|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
224-1579 |
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 1490492289 224 LLSKGTYWWMNAFIKTAHKKPI---DLRAIGK-------LPIAMRAL------TNYQRLCVAFDAQAQRKD--------- 278
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsemvVPVLVENWkkeckkTRKQPVSAVYGKKDPSKPkgssqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 279 -------MQSPQSAR--AIWRALCHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVdhlgkeNHVFQPKTQFLGVYFVSS 349
Cdd:TIGR00957 289 eevealiVKSPHKPRkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLI------RFVNDPMAPDWQGYFYTG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 350 QEFLgnayvlavllflALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKimQLSTSNLSMGEMTAGQICNLVAIDTNQL 429
Cdd:TIGR00957 363 LLFV------------CACLQTLILHQYFHICFVSGMRIKTAVMGAVYRK--ALVITNSARKSSTVGEIVNLMSVDAQRF 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 430 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 509
Cdd:TIGR00957 429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 510 LKLYAWENIFCSRVEMTRKKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVT 589
Cdd:TIGR00957 509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 590 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIhEEQCAPREPAPQGQAgkyqavplkvvnrkrpareevrdllgplqrltp 669
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLSHEEL-EPDSIERRTIKPGEG--------------------------------- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 670 smdgdadnFCVQIIGGFFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGavfwnslpdsege 749
Cdd:TIGR00957 635 --------NSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG------------- 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 750 dpsspeqetvadsDVRTRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGIN 829
Cdd:TIGR00957 694 -------------HVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVN 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQ--AGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGT 907
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRILVTHGISYLPQVDVIIVMSGGK 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 908 I----------QREGTLKDFQRS------EYQLFEHWKTLMNRQDQE--------LEKETV---LERK---APEPSQGLP 957
Cdd:TIGR00957 839 IsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEakliengmLVTDVVgkqLQRQlsaSSSDSGDQS 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 958 RAMSSKDGLLLDEEEEEEEAAESEEDDDLSSVlhqRAKIPWracsKYLSSAGVLLLSLLVFSQLLKHMVLVAIDYWLAKW 1037
Cdd:TIGR00957 919 RHHGSSAELQKAEAKEETWKLMEADKAQTGQV---ELSVYW----DYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLW 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1038 TDSALVLSPAARNcslsqecALDQSVYAmvftvlcSLGI---VLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFE 1114
Cdd:TIGR00957 992 TDDPMVNGTQNNT-------SLRLSVYG-------ALGIlqgFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE 1057
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1115 TTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDD 1194
Cdd:TIGR00957 1058 RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLES 1137
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1195 TTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNslHR 1274
Cdd:TIGR00957 1138 VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVIS--RH 1215
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1275 ELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHALLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQN 1349
Cdd:TIGR00957 1216 SLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE------APWQIqetapPSGWPPRGRVEFRN 1289
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1350 LSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP 1429
Cdd:TIGR00957 1290 YCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDP 1369
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1430 VLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEAT 1509
Cdd:TIGR00957 1370 VLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1510 ASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQKdSIFASFVR 1579
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
222-1580 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 718.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 222 VNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCVAFDAQAQRkdmqsPQSaraiW--RALCHAFGRR 299
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK-----PKP----WllRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 300 LVLSSTFRILADLLGFAGPLcifgIVDHLGKENHVFQPKTQ--------FLGVyfvssqeFLGnayvlavllflalllqr 371
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVGPL----LLNLLLESMQNGEPAWIgyiyafsiFVGV-------VLG----------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 372 TFLQASYYVAI-ETGINLRGAIQTKIYNKIMQLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGV 450
Cdd:PLN03130 355 VLCEAQYFQNVmRVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAM 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 451 ILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKE 530
Cdd:PLN03130 433 VLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 531 MTSLRAFAVYTSISIFMNTAIPIAAVLITFvGHVSFFKeSDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQK 610
Cdd:PLN03130 513 LSWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLG-GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKR 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 611 LSEFLSsAEihEEQCAPREPAPQGQagkyqavplkvvnrkrPAreevrdllgplqrltpsmdgdadnfcVQIIGGFFTWT 690
Cdd:PLN03130 591 LEELLL-AE--ERVLLPNPPLEPGL----------------PA--------------------------ISIKNGYFSWD 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDG-IPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMqkvsgavfwnslpdsegedpsspeqETVADSDVRTRGP 769
Cdd:PLN03130 626 SKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL-------------------------PPRSDASVVIRGT 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 849
Cdd:PLN03130 681 VAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 850 VVFLDDPFSALDVHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-------FQrsey 922
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEElsnngplFQ---- 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 923 QLFEHWKTLMNRQDQELEKE---TVLERKAPEPSQGLPRAMSSKDgllldeeeeeeeaaeseEDDDLSSVLHQRAK---- 995
Cdd:PLN03130 835 KLMENAGKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSKK-----------------KSKEGKSVLIKQEEretg 897
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 996 -IPWRACSKYLSSAGVLLLSLLVFSQLLKHMVL-VAIDYWLAKWTDSALVLSPAArncslsqecaldqSVYAMVFTVLcS 1073
Cdd:PLN03130 898 vVSWKVLERYKNALGGAWVVMILFLCYVLTEVFrVSSSTWLSEWTDQGTPKTHGP-------------LFYNLIYALL-S 963
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1074 LGIVLclVTSVTVEW---TGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLC 1150
Cdd:PLN03130 964 FGQVL--VTLLNSYWlimSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQL 1041
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1151 VSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEY 1230
Cdd:PLN03130 1042 LSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRS 1121
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1231 TDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSI---SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEI 1307
Cdd:PLN03130 1122 MDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVmqnGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAEN 1201
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1308 QLGAVKRIHALLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTG 1382
Cdd:PLN03130 1202 SLNAVERVGTYIDLPSE------APLVIennrpPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTG 1275
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1383 SGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKL 1462
Cdd:PLN03130 1276 AGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKD 1355
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1463 VVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHT 1542
Cdd:PLN03130 1356 VIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNT 1435
|
1370 1380 1390
....*....|....*....|....*....|....*...
gi 1490492289 1543 ILSADLVMVLKRGAILEFDKPETLLNQKDSIFASFVRA 1580
Cdd:PLN03130 1436 IIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-1580 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 709.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCVAFDAQAQRkdmqsPQSAraIWRALCHAFGRRLVL 302
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRR-----PKPW--LLRALNNSLGGRFWL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 303 SSTFRILADLLGFAGPLcifgIVDHLGKENHVFQPKtqFLGvYFVSSQEFLGNAYVlavllflalllqrTFLQASYYVAI 382
Cdd:PLN03232 306 GGIFKIGHDLSQFVGPV----ILSHLLQSMQEGDPA--WVG-YVYAFLIFFGVTFG-------------VLCESQYFQNV 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 383 -ETGINLRGAIQTKIYNKIMQLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 461
Cdd:PLN03232 366 gRVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVAS 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 462 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLRAFAVYT 541
Cdd:PLN03232 444 LFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLS 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 542 SISIFMNTAIPIAAVLITFvgHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSaeih 621
Cdd:PLN03232 524 AFNSFILNSIPVVVTLVSF--GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLS---- 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 622 EEQCAPREPapqgqagkyqavplkvvnrkrpareevrdllgPLQRLTPSmdgdadnfcVQIIGGFFTW-TPDGIPTLSNI 700
Cdd:PLN03232 598 EERILAQNP--------------------------------PLQPGAPA---------ISIKNGYFSWdSKTSKPTLSDI 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 701 SIRIPRGQLTMIVGQVGCGKSSLLLATLGEmqkvsgavfwnsLPDSEgedpsspeqetvaDSDVRTRGPVAYASQKPWLL 780
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGE------------LSHAE-------------TSSVVIRGSVAYVPQVSWIF 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 781 NATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSAL 860
Cdd:PLN03232 692 NATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 861 DVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE--YQLFEHWKTLMNRQDQE 938
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGslFKKLMENAGKMDATQEV 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 939 LEKETVLERKAPEPS-----QGLPRAMSSKDGllldeeeeeeeaaeseedddlSSVL-----HQRAKIPWRACSKYLSSA 1008
Cdd:PLN03232 850 NTNDENILKLGPTVTidvseRNLGSTKQGKRG---------------------RSVLvkqeeRETGIISWNVLMRYNKAV 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1009 GVLLLSLLVFSQLLKHMVL-VAIDYWLAKWTDSALVLSpaarncslsqecaLDQSVYAMVFTVLCSLGIVLCLVTSVTVE 1087
Cdd:PLN03232 909 GGLWVVMILLVCYLTTEVLrVSSSTWLSIWTDQSTPKS-------------YSPGFYIVVYALLGFGQVAVTFTNSFWLI 975
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1088 WTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVA 1167
Cdd:PLN03232 976 SSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWA 1055
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1168 LLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRW 1247
Cdd:PLN03232 1056 IMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRW 1135
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1248 LEVRMEYIGACVVLIAAATSI---SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHALLKTEAE 1324
Cdd:PLN03232 1136 LTIRLETLGGVMIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSE 1215
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1325 syegllAPSLIPKN-----WPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMF 1399
Cdd:PLN03232 1216 ------ATAIIENNrpvsgWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE 1289
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1400 EGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGG 1479
Cdd:PLN03232 1290 KGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGG 1369
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1480 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILE 1559
Cdd:PLN03232 1370 ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
1370 1380
....*....|....*....|.
