRLTIGVE 915
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 843 LYQHTN-VVFLDDPFSALDVHLSdhlmqAGILELLR---DDKRTVVLVTHK 889
Cdd:TIGR00956 916 LVAKPKlLLFLDEPTSGLDSQTA-----WSICKLMRklaDHGQAILCTIHQ 961
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
778-913 |
1.24e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 778 LLNATVEE-NITFesPFNKQrykmvIEAcSLQPDIDI----LPhgdqtqIGERGINLSGGQRQRISVARALY---QHTNV 849
Cdd:PRK00635 1658 LLQTPIEEvAETF--PFLKK-----IQK-PLQALIDNglgyLP------LGQNLSSLSLSEKIAIKIAKFLYlppKHPTL 1723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1274095655 850 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 913
Cdd:PRK00635 1724 FLLDEIATSLDNQQKSALLV--QLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKI 1785
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1344-1568 |
1.37e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.38 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRY----DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM---------VDMFEGRIIIDgidia 1410
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlipsegkvyVDGLDTSDEEN----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1411 klpLHTLRSRLSIILQDP------------VLFSGTirfNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiitegg 1478
Cdd:PRK13633 80 ---LWDIRNKAGMVFQNPdnqivativeedVAFGPE---NLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1479 enfSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILSADLVMVLK 1552
Cdd:PRK13633 146 ---SGGQKQRVAIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMD 218
|
250
....*....|....*.
gi 1274095655 1553 RGAILEFDKPEKLLSQ 1568
Cdd:PRK13633 219 SGKVVMEGTPKEIFKE 234
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1061-1180 |
1.51e-03 |
|
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: 42.46 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1061 SVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID----QHIP 1136
Cdd:cd18577 47 NKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQdgigEKLG 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 1137 STLECLSrstlLCVSALtVISYV---------TPVFLVALLPLAVVCYFIQKY 1180
Cdd:cd18577 127 LLIQSLS----TFIAGF-IIAFIyswkltlvlLATLPLIAIVGGIMGKLLSKY 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
817-862 |
1.58e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.00 E-value: 1.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1274095655 817 GDQTQ-IGErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVH 862
Cdd:TIGR03719 435 SDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
828-890 |
1.58e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.23 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 828 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSDHLMQAGILELLRDDKRTVVLVTHKL 890
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1095-1226 |
1.62e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 42.47 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1095 RLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIdQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVALLPL 1170
Cdd:cd18543 73 DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPplalVALASLPPL 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 1171 AVVCYFIQKYFRVASRDLQQL--DDTTqlpllsHFAETVEGLTTIRAFRYEARFQQKL 1226
Cdd:cd18543 152 VLVARRFRRRYFPASRRAQDQagDLAT------VVEESVTGIRVVKAFGRERRELDRF 203
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
827-908 |
2.17e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.65 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 827 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 906
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
..
gi 1274095655 907 IQ 908
Cdd:PRK10522 527 LS 528
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1570 |
2.26e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.76 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMF--EGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSsgRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDP--VLFSGTIR-------FNLD-PEKKCSdstlwealeiaqlKLVVKALP-GGLDAIITEGGENFSQGQRQLFC 1490
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKlPEDEVR-------------KRVDNALKrTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1491 LARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LSADLVMVLKRGAILEFDKPEKLLS 1567
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFA 231
|
...