gi 1490492289 1560 FDKPETLLNQKDSIFASFVRA 1580
Cdd:PLN03232 1450 YDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
370-1580 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 624.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 370 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMQLSTSNLSMGEMTAGQICNLVAIDT---NQLMWFfflCPNLWAMPVQI 446
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVeriNSFMQY---CMYLWSSPMVL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 447 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMT 526
Cdd:PTZ00243 375 LLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 527 RKKEMTSLRAFAVYTSISIFMNTAIP---IAAVLITF--VGHvsffkesDFSPSVAFASLSLFHILVTPLFLLSSVVRST 601
Cdd:PTZ00243 455 RARELRYLRDVQLARVATSFVNNATPtlmIAVVFTVYylLGH-------ELTPEVVFPTIALLGVLRMPFFMIPWVFTTV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 602 VKALVSVQKLSEFLSS-----------AEIHEEQcapREPAPQGQAGK-------YQAVPLKVV---------------- 647
Cdd:PTZ00243 528 LQFLVSIKRISTFLECdnatcstvqdmEEYWREQ---REHSTACQLAAvlenvdvTAFVPVKLPrapkvktsllsralrm 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 648 --------NRKRPAREEVRDLLGPLQRLTPSMDGDADnfCVQIIGG------------------FFTWTPDGIptLSNIS 701
Cdd:PTZ00243 605 lcceqcrpTKRHPSPSVVVEDTDYGSPSSASRHIVEG--GTGGGHEatptsersaktpkmktddFFELEPKVL--LRDVS 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 702 IRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfWnslpdsegedpsspeqetvadsdvrTRGPVAYASQKPWLLN 781
Cdd:PTZ00243 681 VSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-W-------------------------AERSIAYVPQQAWIMN 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 782 ATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALD 861
Cdd:PTZ00243 735 ATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 862 VHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEyqLFEHWKT-LMNRQ----- 935
Cdd:PTZ00243 815 AHVGERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATLAAeLKENKdskeg 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 936 ---------DQELEKETVLERKAPEP----SQGLPRAMSSKDGLLLdeeeeeeeaaeseedddlssVLHQRA--KIPWRA 1000
Cdd:PTZ00243 891 dadaevaevDAAPGGAVDHEPPVAKQegnaEGGDGAALDAAAGRLM--------------------TREEKAsgSVPWST 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1001 CSKYLSS-AGVLLLSLLVFSQLLKHMVLVAIDYWLAKWTdsalvlspaarncslSQECALDQSVYAMVFtvlcsLGIVLC 1079
Cdd:PTZ00243 951 YVAYLRFcGGLHAAGFVLATFAVTELVTVSSGVWLSMWS---------------TRSFKLSAATYLYVY-----LGIVLL 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1080 LVTSV----TVEWTGLKV-AKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSAL 1154
Cdd:PTZ00243 1011 GTFSVplrfFLSYEAMRRgSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSI 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1155 TVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSN 1234
Cdd:PTZ00243 1091 LVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVV 1170
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1235 NIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELS--AGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAV 1312
Cdd:PTZ00243 1171 YSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSV 1250
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1313 KR----IHAL-------LKTE---AESYEGLLA---------PSLIPKNWP---DQGKIQIQNLSVRYDSSLKPVLKHVN 1366
Cdd:PTZ00243 1251 ERllyyTDEVphedmpeLDEEvdaLERRTGMAAdvtgtvviePASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVS 1330
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1367 ALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKC 1446
Cdd:PTZ00243 1331 FRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEA 1410
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1447 SDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFI-MDEATASIDMATENILQKVVM 1525
Cdd:PTZ00243 1411 SSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQATVM 1490
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1526 TAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQKDSIFASFVRA 1580
Cdd:PTZ00243 1491 SAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1343-1582 |
2.22e-150 |
|
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: 458.99 E-value: 2.22e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1343 GKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1502
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1503 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQKDSIFASFVRADK 1582
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
680-907 |
1.74e-142 |
|
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: 436.38 E-value: 1.74e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 680 VQIIGGFFTWTPdGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSlpdsegedpSSPEQETV 759
Cdd:cd03290 1 VQVTNGYFSWGS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---------KNESEPSF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 760 ADSDVRTRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRIS 839
Cdd:cd03290 71 EATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 907
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 ... |
1023-1316 |
1.91e-141 |
|
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: 437.04 E-value: 1.91e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1023 KHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLL 1102
Cdd:cd18602 11 KQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1103 NCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF 1182
Cdd:cd18602 91 RNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1183 RVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLI 1262
Cdd:cd18602 171 RASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1263 AAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1316
Cdd:cd18602 251 AALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVL 304
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
302-611 |
1.95e-139 |
|
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: 431.66 E-value: 1.95e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 302 LSSTFRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVA 381
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVSYVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 382 IETGINLRGAIQTKIYNKIMQLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 461
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 462 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLRAFAVYT 541
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 542 SISIFMNTAIPIAAVLITFVGHVsFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 611
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYP-YLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
223-1582 |
7.59e-127 |
|
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: 432.80 E-value: 7.59e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCVAFDAQ-AQRKdmQSPQSARAIWRAlchafgrrlv 301
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRElASAK--KNPKLLNALRRC---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 302 lsstfriladllgFAGPLCIFGIVDHLGKENHVFQPKT--QFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYY 379
Cdd:TIGR01271 78 -------------FFWRFVFYGILLYFGEATKAVQPLLlgRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 380 VAIETGINLRGAIQTKIYNKIMQLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGV 459
Cdd:TIGR01271 145 GLHHLGMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 460 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLRAFAv 539
Cdd:TIGR01271 223 NGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 540 ytSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHIL-VTPLFLLSSVVRSTVKALVSVQKLSEFLSSA 618
Cdd:TIGR01271 302 --YLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 619 E--IHEEQCAPREpapqgqagkyqavpLKVVNRKRPAREEVRDLLGPLQ-----RLTPsmDGDAdnfcvqiiGGFFT-WT 690
Cdd:TIGR01271 380 EykTLEYNLTTTE--------------VEMVNVTASWDEGIGELFEKIKqnnkaRKQP--NGDD--------GLFFSnFS 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQkvsgavfwnslpdsegedPSspeqetvaDSDVRTRGPV 770
Cdd:TIGR01271 436 LYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE------------------PS--------EGKIKHSGRI 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNV 850
Cdd:TIGR01271 490 SFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADL 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 851 VFLDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG------------------------ 906
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGvcyfygtfselqakrpdfsslllg 647
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 907 -----------------------TIQREGTLKDFQRSEYQLFEH---------------------------WKTLMNRQD 936
Cdd:TIGR01271 648 leafdnfsaerrnsiltetlrrvSIDGDSTVFSGPETIKQSFKQpppefaekrkqsiilnpiasarkfsfvQMGPQKAQA 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 937 QELEKET--VLERK---APEPSQG---LPRAMSSKDGLLLDEEEEEEEAAESEEDDDLSSVLHQRAK------------- 995
Cdd:TIGR01271 728 TTIEDAVrePSERKfslVPEDEQGeesLPRGNQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQLQTsfrkkssitqqne 807
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 996 ------IPWRACSK-----------------------YLSSAGVLLLSLLVFSQLLKHMVLVAI---DYWLAKWTDSALV 1043
Cdd:TIGR01271 808 laseldIYSRRLSKdsvyeiseeineedlkecfaderENVFETTTWNTYLRYITTNRNLVFVLIfclVIFLAEVAASLLG 887
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1044 L-----SPAARNcSLSQECALDQS---VYAMVFTVLCSLGIVLCLV-TSVTVEWTG-----------LKVAKRLHHSLLN 1103
Cdd:TIGR01271 888 LwlitdNPSAPN-YVDQQHANASSpdvQKPVIITPTSAYYIFYIYVgTADSVLALGffrglplvhtlLTVSKRLHEQMLH 966
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1104 CIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFR 1183
Cdd:TIGR01271 967 SVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFL 1046
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1184 VASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF----RYEARFQQKLLEYTdsnniASLFLTAAN-RWLEVRMEYIgaC 1258
Cdd:TIGR01271 1047 RTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFgrqsYFETLFHKALNLHT-----ANWFLYLSTlRWFQMRIDII--F 1119
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1259 VVLIAAATSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHALLKTEAESYE-------GLLA 1331
Cdd:TIGR01271 1120 VFFFIAVTFIAIGTNQD-GEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRpsggggkYQLS 1198
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1332 PSLIPKN------WPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMfEGRIII 1405
Cdd:TIGR01271 1199 TVLVIENphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQI 1277
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1406 DGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQG 1485
Cdd:TIGR01271 1278 DGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1486 QRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPET 1565
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK 1437
|
1530
....*....|....*..
gi 1490492289 1566 LLNQKDSIFASFVRADK 1582
Cdd:TIGR01271 1438 LLNETSLFKQAMSAADR 1454
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1343-1563 |
2.98e-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: 353.72 E-value: 2.98e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1343 GKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1502
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 1503 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKP 1563
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
680-907 |
4.09e-102 |
|
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: 324.81 E-value: 4.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 680 VQIIGGFFTWTPDGI---PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdsegedpsspeq 756
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 757 etvadsdvrtrGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQ 836
Cdd:cd03250 66 -----------GSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 907
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1064-1580 |
3.36e-92 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 311.33 E-value: 3.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1064 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1143
Cdd:COG1132 63 LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1144 SRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1219
Cdd:COG1132 143 VRSVVTLIGALVVLFVIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAE----LNGRLQESLSGIRVVKAFGR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1220 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMV 1299
Cdd:COG1132 219 EERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1300 RNLADMEIQLGAVKRIHALLKTEAESYEGLLAPSLIPknwpDQGKIQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICG 1379
Cdd:COG1132 299 NVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPP----VRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1380 RTGSGKSSF-SLaFFRM------------VDMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPE 1443
Cdd:COG1132 374 PSGSGKSTLvNL-LLRFydptsgrilidgVDI------------RDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1444 KkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 1523
Cdd:COG1132 441 A--TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 1524 VMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLnQKDSIFASFVRA 1580
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 ... |
1028-1316 |
3.52e-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: 280.54 E-value: 3.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1028 VAIDYWLAKWTDSAlvlspaarncslSQECALDQSVYAMVFTVLCSLG-IVLCLVTSVTVEWTGLKVAKRLHHSLLNCII 1106
Cdd:cd18580 16 QFSNIWLDWWSSDW------------SSSPNSSSGYYLGVYAALLVLAsVLLVLLRWLLFVLAGLRASRRLHDKLLRSVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1107 LAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVAS 1186
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1187 RDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAAT 1266
Cdd:cd18580 164 RQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1267 SIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1316
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, ... |
1024-1316 |
3.89e-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: 272.04 E-value: 3.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1024 HMVLVAIDYWLAKWTDSALVLSPAARNcslsqecalDQSVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLN 1103
Cdd:cd18603 12 QAFSVGSNIWLSEWSDDPALNGTQDTE---------QRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1104 CIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFR 1183
Cdd:cd18603 83 NILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1184 VASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIA 1263
Cdd:cd18603 163 ATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1264 AATSIsnsLHRE-LSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1316
Cdd:cd18603 243 ALFAV---LSRDsLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIK 293
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1339-1563 |
1.37e-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: 258.11 E-value: 1.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1339 WPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTL 1418
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1419 RSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEiaqlklvvkalpggldaiITEGGENFSQGQRQLFCLARAFVR 1498
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1499 KTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKP 1563
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; ... |
1024-1319 |
1.23e-77 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 259.32 E-value: 1.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1024 HMVLVAIDYWLAKWT---DSALVLSPAARNcslsqecaldQSVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHS 1100
Cdd:cd18604 12 QLLSVGQSWWLGIWAsayETSSALPPSEVS----------VLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1101 LLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQK 1180
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1181 YFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVV 1260
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 1261 LIAAATSISNslhRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHALL 1319
Cdd:cd18604 242 FATAALLVYG---PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1063-1579 |
1.10e-76 |
|
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: 270.17 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1063 VYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLEC 1142
Cdd:COG2274 197 VLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1143 LSRSTLLCVSALTVISY----VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 1218
Cdd:COG2274 276 ALLDLLFVLIFLIVLFFysppLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQ----SLLVETLRGIETIKALG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1219 YEARFQQK-------LLEYTDSNNIASLFLTAANRWLEVrmeyIGACVVLIAAATSIsnsLHRELSAGlvglGLTYALMV 1291
Cdd:COG2274 352 AESRFRRRwenllakYLNARFKLRRLSNLLSTLSGLLQQ----LATVALLWLGAYLV---IDGQLTLG----QLIAFNIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1292 SNYLNWMVRNLADM--EIQ--LGAVKRIHALLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSLKPVLKHVNA 1367
Cdd:COG2274 421 SGRFLAPVAQLIGLlqRFQdaKIALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGDSPPVLDNISL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1368 LISPGQKIGICGRTGSGKSSFS--LAFFRM----------VDMfegriiidgidiAKLPLHTLRSRLSIILQDPVLFSGT 1435
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLklLLGLYEptsgrilidgIDL------------RQIDPASLRRQIGVVLQDVFLFSGT 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1436 IRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASI 1512
Cdd:COG2274 565 IRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 1513 DMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLnQKDSIFASFVR 1579
Cdd:COG2274 643 DAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL-ARKGLYAELVQ 708
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
1029-1316 |
5.83e-73 |
|
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: 245.90 E-value: 5.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1029 AIDYWLAKWTDSAlvlspaarNCSLSQECALDQSVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILA 1108
Cdd:cd18605 17 LIDFWLSYWVSHS--------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1109 PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRD 1188
Cdd:cd18605 89 KMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1189 LQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSI 1268
Cdd:cd18605 169 LKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAV 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1490492289 1269 -SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1316
Cdd:cd18605 249 vQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVR 297
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
302-611 |
1.77e-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: 241.24 E-value: 1.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 302 LSSTFRILADLLGFAGPLCIFGIVDHLGKENHvfQPKTQ-------FLGVYFVSSqeflgnayvlavllflalllqrTFL 374
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD--EPLSEgyllalaLFLVSLLQS----------------------LLL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 375 QASYYVAIETGINLRGAIQTKIYNKIMQLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 454
Cdd:cd18579 57 HQYFFLSFRLGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 455 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSL 534
Cdd:cd18579 135 RLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKAL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 535 RAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKEsdFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 611
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, ... |
1031-1316 |
1.91e-66 |
|
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: 227.83 E-value: 1.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1031 DYWLAKW------TDSALVLSPAARNCSLSQECALD--QSVYAMVFTVLcslgIVLCLVTSVTVEWTGLKVAKRLHHSLL 1102
Cdd:cd18599 23 DWWLSYWlkqgsgNTTNNVDNSTVDSGNISDNPDLNfyQLVYGGSILVI----LLLSLIRGFVFVKVTLRASSRLHNKLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1103 NCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF 1182
Cdd:cd18599 99 QKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1183 RVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLI 1262
Cdd:cd18599 179 RRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLI 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1263 AAATSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1316
Cdd:cd18599 259 TALLVV--LLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERIL 310
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
1028-1316 |
2.53e-65 |
|
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: 223.51 E-value: 2.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1028 VAIDYWLAKWTDSALVLSpaarncslsqecaldQSVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIIL 1107
Cdd:cd18606 16 VFTNLWLSFWTEDFFGLS---------------QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1108 APMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASR 1187
Cdd:cd18606 81 APMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1188 DLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASlFLTAAN-RWLEVRMEYIGACVVLIAAAT 1266
Cdd:cd18606 161 ELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAY-FLTIANqRWLAIRLDLLGSLLVLIVALL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1267 SISNSLHreLSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1316
Cdd:cd18606 240 CVTRRFS--ISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLL 287
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
284-913 |
5.86e-62 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 223.50 E-value: 5.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 284 SARAIWRALCHAFG---RRLVLSSTFRILADLLGFAGPLCIFGIVDHLGkENHVFQPKTQFLGVYFVSsqeFLGNAyvla 360
Cdd:COG1132 4 SPRKLLRRLLRYLRpyrGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSALLLLLLLLLGL---ALLRA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 361 vllflalllqrTFLQASYYVAIETGINLRGAIQTKIYNKIMQLSTSNLSmgEMTAGQICNLVAIDTNQLMWFF-FLCPNL 439
Cdd:COG1132 76 -----------LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 440 WAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI- 518
Cdd:COG1132 143 VRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERe 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 519 ---FCSRVEMTRKKEMTSLRAFAVYTSISIFMNTaipIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLS 595
Cdd:COG1132 223 lerFREANEELRRANLRAARLSALFFPLMELLGN---LGLALVLLVG-GLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 596 SVVRSTVKALVSVQKLSEFLSsaeiheeqcaprepAPQGQAGKYQAVPLKvvnrkrPAREEVRdllgpLQRLTpsmdgda 675
Cdd:COG1132 299 NVLNQLQRALASAERIFELLD--------------EPPEIPDPPGAVPLP------PVRGEIE-----FENVS------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 676 dnfcvqiiggfFTWtPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLatLGEMQKVSGAVFWNslpdseGEDpss 753
Cdd:COG1132 347 -----------FSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnLL--LRFYDPTSGRILID------GVD--- 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 754 peQETVADSDVRTRgpVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGIN 829
Cdd:COG1132 404 --IRDLTLESLRRQ--IGVVPQDTFLFSGTIRENIRYGRPdATDEE---VEEAAkaaQAHEFIEALPDGYDTVVGERGVN 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQ 909
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
....
gi 1490492289 910 REGT 913
Cdd:COG1132 554 EQGT 557
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1343-1571 |
3.14e-60 |
|
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: 206.69 E-value: 3.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1343 GKIQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFSGTIRFNLDPEKKCSDSTLW-EALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1501
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1502 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQKD 1571
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
370-611 |
4.50e-60 |
|
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: 208.48 E-value: 4.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 370 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMQLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVG 449
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 450 VILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKK 529
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 530 EMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 609
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 1490492289 610 KL 611
Cdd:cd18595 289 RL 290
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1163-1570 |
2.40e-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: 215.01 E-value: 2.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1163 VFLVA--LLPLAVVcyFIQKYFRVASRdlQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASL- 1239
Cdd:COG4988 163 ILLVTapLIPLFMI--LVGKGAAKASR--RQWRALARLS--GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMk 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1240 -----FLTAAnrwleVrME---YIGACVVLIAAATSisnslhreLSAGLVGL--GLTYALMVSNYLNWMvRNL-----AD 1304
Cdd:COG4988 237 vlrvaFLSSA-----V-LEffaSLSIALVAVYIGFR--------LLGGSLTLfaALFVLLLAPEFFLPL-RDLgsfyhAR 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1305 MEIqLGAVKRIHALLKTEAESyeglLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSG 1384
Cdd:COG4988 302 ANG-IAAAEKIFALLDAPEPA----APAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAG 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1385 KSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLK 1461
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPD--ASDEELEAALEAAGLD 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1462 LVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVH 1541
Cdd:COG4988 454 EFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLA 533
|
410 420
....*....|....*....|....*....
gi 1490492289 1542 TILSADLVMVLKRGAILEFDKPETLLNQK 1570
Cdd:COG4988 534 LLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
1031-1315 |
6.24e-57 |
|
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: 200.24 E-value: 6.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1031 DYWLAKWTDS-----ALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCI 1105
Cdd:cd18601 23 DWWLSYWANLeeklnDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1106 ILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVA 1185
Cdd:cd18601 103 LRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1186 SRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIA-SLFLTaANRWLEVRMEYIgaCVVLIAA 1264
Cdd:cd18601 183 SREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAwFLFLA-TSRWLAVRLDAL--CALFVTV 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 1265 ATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1315
Cdd:cd18601 260 VAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
372-913 |
3.85e-56 |
|
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: 209.30 E-value: 3.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 372 TFLQASYYVAIETGINLRgaIQTKIYNKIMQLSTSNL---SMGEMTA-----GQICNLVaidTNQLMWFFFLCPnlwamp 443
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDLASrfrdvESIREFL---TGSLLTALLDLL------ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 444 vQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRV 523
Cdd:COG2274 282 -FVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRW 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 524 E-MTRKKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTV 602
Cdd:COG2274 361 EnLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 603 KALVSVQKLSEFLSsaeiheeqcAPREPAPqgqagkyqavplkvvnrkrpareevrdllGPLQRLTPSMDGDadnfcVQI 682
Cdd:COG2274 440 DAKIALERLDDILD---------LPPEREE-----------------------------GRSKLSLPRLKGD-----IEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 683 IGGFFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPdsegedpsspeQETVADS 762
Cdd:COG2274 477 ENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID-----------LRQIDPA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 763 DVRTRgpVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRI 838
Cdd:COG2274 546 SLRRQ--IGVVLQDVFLFSGTIRENITLGDPdATDEE---IIEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRL 620
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
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 ... |
373-611 |
6.22e-54 |
|
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: 190.74 E-value: 6.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 373 FLQASYYVAIETGINLRGAIQTKIYNKIMQLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 452
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 453 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMT 532
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 533 SLRAFAVYTSISIFMNTAIPIAAVLITFVghVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 611
Cdd:cd18597 217 YVRKLQILRSILTAVAFSLPVLASMLSFI--TYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1081-1569 |
7.09e-50 |
|
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: 187.23 E-value: 7.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1081 VTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISY- 1159
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYy 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1160 ---VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTtqlplLSHFA-ETVEGLTTIRAFRYEARFQQKLLEYTDSNN 1235
Cdd:TIGR02203 153 swqLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQ-----VTTVAeETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1236 IASLFLTAANRWLEVRMEYIG--ACVVLIAAATSISNSlhRELSAG-LVGLGLTYALMVSNylnwmVRNLADMEIQ---- 1308
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIAslALAVVLFIALFQAQA--GSLTAGdFTAFITAMIALIRP-----LKSLTNVNAPmqrg 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1309 LGAVKRIHALLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSF 1388
Cdd:TIGR02203 301 LAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1389 SLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkCSDSTLWEALEIAQLKLVVK 1465
Cdd:TIGR02203 375 VNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTEQ-ADRAEIERALAAAYAQDFVD 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1466 ALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILS 1545
Cdd:TIGR02203 454 KLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK 533
|
490 500
....*....|....*....|....
gi 1490492289 1546 ADLVMVLKRGAILEFDKPETLLNQ 1569
Cdd:TIGR02203 534 ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1345-1555 |
7.95e-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: 174.49 E-value: 7.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPVLFSGTIRFNLdpekkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFI 1504
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 1505 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRG 1555
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; ... |
312-609 |
2.02e-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: 178.46 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 312 LLGFAGPLCIFGIVDHLgkENHVFQPKTQ--------FLGVyFVSSQeflgnayvlavllflalllqrtFLQASYYVAIE 383
Cdd:cd18596 11 VLSFAPPFFLNRLLRYL--EDPGEDATVRpwvwvlllFLGP-LLSSL----------------------LDQQYLWIGRR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 384 TGINLRGAIQTKIYNKIMQL-----------------STSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQI 446
Cdd:cd18596 66 LSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 447 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMT 526
Cdd:cd18596 146 VIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 527 RKKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKEsDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALV 606
Cdd:cd18596 226 REEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQ-ELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKV 304
|
...