gi 1274095655 1568 QKD 1570
Cdd:PRK13636 232 EKE 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1344-1560 |
2.53e-03 |
|
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: 41.09 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPlhtLRS 1419
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEptsgRIYIGGRDVTDLP---PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1420 R-LSIILQDPVLFS-----GTIRFNLD----PEKKCSDSTLWEAlEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLF 1489
Cdd:cd03301 72 RdIAMVFQNYALYPhmtvyDNIAFGLKlrkvPKDEIDERVREVA-ELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1274095655 1490 CLARAFVRKTSIFIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILSADLVMVLKRGAILEFD 1560
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1344-1558 |
2.54e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.99 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSsfSLAffRMVDMFEGriiidgidiaklP-------- 1413
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLI--RCINLLER------------Ptsgsvlvd 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1414 -----------LHTLRSRLSIILQDpvlfsgtirFNLDPEKkcsdsTLWE----ALEIAQ-------------LKLV--- 1462
Cdd:COG1135 66 gvdltalsereLRAARRKIGMIFQH---------FNLLSSR-----TVAEnvalPLEIAGvpkaeirkrvaelLELVgls 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1463 --VKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENIL---QKVvmtafADR---TVV 1533
Cdd:COG1135 132 dkADAYPSQL-----------SGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIV 195
|
250 260
....*....|....*....|....*.
gi 1274095655 1534 TIAHRVHTILS-ADLVMVLKRGAILE 1558
Cdd:COG1135 196 LITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
829-912 |
2.54e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 829 LSGGQRQRISVA---------RALYqhtnvvFLDDPFSAL---DVHlsdHLMQagILELLRDDKRTVVLVTHKLQYLPHA 896
Cdd:PRK00349 831 LSGGEAQRVKLAkelskrstgKTLY------ILDEPTTGLhfeDIR---KLLE--VLHRLVDKGNTVVVIEHNLDVIKTA 899
|
90 100
....*....|....*....|..
gi 1274095655 897 DWIIAM------KDGTIQREGT 912
Cdd:PRK00349 900 DWIIDLgpeggdGGGEIVATGT 921
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
824-900 |
2.65e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 824 ERGIN-LSGGQRQRISVARALYQHTNVV--FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWII 900
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
816-935 |
2.80e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 816 HGDQ-TQIGERginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHKLQYL- 893
Cdd:PRK10636 420 QGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVSHDRHLLr 491
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1274095655 894 PHADWIIAMKDGTIQR-EGTLKDFQRsecqlfehWKTLMNRQD 935
Cdd:PRK10636 492 STTDDLYLVHDGKVEPfDGDLEDYQQ--------WLSDVQKQE 526
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1479-1556 |
2.92e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.93 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRG 1554
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDG 216
|
..
gi 1274095655 1555 AI 1556
Cdd:COG1129 217 RL 218
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
391-608 |
2.96e-03 |
|
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: 41.64 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 391 IQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYI---LGVSALIGAAV 466
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTsALTVLVRDPLTVIGLLGVLFYLdwkLTLIALVVLPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 467 IILlaPVQYFvATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FCSRVEMTRRKEMTSLRAFAVYTSI 542
Cdd:cd18552 152 AAL--PIRRI-GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1274095655 543 SIFMnTAIPIAAVLItFVGHVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18552 229 MELL-GAIAIALVLW-YGGYQVI--SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
690-907 |
3.49e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.94 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNslpdseGEDPsnpereTAADSDARSRGPV 769
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD------GEDI------TGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQKPW----LLNATVEENITFES----PFNK----QRYKMVIEACSLQPDIDILPHGDQTQIGergiNLSGGQRQRI 837
Cdd:COG3845 336 AYIPEDRLgrglVPDMSVAENLILGRyrrpPFSRggflDRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1274095655 838 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTI 907
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQR-LLE-LRDAGAAVLLISEDLDeILALSDRIAVMYEGRI 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
830-893 |
3.65e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 3.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274095655 830 SGGQRQRISVARALYQHTNVVFLDDPFSALDVH----LSDHLMQAgilellrddKRTVVLVTHKLQYL 893
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKW---------PKTFIVVSHAREFL 404
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
698-888 |
4.95e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 698 NITIRIPRGQLTMIVGQVGCGKSSlllaTlgeMQRVSGAvfwnsLPDSEGE--------DPSnperetaaDSDARSRgpV 769
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKST----T---MKMLTGL-----LPASEGEawlfgqpvDAG--------DIATRRR--V 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 770 AYASQkpwllnA-------TVEENIT-----FESPFNK--QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 835
Cdd:NF033858 342 GYMSQ------AfslygelTVRQNLElharlFHLPAAEiaARVAEMLERFDLADVADALPD-----------SLPLGIRQ 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1274095655 836 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTH 888
Cdd:NF033858 405 RLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL-LIELSREDGVTIFISTH 456
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
817-905 |
5.46e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 817 GDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHA 896
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGIT 458
|
....*....