gi 1490492289 607 SVQ 609
Cdd:cd18596 305 SLD 307
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
691-921 |
5.67e-47 |
|
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: 178.41 E-value: 5.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQETVadsdvrtRGPV 770
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN------GVDLSDLDPASW-------RRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 849
Cdd:COG4988 414 AWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 850 VVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:COG4988 494 LLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1343-1582 |
5.77e-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: 167.34 E-value: 5.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1343 GKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMfEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1502
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1503 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQKDSIFASFVRADK 1582
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDR 239
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
373-611 |
6.73e-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: 6.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 373 FLQASYYVAIETGINLRGAIQTKIYNKIMQLStsnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 452
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 453 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMT 532
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 533 SLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 611
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAHVAL--GNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1065-1570 |
1.20e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 175.29 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1065 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1144
Cdd:PRK10790 68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1145 RSTLLcVSALTVISYVTP--VFLVALL--PLAVVCYFIQKYF------RVASRdLQQLDDTtqlpllshFAETVEGLTTI 1214
Cdd:PRK10790 148 RSAAL-IGAMLVAMFSLDwrMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEVINGMSVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1215 RAFRYEARFQQKLLEYTDSNNIASL-------FLTaanRWLEVRMEYIGACVVLIAAATSisnslhrelSAGLVGLGLTY 1287
Cdd:PRK10790 218 QQFRQQARFGERMGEASRSHYMARMqtlrldgFLL---RPLLSLFSALILCGLLMLFGFS---------ASGTIEVGVLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1288 ALMvsNYLNWMVRNLADMEIQ-------LGAVKRIHALLKTEAESYegllAPSLIPKNwpdQGKIQIQNLSVRYDSSlKP 1360
Cdd:PRK10790 286 AFI--SYLGRLNEPLIELTTQqsmlqqaVVAGERVFELMDGPRQQY----GNDDRPLQ---SGRIDIDNVSFAYRDD-NL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1361 VLKHVNALISPGQKIGICGRTGSGKSSfsLAFFRM----VDMFEGRIIIDGIdiAKLPLHTLRSRLSIILQDPVLFSGTI 1436
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyypLTEGEIRLDGRPL--SSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1437 RFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1516
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1517 ENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQK 1570
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1345-1576 |
4.56e-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: 163.17 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1501
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1502 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNqKDSIFAS 1576
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAE 231
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
306-611 |
6.27e-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: 161.95 E-value: 6.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 306 FRILADLLGFAGPLCIFGIVDHLgkENHVFQPKTQFL--GVYFVSSqeFLGnayvlavllflalllqrTFLQASY-YVAI 382
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFL--EDSSEPLSDGYLyaLGLVLSS--LLG-----------------ALLSSHYnFQMN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 383 ETGINLRGAIQTKIYNKIMQLSTSnlSMGEMTAGQICNLVAIDTNQLMWFfflCPNL---WAMPVQIIVGVILLYYILGV 459
Cdd:cd18598 64 KVSLKVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 460 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLR---- 535
Cdd:cd18598 139 AFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKgrky 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 536 --AFAVYtsisiFMNTAiPIAAVLITFVGHVsfFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 611
Cdd:cd18598 219 ldALCVY-----FWATT-PVLISILTFATYV--LMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
446-913 |
2.28e-42 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 164.94 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 446 IIVGVILLYYILGVSALI---GAAVIILLAPVqyFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSR 522
Cdd:COG4987 143 ILAAVAFLAFFSPALALVlalGLLLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALAR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 523 VEMTRKKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPS----VAFASLSLFHILVTplflLSSVV 598
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPllalLVLAALALFEALAP----LPAAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 599 RSTVKALVSVQKLSEFLSSAeiheeqcaPREPAPQGQAGKYQAVPLKvvnrkrpareevrdllgpLQRLTpsmdgdadnf 678
Cdd:COG4987 297 QHLGRVRAAARRLNELLDAP--------PAVTEPAEPAPAPGGPSLE------------------LEDVS---------- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 679 cvqiiggfFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSspeqeT 758
Cdd:COG4987 341 --------FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG------GVDLR-----D 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 759 VADSDVRTRgpVAYASQKPWLLNATVEENITFESPfNKQRYKM--VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQ 836
Cdd:COG4987 402 LDEDDLRRR--IAVVPQRPHLFDTTLRENLRLARP-DATDEELwaALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
693-918 |
4.85e-42 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 156.17 E-value: 4.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdsegedpsspeqetvadsdvRTRGPVAY 772
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------------------KHSGRISF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVF 852
Cdd:cd03291 103 SSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 853 LDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 918
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1345-1570 |
1.27e-41 |
|
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: 153.16 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1501
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 1502 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQK 1570
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1345-1580 |
4.41e-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: 151.92 E-value: 4.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLK-PVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 1423
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1424 IILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1500
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1501 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLnQKDSIFASFVRA 1580
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM-AQKGVYAKLVKA 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1093-1571 |
7.12e-41 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 162.58 E-value: 7.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1093 VAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVAL 1168
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrltmVTLINL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1169 LPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPLlshfaETVEGLTTIRAF---RYEA-RFQQKLLEYTDSN---NIASLF 1240
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFaaeEGEAsRFKEALEETLQLNkrkALAYAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1241 LTAANRWLE----VRMEYIGACVVLIAaatsisnslhrELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1316
Cdd:TIGR00958 387 YLWTTSVLGmliqVLVLYYGGQLVLTG-----------KVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVF 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1317 ALL-KTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDS-SLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFR 1394
Cdd:TIGR00958 456 EYLdRKPNIPLTGTLAPL------NLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1395 MVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPE-KKCSDSTLWEALEIAQLKLVVKALPGGLDA 1473
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDT 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1474 IITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILSADLVMVLK 1553
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLK 687
|
490
....*....|....*...
gi 1490492289 1554 RGAILEFDKPETLLNQKD 1571
Cdd:TIGR00958 688 KGSVVEMGTHKQLMEDQG 705
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
687-912 |
1.57e-40 |
|
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: 149.66 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLpDSEGEDPSspeqetvadsDVRT 766
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT-DIRQLDPA----------DLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RgpVAYASQKPWLLNATVEENITFESPF-NKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 845
Cdd:cd03245 79 N--IGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 846 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 912
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
687-906 |
2.43e-40 |
|
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: 147.14 E-value: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgedpsspeqetVADSDVRT 766
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD-----------LDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RgpVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQ 846
Cdd:cd03228 77 N--IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 906
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEA-LRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1024-1295 |
4.46e-40 |
|
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: 150.10 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1024 HMVLVAIDYWLAKWTDSALVLSPAARNcslsqecalDQSVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLN 1103
Cdd:pfam00664 12 GAISPAFPLVLGRILDVLLPDGDPETQ---------ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1104 CIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFR 1183
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1184 VASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIA 1263
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 1490492289 1264 AATSISNSLHRELSAGLVGLGLTYALMVSNYL 1295
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
686-913 |
7.66e-40 |
|
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: 148.15 E-value: 7.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 686 FFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATlgemqkvsgavFWnslpdsegeDPSSPeQETVADSD 763
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPR-----------FY---------DVDSG-RILIDGHD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 764 VRT------RGPVAYASQKPWLLNATVEENITFESPfNKQRyKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQ 834
Cdd:cd03251 66 VRDytlaslRRQIGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 835 RQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1343-1557 |
4.29e-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: 145.42 E-value: 4.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1343 GKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRK 1499
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 1500 TSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 1557
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1074-1579 |
9.76e-38 |
|
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: 152.79 E-value: 9.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1074 LGIVLCLVTSVTVEWTGLKVAKRLH--------HSLLNCIILAPMRFFETTPLGSILNRFSSDcNTIDQHIPSTLECLSR 1145
Cdd:TIGR03796 198 LGMGLTALLQGVLTWLQLYYLRRLEiklavgmsARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTAL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1146 STLLCV-SALTVISYVTPVFLVALLPLAV---VCYFIQKYFRVASRDLQQldDTTQLpllshFAETVEGLTTIR------ 1215
Cdd:TIGR03796 277 DAVMLVfYALLMLLYDPVLTLIGIAFAAInvlALQLVSRRRVDANRRLQQ--DAGKL-----TGVAISGLQSIEtlkasg 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1216 ----AFRYEARFQQKLL----EYTDSNNIASL---FLTAAN----------RWLEVRMEyIGACVvliaAATSISNSLHR 1274
Cdd:TIGR03796 350 lesdFFSRWAGYQAKLLnaqqELGVLTQILGVlptLLTSLNsalilvvgglRVMEGQLT-IGMLV----AFQSLMSSFLE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1275 ELSaGLVGLGLTyalmvsnylnwmvrnLADMEiqlGAVKRIHALLKTEAESYEGLLAP--SLIPKNWPDQGKIQIQNLSV 1352
Cdd:TIGR03796 425 PVN-NLVGFGGT---------------LQELE---GDLNRLDDVLRNPVDPLLEEPEGsaATSEPPRRLSGYVELRNITF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1353 RYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSlaffRMVD----------MFEGRIIidgidiAKLPLHTLRSRL 1422
Cdd:TIGR03796 486 GYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIA----KLVAglyqpwsgeiLFDGIPR------EEIPREVLANSV 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFSGTIRFNL---DPekKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRK 1499
Cdd:TIGR03796 556 AMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1500 TSIFIMDEATASIDMATEnilqKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLnQKDSIFASF 1577
Cdd:TIGR03796 634 PSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELW-AVGGAYARL 708
|
..
gi 1490492289 1578 VR 1579
Cdd:TIGR03796 709 IR 710
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
319-611 |
1.41e-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: 140.46 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 319 LCIFGIVDHLGKenhVFQPktQFLG---VYFV-SSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQT 394
Cdd:cd18594 2 LGILLFLEESLK---IVQP--LLLGrlvAYFVpDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 395 KIYNKIMQLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPV 474
Cdd:cd18594 77 LIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 475 QYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLR--AFAVYTSISIFMNTAIP 552
Cdd:cd18594 155 QAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRkaAYIRAFNMAFFFFSPTL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 553 IaaVLITFVGHVSFFKESDfsPSVAFASLSLFHILVTPL-FLLSSVVRSTVKALVSVQKL 611
Cdd:cd18594 235 V--SFATFVPYVLTGNTLT--ARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1081-1570 |
5.11e-36 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 145.93 E-value: 5.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1081 VTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYV 1160
Cdd:PRK11176 84 ISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1161 T---PVFLVALLPL-AVVCYFIQKYFRVASRDLQ----QLDDTTQLPL------LSHFAETVEglttirafryEARFQQK 1226
Cdd:PRK11176 164 SwqlSLILIVIAPIvSIAIRVVSKRFRNISKNMQntmgQVTTSAEQMLkghkevLIFGGQEVE----------TKRFDKV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1227 lleytdSNNI--ASLFLTAANRWLEVRMEYIGA---CVVLIAAATSisnSLHRELSAGlvglglTYALMVSNYLNWM--V 1299
Cdd:PRK11176 234 ------SNRMrqQGMKMVSASSISDPIIQLIASlalAFVLYAASFP---SVMDTLTAG------TITVVFSSMIALMrpL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1300 RNLADMEIQ----LGAVKRIHALLKTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKI 1375
Cdd:PRK11176 299 KSLTNVNAQfqrgMAACQTLFAILDLEQEKDEGKRVIE------RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1376 GICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPEKKCSDSTLWE 1453
Cdd:PRK11176 373 ALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1454 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 1533
Cdd:PRK11176 453 AARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS 532
|
490 500 510
....*....|....*....|....*....|....*..
gi 1490492289 1534 VTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQK 1570
Cdd:PRK11176 533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
377-618 |
6.56e-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: 138.51 E-value: 6.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 377 SYYVAIETGINLRGAIQTKIYNKIMQLSTSnlSMGEMTAGQICNLVAIDTNQL-MWFFFLcPNLWAMPVQIIVGVILLYY 455
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 456 ILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLR 535
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 536 --AFAVYTSISIFMntaipIAAVLITFVGHVSFF-KESDFSPSVAFASLSLFHilvtplfllssVVRSTVKALV--SVQK 610
Cdd:cd18593 217 rtSFLRALNMGLFF-----VSSKLILFLTFLAYIlLGNILTAERVFVTMALYN-----------AVRLTMTLFFpfAIQF 280
|
....*...
gi 1490492289 611 LSEFLSSA 618
Cdd:cd18593 281 GSELSVSI 288
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
693-913 |
6.62e-36 |
|
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: 136.59 E-value: 6.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQETVadsdvrtRGPVAY 772
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID------GIDIRDISRKSL-------RSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWLLNATVEENITFESPFNKQryKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 849
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 850 VVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03254 160 ILILDEATSNIDTE-TEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1109-1570 |
7.77e-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: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1109 PMRFFETTPLGSILNRFSsDCNTIDQHIPSTLeclsRSTLLCVSALTVISYV-----TPVFLVALLPL---AVVCYFIQK 1180
Cdd:TIGR01193 243 PMSFFSTRRTGEIVSRFT-DASSIIDALASTI----LSLFLDMWILVIVGLFlvrqnMLLFLLSLLSIpvyAVIIILFKR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1181 YFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYEA-RFQQ----------KLLEYTDSNNIASLFLTAANRWLE 1249
Cdd:TIGR01193 318 TFNKLNHDAMQ----ANAVLNSSIIEDLNGIETIKSLTSEAeRYSKidsefgdylnKSFKYQKADQGQQAIKAVTKLILN 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1250 VRMEYIGACVVLIAAATsisnslhrelsaglVGLGLTYALMVSNYLNwMVRNLADMEIQLGAVK----RIHALLKTEAES 1325
Cdd:TIGR01193 394 VVILWTGAYLVMRGKLT--------------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvannRLNEVYLVDSEF 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1326 YEGLLAPSLIPKNwpdqGKIQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIII 1405
Cdd:TIGR01193 459 INKKKRTELNNLN----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1406 DGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFS 1483
Cdd:TIGR01193 534 NGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSIS 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1484 QGQRQLFCLARAFVRKTSIFIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFD 1561
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
|
....*....
gi 1490492289 1562 KPETLLNQK 1570
Cdd:TIGR01193 691 SHDELLDRN 699
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1345-1567 |
8.79e-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: 136.46 E-value: 8.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPVLFSGTIRFNL---DPekKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1501
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 1502 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLL 1567
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1147-1552 |
1.71e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 143.58 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1147 TLLCVSALTVISYVTPVFLVALLPLAVVcYFIQKYFRVASRDLQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQK 1226
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPLIPI-FMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1227 LLEYTDSNniaslfltaANRWLEV-RMEYIGACVVLIAAATSISnslhreLSAGLVGLGLTY----------ALMVSNYL 1295
Cdd:TIGR02857 209 IRRSSEEY---------RERTMRVlRIAFLSSAVLELFATLSVA------LVAVYIGFRLLAgdldlatglfVLLLAPEF 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1296 NWMVRNL-----ADMEIQlGAVKRIHALLkteaeSYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIS 1370
Cdd:TIGR02857 274 YLPLRQLgaqyhARADGV-AAAEALFAVL-----DAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVP 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1371 PGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEKkcS 1447
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--S 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1448 DSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTA 1527
Cdd:TIGR02857 425 DAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL 504
|
410 420
....*....|....*....|....*
gi 1490492289 1528 FADRTVVTIAHRVHTILSADLVMVL 1552
Cdd:TIGR02857 505 AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1293-1570 |
9.77e-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: 142.27 E-value: 9.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1293 NYLNWMVR----NLADMEiqlgavkRIHALLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSlKPVLKHVNAL 1368
Cdd:COG5265 313 NFLGFVYReirqALADME-------RMFDLLDQPPEVADAPDAPPLVVG----GGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1369 ISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkk 1445
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPD-- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1446 CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM 1525
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1490492289 1526 TAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQK 1570
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
691-913 |
1.20e-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: 133.43 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDgIPTLSNISIRIPRGQLTMIVGQVGCGKS---SLLLAtlgemqkvsgavFWnslpdsegeDPSSPEQeTVADSDVRT- 766
Cdd:cd03249 14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKStvvSLLER------------FY---------DPTSGEI-LLDGVDIRDl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 -----RGPVAYASQKPWLLNATVEENITFESPFNKQryKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRI 838
Cdd:cd03249 71 nlrwlRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
376-913 |
2.00e-34 |
|
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: 141.01 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 376 ASYYVAIETGINLRGaIQTKIYNKIMQLSTSNLSmgEMTAGQICNLVAIDTNQLmwfffLCPNLWAMPVQI-----IVG- 449
Cdd:TIGR02203 74 STYLLSWVSNKVVRD-IRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQV-----ASAATDAFIVLVretltVIGl 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 450 -VILLYYILGVSAligaaVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTN----EMLRGIKLLKLYAWE----NIFC 520
Cdd:TIGR02203 146 fIVLLYYSWQLTL-----IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaeETLQGYRVVKLFGGQayetRRFD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 521 SRVEMTRKKEMTSLRAFAVYTSISIFmntaipIAAVLITFVGHVSFFKESDFSPSVA-FASLSLFHILV-TPLFLLSSVV 598
Cdd:TIGR02203 221 AVSNRNRRLAMKMTSAGSISSPITQL------IASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALiRPLKSLTNVN 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 599 RSTVKALVSVQKLSEFLSSAeiheeqcaprepaPQGQAGKyqavplKVVNRKRpAREEVRDLLgplqrltpsmdgdadnf 678
Cdd:TIGR02203 295 APMQRGLAAAESLFTLLDSP-------------PEKDTGT------RAIERAR-GDVEFRNVT----------------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 679 cvqiiggfFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLlatlgemqkvsgavfwNSLPD----SEGE---DP 751
Cdd:TIGR02203 338 --------FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLV----------------NLIPRfyepDSGQillDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 752 SSPEQETVADsdvrTRGPVAYASQKPWLLNATVEENITFESP--FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGIN 829
Cdd:TIGR02203 394 HDLADYTLAS----LRRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQ 909
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
....
gi 1490492289 910 REGT 913
Cdd:TIGR02203 547 ERGT 550
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1215-1579 |
2.29e-34 |
|
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: 142.02 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1215 RAF-RYEARF-QQKLLEYtDSNNIASlFLTAANRWLEVRmeyigACVVLIAAATSIsnslhreLSAGLVGLG--LTYALM 1290
Cdd:TIGR03797 335 RAFaRWAKLFsRQRKLEL-SAQRIEN-LLTVFNAVLPVL-----TSAALFAAAISL-------LGGAGLSLGsfLAFNTA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1291 VSNYLNWMvRNLADMEIQLGAV----KRIHALLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVN 1366
Cdd:TIGR03797 401 FGSFSGAV-TQLSNTLISILAViplwERAKPILEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1367 ALISPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGID----IAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdp 1442
Cdd:TIGR03797 474 LQIEPGEFVAIVGPSGSGKSTL----LRLLLGFETPESGSVFYdgqdLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-- 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1443 ekkCSDSTL-----WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDmate 1517
Cdd:TIGR03797 548 ---AGGAPLtldeaWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD---- 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1518 NILQKVVMTAFA--DRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNqKDSIFASFVR 1579
Cdd:TIGR03797 621 NRTQAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REGLFAQLAR 683
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
691-913 |
4.34e-34 |
|
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: 131.58 E-value: 4.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQkvSGAVFWNslpdseGEDPSSPEQETVadsdvrtRG 768
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIlrLLFRFYDVS--SGSILID------GQDIREVTLDSL-------RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 PVAYASQKPWLLNATVEENITFESP--FNKQrykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 843
Cdd:cd03253 76 AIGVVPQDTVLFNDTIGYNIRYGRPdaTDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 844 LYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03253 152 ILKNPPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGT 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
695-913 |
1.30e-33 |
|
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: 138.34 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeqetVADSDVRTRGP-VAYA 773
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD------GAD--------LSQWDREELGRhIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQKPWLLNATVEENIT-FESPfNKQRykmVIEACSLqpdIDI------LPHGDQTQIGERGINLSGGQRQRISVARALYQ 846
Cdd:COG4618 412 PQDVELFDGTIAENIArFGDA-DPEK---VVAAAKL---AGVhemilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAA--IRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
691-903 |
3.20e-33 |
|
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: 136.65 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgedpsspeqetvADSDVRtRGPV 770
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD------------ADADSW-RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNATVEENITFESPFNKQ-RYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 849
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 850 VVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAM 903
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEA-LRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
380-913 |
8.46e-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: 135.55 E-value: 8.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 380 VAIETGINLRGAIQTKIYNKIMQlstSNLSMGEMTAGQICNlvaiDTNQLMWF--------FFLCPnlWaMPVQIIVgVI 451
Cdd:TIGR01842 69 VLVRIGEKLDGALNQPIFAASFS---ATLRRGSGDGLQALR----DLDQLRQFltgpglfaFFDAP--W-MPIYLLV-CF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 452 LLYYILGVSALIGAAVIILLAPV-QYFVATKLSQAQrstlEYSNERLKQTNEMLRGIKLLK-------LYA-WENifcSR 522
Cdd:TIGR01842 138 LLHPWIGILALGGAVVLVGLALLnNRATKKPLKEAT----EASIRANNLADSALRNAEVIEamgmmgnLTKrWGR---FH 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 523 VEMTRKKEMTSLRAFAVYTSISIFMNtaipIAAVLITFVG-HVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRST 601
Cdd:TIGR01842 211 SKYLSAQSAASDRAGMLSNLSKYFRI----VLQSLVLGLGaYLAI--DGEITPGMMIAGSILVGRALAPIDGAIGGWKQF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 602 VKALVSVQKLSEFLssAEIHEEQCAPREPAPQGQagkyqavpLKVvnrkrparEEVrDLLGPLQRLtpsmdgdadnfcvq 681
Cdd:TIGR01842 285 SGARQAYKRLNELL--ANYPSRDPAMPLPEPEGH--------LSV--------ENV-TIVPPGGKK-------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 682 iiggfftwtpdgiPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpDSEGEDPSSPEQETVAD 761
Cdd:TIGR01842 332 -------------PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV------RLDGADLKQWDRETFGK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 762 SdvrtrgpVAYASQKPWLLNATVEENIT-FESPFNKQRykmVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQR 837
Cdd:TIGR01842 393 H-------IGYLPQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILRLPDGYDTVIGPGGATLSGGQRQR 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 838 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
300-591 |
4.78e-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: 126.99 E-value: 4.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 300 LVLSSTFRILADLLGFAGPLCIFGIVDHLGKEN-HVFQPKTQFLGVYFVssqeflgnayvlavllflALLLQRTFLQASY 378
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGdPETQALNVYSLALLL------------------LGLAQFILSFLQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 379 YVAIETGINLRGAIQTKIYNKIMQLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILG 458
Cdd:pfam00664 63 YLLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 459 VS-ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLRAF 537
Cdd:pfam00664 141 WKlTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKK 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 538 AVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPL 591
Cdd:pfam00664 221 AVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
687-907 |
1.38e-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: 120.65 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdsegedpsspEQETVADSDVRT 766
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-------------GKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 836
Cdd:cd03225 74 RRKVGLVFQNPddQFFGPTVEEEVAF-GLENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 907
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1342-1580 |
1.98e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 128.93 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1342 QGKIQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSR 1421
Cdd:PRK13657 332 KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1422 LSIILQDPVLFSGTIRFNLDPEKK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1500
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1501 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILE---FDKpetlLNQKDSIFASF 1577
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAAL 566
|
...