gi 1274095655 897 DWIIAMKDG 905
Cdd:PRK10982 459 DRILVMSNG 467
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1344-1385 |
6.11e-03 |
|
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: 41.21 E-value: 6.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1274095655 1344 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKS 1385
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKS 50
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1572 |
6.84e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 40.45 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV--DMFEGRIIIDGIDIAKLPLHTLRSRL 1421
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILkpTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1422 SIILQDP--VLFSGTIRFNLdpekkcsdstlweALEIAQLKL----VVKALPGGLDAIITEGGEN-----FSQGQRQLFC 1490
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDV-------------AFGPLNLGLskeeVEKRVKEALKAVGMEGFENkpphhLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1491 LARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTI-LSADLVMVLKRGAILEFDKPEKLLSQ 1568
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
....
gi 1274095655 1569 KDSV 1572
Cdd:PRK13639 228 IETI 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
815-920 |
7.00e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 815 PHGDQtQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYL 893
Cdd:PRK10762 387 PSMEQ-AIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ--LINQFKAEGLSIILVSSEMpEVL 459
|
90 100
....*....|....*....|....*..
gi 1274095655 894 PHADWIIAMKDGTIQREgtlkdFQRSE 920
Cdd:PRK10762 460 GMSDRILVMHEGRISGE-----FTREQ 481
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1344-1558 |
7.44e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1344 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLP---L 1414
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLLERptsgRVLVDGQDLTALSekeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1415 HTLRSRLSIILQdpvlfsgtiRFNLdpekkCSDSTLWE----ALEIAQ-------------LKLVvkalpgGLDAIITEG 1477
Cdd:PRK11153 78 RKARRQIGMIFQ---------HFNL-----LSSRTVFDnvalPLELAGtpkaeikarvtelLELV------GLSDKADRY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1478 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvvMTAFADR----TVVTIAHRVHTILS-ADLVMVL 1551
Cdd:PRK11153 138 PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAtTRSILE---LLKDINRelglTIVLITHEMDVVKRiCDRVAVI 214
|
....*..
gi 1274095655 1552 KRGAILE 1558
Cdd:PRK11153 215 DAGRLVE 221
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1089-1233 |
7.50e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 40.22 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1089 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCntidQHIPSTLE-CLS---RSTLL---CVSALTVISYVTP 1161
Cdd:cd18574 70 GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV----QEFKSSFKqCVSqglRSVTQtvgCVVSLYLISPKLT 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1274095655 1162 VFLVALLPLAVVC-YFIQKYFRVASRDLQQLDDTTqlplLSHFAETVEGLTTIRAFRYEAR----FQQKLLEYTDSN 1233
Cdd:cd18574 146 LLLLVIVPVVVLVgTLYGSFLRKLSRRAQAQVAKA----TGVADEALGNIRTVRAFAMEDRelelYEEEVEKAAKLN 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1344-1390 |
8.61e-03 |
|
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: 39.43 E-value: 8.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1274095655 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLA 1390
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKT 45
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1366-1521 |
8.74e-03 |
|
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: 39.59 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1366 ALIAPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGID--------IAKLPLHTLRSRLSIILQDPVLFSG-TIR 1436
Cdd:cd03297 18 DFDLNEEVTGIFGASGAGKSTL----LRCIAGLEKPDGGTIVLngtvlfdsRKKINLPPQQRKIGLVFQQYALFPHlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274095655 1437 FNLD-PEKKCSDSTLW----EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASI 1511
Cdd:cd03297 94 ENLAfGLKRKRNREDRisvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170
....*....|
gi 1274095655 1512 DMATENILQK 1521
Cdd:cd03297 163 DRALRLQLLP 172
|
|
| |