gi 1490492289 1578 VRA 1580
Cdd:PRK13657 567 LRA 569
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1063-1314 |
2.59e-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: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1063 VYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC 1142
Cdd:cd18559 39 VYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1143 LSRSTLLCVSALTVISYVTPVFLVAlLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEAR 1222
Cdd:cd18559 119 WMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1223 FQQKLLEYTDsNNIASLFLTAANRWLEVRMEYIGACVVLIAA-ATSISnslhRELSAGLVGLGLTYALMVSNYLNWMVRN 1301
Cdd:cd18559 198 FIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASfFAYVS----RHSLAGLVALKVFYSLALTTYLNWPLNM 272
|
250
....*....|...
gi 1490492289 1302 LADMEIQLGAVKR 1314
Cdd:cd18559 273 SPEVITNIVAAEV 285
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
687-911 |
2.76e-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: 121.35 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPeqetvadsdvrt 766
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD------GKPVTGP------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGPVAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGG 833
Cdd:COG1116 79 GPDRGVVFQEpallPWL---TVLDNVALglelrgVPK--AERRERArelLELVGLAGFEDAYPH-----------QLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 834 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAMKD--GTI 908
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSArpGRI 219
|
...
gi 1490492289 909 QRE 911
Cdd:COG1116 220 VEE 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
687-921 |
3.07e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 120.67 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnslpdSEGEDPSSPEQETVadsdvrt 766
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL------VDGHDLALADPAWL------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGPVAYASQKPWLLNATVEENITFESPFNKQRykMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 843
Cdd:cd03252 75 RRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 844 LYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:cd03252 153 LIHNPRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1119-1539 |
5.62e-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: 126.71 E-value: 5.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1119 GSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF-----RVASRDLQQLD 1193
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVslraaRAAEQALARLR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1194 DTtqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLH 1273
Cdd:TIGR02868 190 GE----LAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVAD 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1274 RELSAG------LVGLGLTYALMVsnylnwmvrnLADMEIQLGAVK----RIHALLKTEAESYEGLL-APSLIPKNWPDq 1342
Cdd:TIGR02868 266 GRLAPVtlavlvLLPLAAFEAFAA----------LPAAAQQLTRVRaaaeRIVEVLDAAGPVAEGSApAAGAVGLGKPT- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1343 gkIQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:TIGR02868 335 --LELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFSGTIRFNL---DPEkkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRK 1499
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENLrlaRPD--ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLAD 489
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1490492289 1500 TSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1539
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
382-935 |
7.13e-30 |
|
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: 128.15 E-value: 7.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 382 IETGINlrGAIQTKIYNKIMQL--------STSNLSMGEMTAGQICNLVAIDT-NQLMWFFFLCPNLWampvqiivgviL 452
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLG-----------L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 453 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAWENIFCSRVE 524
Cdd:TIGR03797 270 MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 525 MTRKKEM------TSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFkesdfspsVAFASLSlfhilvtplfllsSVV 598
Cdd:TIGR03797 350 LELSAQRienlltVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFN--------TAFGSFS-------------GAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 599 RSTVKALVSVqklseflssaeiheeqcaprepapqgqagkYQAVPLkvVNRKRP---AREEVRDLLGPLQRLTPSMDgdA 675
Cdd:TIGR03797 409 TQLSNTLISI------------------------------LAVIPL--WERAKPileALPEVDEAKTDPGKLSGAIE--V 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 676 DNFCvqiiggfFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPSSPE 755
Cdd:TIGR03797 455 DRVT-------FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFY------DGQDLAGLD 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 756 QETVAdsdvRTRGPVAYASQkpwLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 835
Cdd:TIGR03797 522 VQAVR----RQLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQR 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 836 QRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 915
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYD 669
|
570 580
....*....|....*....|
gi 1490492289 916 DFQRSEYQLFEhwktLMNRQ 935
Cdd:TIGR03797 670 ELMAREGLFAQ----LARRQ 685
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
692-921 |
1.27e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.04 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSspeqetvadsdvRTRGPVA 771
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF------GKPPR------------RARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRISV 840
Cdd:COG1121 79 YVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADR-PIGE----LSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 841 ARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIqREGTLKDFQR 919
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVReYFDRVLLLNRGLV-AHGPPEEVLT 227
|
..
gi 1490492289 920 SE 921
Cdd:COG1121 228 PE 229
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1165-1569 |
1.28e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.98 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1165 LVALLPLAVVCYFIQKY-------FRVASRDLQQLDDTTQlpllshfaetvEGLTTIR---AFRyearfqqklLEYTDSN 1234
Cdd:PRK10789 141 LLALLPMPVMAIMIKRYgdqlherFKLAQAAFSSLNDRTQ-----------ESLTSIRmikAFG---------LEDRQSA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1235 NIASLFLTAANRWLEV-RMEYIGACVVLIAAATS------------ISNSLHR-ELSAGLVGLGLTYALMVSnyLNWMVr 1300
Cdd:PRK10789 201 LFAADAEDTGKKNMRVaRIDARFDPTIYIAIGMAnllaigggswmvVNGSLTLgQLTSFVMYLGLMIWPMLA--LAWMF- 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1301 NLadMEIQLGAVKRIHALLKTEAESYEGLLApslIPknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGR 1380
Cdd:PRK10789 278 NI--VERGSAAYSRIRAMLAEAPVVKDGSEP---VP---EGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1381 TGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpEKKCSDSTLWEALEIAQL 1460
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI--ALGRPDATQQEIEHVARL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1461 KLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAfADRTVVTI 1536
Cdd:PRK10789 428 ASVhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHNLRQWG-EGRTVIIS 506
|
410 420 430
....*....|....*....|....*....|...
gi 1490492289 1537 AHRVHTILSADLVMVLKRGAILEFDKPETLLNQ 1569
Cdd:PRK10789 507 AHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1089-1315 |
1.31e-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: 121.45 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1089 TGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVAL 1168
Cdd:cd18600 97 TLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLAT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1169 LPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFR----YEARFQQKLLEYTdsnniASLFL-TA 1243
Cdd:cd18600 177 VPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHT-----ANWFLyLS 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 1244 ANRWLEVRMEYIgaCVVLIAAATSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1315
Cdd:cd18600 252 TLRWFQMRIEMI--FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
688-913 |
3.21e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 118.22 E-value: 3.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 688 TWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQETVAdsdvRTr 767
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD------GRDLASLSRRELA----RR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 768 gpVAYASQK---PWLLnaTVEENI--------TFESPFNKQRYKMVIEACslqpdidilphgDQTQIG---ERGIN-LSG 832
Cdd:COG1120 77 --IAYVPQEppaPFGL--TVRELValgryphlGLFGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL-QYLPHADWIIAMKDGT 907
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKDGR 215
|
....*.
gi 1490492289 908 IQREGT 913
Cdd:COG1120 216 IVAQGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
691-917 |
6.88e-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: 116.28 E-value: 6.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSspeQETVADsdVRTRgpV 770
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD------GKDIT---KKNLRE--LRRK--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPW--LLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 840
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAF-GPENlglpreeiRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 841 ARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTIQREGTLKDF 917
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
691-913 |
9.87e-29 |
|
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: 115.67 E-value: 9.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSspeqeTVADSDVRTRgpV 770
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID------GVDIS-----KIGLHDLRSR--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNATVEENItfeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 847
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 848 TNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03244 158 SKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
690-913 |
1.41e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 123.03 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ-----KVSGaVFWNSLpdsegeDPSSpeqetvadsdv 764
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKING-IELREL------DPES----------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 765 rTRGPVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 843
Cdd:PRK11174 421 -WRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 844 LYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQA--LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
306-611 |
1.80e-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: 116.93 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 306 FRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVS--SQEFLGNAYvlavllflalllqrtflqasYYVAIE 383
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALaiLQGITVFQY--------------------SMAVSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 384 TGINLRGAIQTKIYNKIMQLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALI 463
Cdd:cd18559 65 GGIFASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 464 GAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLRAFAVYTSI 543
Cdd:cd18559 143 GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 544 SIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 611
Cdd:cd18559 223 AVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1328-1557 |
4.70e-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: 113.72 E-value: 4.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1328 GLLAPSLIpknwpdQGKIQIQNLSVRYDS-SLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMvdmFEGRIIID 1406
Cdd:cd03248 1 GSLAPDHL------KGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF---YQPQGGQV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1407 GIDIAKLPLHT---LRSRLSIILQDPVLFSGTIRFNLD-PEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENF 1482
Cdd:cd03248 72 LLDGKPISQYEhkyLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1483 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 1557
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
697-911 |
5.77e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 113.34 E-value: 5.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdsegedpsspeqeTVADSDVRTRGP-VAYASQ 775
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-------------------LVDGEPVTGPGPdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 K----PWLlnaTVEENITFesPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 842
Cdd:cd03293 81 QdallPWL---TVLDNVAL--GLElqgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 843 ALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM--KDGTIQRE 911
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQ-LQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1345-1555 |
6.91e-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: 6.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDS---SLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAffrmvdmfegriiidgiDIAKLPLH----T 1417
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSA-----------------LLGELEKLsgsvS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1418 LRSRLSIILQDPVLFSGTIRFN------LDPEKkcsdstLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFC 1491
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENilfgkpFDEER------YEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 1492 LARAFVRKTSIFIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILSADLVMVLKRG 1555
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
697-912 |
2.78e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.22 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdsegedpsspeqeTVADSDVRTRGP------V 770
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------------------LLDGKDLASLSPkelarkI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQkpwllnatveenitfespfnkqrykmVIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQRISVARALYQHTN 849
Cdd:cd03214 76 AYVPQ--------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 850 VVFLDDPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 912
Cdd:cd03214 118 ILLLDEPTSHLDIA-----HQIELLELLRRLARergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
687-912 |
3.36e-27 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 111.07 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeqetVADSDVRT 766
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID------GRD--------VTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGpVAYASQK----PWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQR 835
Cdd:cd03259 72 RN-IGMVFQDyalfPHL---TVAENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 836 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 912
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
687-908 |
4.26e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.68 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgedpSSPEQetvadsdVRT 766
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA----MPPPE-------WRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RgpVAYASQKPWLLNATVEENITF-----ESPFNKQRYKMVIEACSLQPDIdiLphgdQTQIGErginLSGGQRQRISVA 841
Cdd:COG4619 75 Q--VAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI--L----DKPVER----LSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEEL-LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
695-959 |
4.40e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 118.28 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSegedpsspeqeTVADSDVRTRgpVAYAS 774
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-----------KLQLDSWRSR--LAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFL 853
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 854 DDPFSALDVHlSDHlmqaGILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKdfqrseyQLFEH--WK 929
Cdd:PRK10789 476 DDALSAVDGR-TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD-------QLAQQsgWY 543
|
250 260 270
....*....|....*....|....*....|
gi 1490492289 930 TLMNRQdQELEKEtvLErKAPEPSQGLPRA 959
Cdd:PRK10789 544 RDMYRY-QQLEAA--LD-DAPEIREEAVDA 569
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
697-920 |
1.60e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.77 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSpeqetvADSDVRTRgpVAYASQK 776
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL------GEDVAR------DPAEVRRR--IGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWL-LNATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARALYQHT 848
Cdd:COG1131 82 PALyPDLTVRENLRFfarlyglPRKEARERIDELLELFGLTDAAD-------RKVG----TLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 849 NVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKDFQRS 920
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
687-921 |
2.10e-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: 117.15 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQKvsGAVFWNSLpDSEGEDPSSpeqetvadsdv 764
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQH--GQVLVDGV-DLAIADPAW----------- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 765 rTRGPVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRISVA 841
Cdd:TIGR01846 529 -LRRQMGVVLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIA 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
390-891 |
2.40e-26 |
|
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: 115.54 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 390 GAIQTKIYNKIMQLSTSnlSMGEMTAGQICNLVA--IDTNQLMWFFFLCPNLWAMPVQIIV--GVILLYYILGVSALIGA 465
Cdd:TIGR02868 86 GALRVRVYERLARQALA--GRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVGAAAvaAIAVLSVPAALILAAGL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 466 AVIILLAPvqyFVATKLSQAQRSTLEYS-NERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRKKEMTSLRAFAVYTSIS 544
Cdd:TIGR02868 164 LLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 545 IFMNTAIPIAAVLITFVGHVSFFKESDFSPS----VAFASLSLFHilvtPLFLLSSVVRSTVKALVSVQKLSEFLssaei 620
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADGRLAPVtlavLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVL----- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 621 heeqcAPREPAPQGQAGKYQAVPLKVVNRkrpareEVRDLLgplqrltpsmdgdadnfcvqiiggfFTWtPDGIPTLSNI 700
Cdd:TIGR02868 312 -----DAAGPVAEGSAPAAGAVGLGKPTL------ELRDLS-------------------------AGY-PGAPPVLDGV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 701 SIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQetvadSDVRTRgpVAYASQKPWLL 780
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD------GVPVSSLDQ-----DEVRRR--VSVCAQDAHLF 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 781 NATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSA 859
Cdd:TIGR02868 422 DTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
490 500 510
....*....|....*....|....*....|....
gi 1490492289 860 LDVHLSDHLmqagiLELLRD--DKRTVVLVTHKL 891
Cdd:TIGR02868 502 LDAETADEL-----LEDLLAalSGRTVVLITHHL 530
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
694-908 |
3.85e-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: 107.96 E-value: 3.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQKV-SGAVFwnslpdSEGEDPSS-PEQETvaDSDVRTRgpVA 771
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVR------VDGTDISKlSEKEL--AAFRRRH--IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLLNA-TVEENI----TFESPFNKQRYKMVIEACslqpdidilphgDQTQIGERgIN-----LSGGQRQRISVA 841
Cdd:cd03255 86 FVFQSFNLLPDlTALENVelplLLAGVPKKERRERAEELL------------ERVGLGDR-LNhypseLSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
692-904 |
9.70e-26 |
|
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: 106.85 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSegedpsspeqetvadsdvRTRGPVA 771
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------------------KERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRISV 840
Cdd:cd03235 72 YVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALER---VGLSELADR-QIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 841 ARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILEL---LRDDKRTVVLVTHKL-QYLPHADWIIAMK 904
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPK-----TQEDIYELlreLRREGMTILVVTHDLgLVLEYFDRVLLLN 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
697-921 |
9.84e-26 |
|
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: 107.59 E-value: 9.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPS--SPEQETvadsDVRTRgpVAYAS 774
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI------DGEDISglSEAELY----RLRRR--MGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 843
Cdd:cd03261 84 QSGALFDSlTVFENVAF--PLRehtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 844 LYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQ 918
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASG-----VIDDLIRSLKKelglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELR 225
|
...
gi 1490492289 919 RSE 921
Cdd:cd03261 226 ASD 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1310-1580 |
9.97e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 114.17 E-value: 9.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1310 GAVKRIHALLKTEAESYEGllAPSLIPKNWPDQgkIQIQNLSVR-YDSslKPVLKHVNALISPGQKIGICGRTGSGKSSF 1388
Cdd:PRK11174 319 GAAESLVTFLETPLAHPQQ--GEKELASNDPVT--IEAEDLEILsPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1389 ------------SLaffrMVDMFEGriiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPEkkCSDSTLWE 1453
Cdd:PRK11174 393 lnallgflpyqgSL----KINGIEL---------RELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQ 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1454 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 1533
Cdd:PRK11174 458 ALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT 537
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1490492289 1534 VTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQkDSIFASFVRA 1580
Cdd:PRK11174 538 LMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQA-GGLFATLLAH 583
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
687-916 |
1.54e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.58 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQkvSGAVFWNSLPDSEGEDPSSPEQetvadsdv 764
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDID--EGEILLDGHDLRDYTLASLRNQ-------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 765 rtrgpVAYASQKPWLLNATVEENITFESpfnKQRY--KMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRIS 839
Cdd:PRK11176 419 -----VALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRIA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1345-1559 |
1.99e-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: 104.70 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPlHTLRSRLSI 1424
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPVLFSGTIRFNLdpekkcsdstlwealeiaqlklvvkalpggldaiitegGENFSQGQRQLFCLARAFVRKTSIFI 1504
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1505 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILE 1559
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
694-912 |
2.07e-25 |
|
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: 106.44 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPSSPEQETVADsdvrTRGPVAYA 773
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF------DGKDLLKLSRRLRKI----RRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVI--EACSLQPDIDIL---PHGdqtqigerginLSGGQRQRISV 840
Cdd:cd03257 88 FQDPMSsLNPrmTIGEQIAeplriHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 841 ARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKDGTIQREG 912
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKLQEelglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
376-913 |
2.92e-25 |
|
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: 112.49 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 376 ASYYVAIETGINLRGAIQTKIYNKIMQLSTS----NLSmgemtaGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 451
Cdd:TIGR02204 77 ARFYLVTWLGERVVADIRRAVFAHLISLSPSffdkNRS------GEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 452 LLYYILGV--SALIGAAVIILLAPVqYFVATKLSQAQRStleySNERLKQTN----EMLRGIKLLKLYAWENI----FCS 521
Cdd:TIGR02204 151 IMMFITSPklTSLVLLAVPLVLLPI-LLFGRRVRKLSRE----SQDRIADAGsyagETLGAIRTVQAFGHEDAersrFGG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 522 RVEMTRKKEMTSLRAFAVYTSISIFMNTAipiAAVLITFVGhVSFFKESDFSPSV--AFASLSLFhiLVTPLFLLSSVVR 599
Cdd:TIGR02204 226 AVEKAYEAARQRIRTRALLTAIVIVLVFG---AIVGVLWVG-AHDVIAGKMSAGTlgQFVFYAVM--VAGSIGTLSEVWG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 600 STVKALVSVQKLSEFLSSAEIHEEQCAPREPAPQGQAgkyqAVPLKVVNRKRPAREEVrdllgplqrltpsmdgdadnfc 679
Cdd:TIGR02204 300 ELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRG----EIEFEQVNFAYPARPDQ---------------------- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 680 vqiiggfftwtpdgiPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGeDPSspeqetv 759
Cdd:TIGR02204 354 ---------------PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL-DPA------- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 760 adsDVRTRgpVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEAC-SLQPD--IDILPHGDQTQIGERGINLSGGQRQ 836
Cdd:TIGR02204 411 ---ELRAR--MALVPQDPVLFAASVMENIRYGRP--DATDEEVEAAArAAHAHefISALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVAQGT 557
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
691-920 |
4.07e-25 |
|
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: 105.85 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgEDPsspeqetvadsdVRTRGPV 770
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDP------------VELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLL-NATVEENIT-------FESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRISV 840
Cdd:cd03295 78 GYVIQQIGLFpHMTVEENIAlvpkllkWPKEKIRERADELLALVGLDPAefADRYPH-----------ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 841 ARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQR 919
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
.
gi 1490492289 920 S 920
Cdd:cd03295 226 S 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1345-1557 |
1.13e-24 |
|
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: 102.29 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFslaffrmvdmfegriiidgidiAKLPLHTLRsrlsi 1424
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTL----------------------ARLILGLLR----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ilqdPVlfSGTIRfnLDpekkCSDSTLWEALEIAQLklvVKALPGglDAIITEG--GEN-FSQGQRQLFCLARAFVRKTS 1501
Cdd:cd03246 54 ----PT--SGRVR--LD----GADISQWDPNELGDH---VGYLPQ--DDELFSGsiAENiLSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 1502 IFIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAI 1557
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
693-907 |
1.68e-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: 101.17 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQETVadsdvrtRGPVAY 772
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID------GKDIAKLPLEEL-------RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVVF 852
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 853 LDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 907
Cdd:cd00267 104 LDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
687-920 |
2.44e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 103.73 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEqetvadsDVRT 766
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD------GRPVTRRR-------RKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGPVAYASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVIEACSLQPDI-DILPHgdqtQigerginLSGGQRQR 837
Cdd:COG1124 78 RRRVQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYPH----Q-------LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 838 ISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 912
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
....*...
gi 1490492289 913 TLKDFQRS 920
Cdd:COG1124 222 TVADLLAG 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1340-1571 |
2.46e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.91 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1340 PDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSS-FSLaFFRMVDMFEGRIIIDGIDIAKLPLHTL 1418
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTlLQL-LTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1419 RSRLSIILQDPVLFSGTIRFNL---DPEKkcSDSTLWEALEIAQL-KLVvkALPGGLDAIITEGGENFSQGQRQLFCLAR 1494
Cdd:PRK11160 413 RQAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLeKLL--EDDKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 1495 AFVRKTSIFIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQKD 1571
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
686-913 |
3.45e-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: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 686 FFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSspeqeTVADSDVR 765
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD------GKDLT-----KLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 T-RGPVAYASQKPWL-LNA--TVEENITfESPFN------KQRYKMV---IEACSLQPD-IDILPHGdqtqigerginLS 831
Cdd:COG1123 339 ElRRRVQMVFQDPYSsLNPrmTVGDIIA-EPLRLhgllsrAERRERVaelLERVGLPPDlADRYPHE-----------LS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 832 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMK 904
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvRYI--ADRVAVMY 479
|
....*....
gi 1490492289 905 DGTIQREGT 913
Cdd:COG1123 480 DGRIVEDGP 488
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
694-911 |
4.90e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.43 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQKV-SGAVFWNslpdseGEDPSSpeqetvADSDVRTR--- 767
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLniLGGL---DRPtSGEVLID------GQDISS------LSERELARlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 768 ---GpvaYASQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 836
Cdd:COG1136 86 rhiG---FVFQFFNLLpELTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 911
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
687-912 |
7.77e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 100.08 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDpsspeqetvadsdvRT 766
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--------------AL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGPVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQ 846
Cdd:cd03247 74 SSLISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 912
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSL-IFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1313-1580 |
7.92e-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: 107.91 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1313 KRIHALLKTEAESYEGLLAPslipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSfsLAf 1392
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLP-------RPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKST--LA- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1393 fRM----------------VDMFEGRIIIDGIDIAKLPlhtlrsrlsiilQDPVLFSGTI-----RF-NLDPEKkcsdst 1450
Cdd:COG4618 376 -RLlvgvwpptagsvrldgADLSQWDREELGRHIGYLP------------QDVELFDGTIaeniaRFgDADPEK------ 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1451 lweALEIAQL----KLVVKaLPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT 1526
Cdd:COG4618 437 ---VVAAAKLagvhEMILR-LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA 512
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1527 AFAD-RTVVTIAHRVHTILSADLVMVLKRGAILEFDKpetllnqKDSIFASFVRA 1580
Cdd:COG4618 513 LKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP-------RDEVLARLARP 560
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
693-916 |
1.47e-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: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPdsegedpsspeqetVADSDVRT-RGPVA 771
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS--------------LKDIDRHTlRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLLNATVEENITFESPFNKQRyKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 848
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 849 NVVFLDDPFSALDVhlsdhLMQAGILE-LLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:TIGR01193 631 KVLILDESTSNLDT-----ITEKKIVNnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
695-908 |
2.42e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 98.44 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsLPDseGEDpsspeqetVADSDVRTRGP-VAYA 773
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV----RLD--GAD--------ISQWDPNELGDhVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVVFL 853
Cdd:cd03246 82 PQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 854 DDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03246 121 DEPNSHLDVEGERALNQA--IAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
691-918 |
2.52e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 100.72 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeQETVADSDVRT-RGP 769
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID------GTD-----INKLKGKALRQlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKPWLLN-ATVEENI---------TFESPFN------KQRykmvieACSLQPDIDILPHGDQtqigeRGINLSGG 833
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVlsgrlgrrsTWRSLFGlfpkeeKQR------ALAALERVGLLDKAYQ-----RADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 834 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 912
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL-LKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDG 227
|
....*.
gi 1490492289 913 TLKDFQ 918
Cdd:cd03256 228 PPAELT 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
697-858 |
2.75e-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: 97.72 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDPSspeqetvadsdvrTRGPVAYASQK 776
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS-------------LRKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLLNA-TVEENITFESPFnKQRYKMVIEAcslQPDIDI----LPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVV 851
Cdd:pfam00005 68 PQLFPRlTVRENLRLGLLL-KGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 1490492289 852 FLDDPFS 858
Cdd:pfam00005 144 LLDEPTA 150
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
691-908 |
4.38e-23 |
|
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: 99.47 E-value: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDgIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQKvsGAVFWNSLPDSEGEDPSSPEQetvadsdvrtrg 768
Cdd:cd03248 25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQG--GQVLLDGKPISQYEHKYLHSK------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 pVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 845
Cdd:cd03248 90 -VSLVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 846 QHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03248 167 RNPQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
695-921 |
1.53e-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: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWNslpdseGEDPSSpeqetvADSDVRTRgPVAY 772
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLsmISRLLPPD--SGEVLVD------GLDVAT------TPSRELAK-RLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWL-LNATVEENITF-ESPFNKQR-----YKMVIEAcslqpdIDILphgDQTQIGERGIN-LSGGQRQRISVARAL 844
Cdd:COG4604 80 LRQENHInSRLTVRELVAFgRFPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDK-RTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
693-907 |
2.23e-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: 96.10 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQETVAdsdvrTRGPVAY 772
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID------GEDLTDLEDELPP-----LRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWLL-NATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVV 851
Cdd:cd03229 81 VFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 852 FLDDPFSALDVhlsdhLMQAGILELLRD----DKRTVVLVTHKLQYLPH-ADWIIAMKDGT 907
Cdd:cd03229 123 LLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
687-924 |
2.98e-22 |
|
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: 102.67 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQKVSGAVFWNslpdseGEDpsspeqetVADSD 763
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLD------GRD--------LLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 764 VRTRGP-VAYASQKPW--LLNATVEENITfESPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 832
Cdd:COG1123 78 EALRGRrIGMVFQDPMtqLNPVTVGDQIA-EALENlglsraeaRARVLELLEAVGLERRLDRYPH-----------QLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQY-LPHADWIIAMKDGT 907
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTT-----QAEILDLLRELQRergtTVLLITHDLGVvAEIADRVVVMDDGR 220
|
250
....*....|....*..
gi 1490492289 908 IQREGTLKDFQRSEYQL 924
Cdd:COG1123 221 IVEDGPPEEILAAPQAL 237
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
692-917 |
5.24e-22 |
|
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: 96.85 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQEtvadsdVRTRgpVA 771
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID------GEDVRKEPRE------ARRQ--IG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWL-LNATVEENITFESPFN-------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARA 843
Cdd:COG4555 78 VLPDERGLyDRLTVRENIRYFAELYglfdeelKKRIEELIELLGLEEFLDRRVGE-----------LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 844 LYQHTNVVFLDDPFSALDVhLSDHLMQaGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 917
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDV-MARRLLR-EILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
692-913 |
2.98e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.07 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWNslpdseGEDpsspeqetVADSDVRTRGp 769
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrmIAGLEDPT--SGEILIG------GRD--------VTDLPPKDRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKPWLL-NATVEENITF------ESPfnKQRYKMVIEAcslqpdIDILphgdqtQIGE----RGINLSGGQRQRI 838
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFplklrkVPK--AEIDRRVREA------AELL------GLEDlldrKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQREG 912
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVE-MRAEIKRLHRRLGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQVG 216
|
.
gi 1490492289 913 T 913
Cdd:COG3839 217 T 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
689-908 |
4.35e-21 |
|
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: 93.25 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 689 WTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpDSEGEDPSspeqeTVADSDVRTRg 768
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI------EIDGIDIS-----TIPLEDLRSS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 pVAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEACSlqpdidilphgdqtqIGERGINLSGGQRQRISVARALYQHT 848
Cdd:cd03369 84 -LTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 849 NVVFLDDPFSALDVHlSDHLMQAGILELLRDDkrTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03369 145 RVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1346-1555 |
7.99e-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: 90.77 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1346 QIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSII 1425
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1426 LQdpvlfsgtirfnldpekkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFIM 1505
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 1506 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTI-LSADLVMVLKRG 1555
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1345-1569 |
1.30e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 97.67 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVD---MFEGRIIIDGIDIAKLPLHTLRSR 1421
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1422 LSIILQDP--VLFSGTIRFNLD--PEKKCSDSTLWEALEIAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFV 1497
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 1498 RKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLNQ 1569
Cdd:COG1123 159 LDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
697-908 |
2.41e-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: 89.76 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPsspeqetvADSDVRTRGPVAYASQK 776
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL------GKDI--------KKEPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLL-NATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLDD 855
Cdd:cd03230 82 PSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 856 PFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:cd03230 122 PTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
697-921 |
3.34e-20 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 91.58 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGED-PSSPEQETVAdsdVRTRgpVAYASQ 775
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD------GQDiTGLSEKELYE---LRRR--IGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 KPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARAL 844
Cdd:COG1127 90 GGALFDSlTVFENVAF--PLRehtdlseaeiRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLS---DHLmqagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSaviDEL----IRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
.
gi 1490492289 921 E 921
Cdd:COG1127 233 D 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
687-926 |
4.61e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.74 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDpsspeqetvadSDVRT 766
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF-----------EKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGPVAYASQKPWLLNATVEENITFESPFNKQRY-KMVIEACSLQPDIDILPHGD-QTQigergiNLSGGQRQRISVARAL 844
Cdd:PRK13648 84 HIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYdEMHRRVSEALKQVDMLERADyEPN------ALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEYQL 924
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
..
gi 1490492289 925 FE 926
Cdd:PRK13648 237 TR 238
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
697-927 |
5.94e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.29 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLgEMQKvSGAVFWNslpdseGEDpsspeqeTVADSDVRTRGpVAYAS 774
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLriIAGL-ETPD-SGRIVLN------GRD-------LFTNLPPRERR-VGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLL-NATVEENITF----ESPFNKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQ 846
Cdd:COG1118 82 QHYALFpHMTVAENIAFglrvRPPSKAEIRARVeelLELVQLEGLADRYPS-----------QLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQaGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDfqrseyqLF 925
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRR-WLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDE-------VY 222
|
..
gi 1490492289 926 EH 927
Cdd:COG1118 223 DR 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
697-889 |
6.34e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 89.85 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeqetVADSDVRTRGPVAYASQK 776
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN------GEP--------IRDAREDYRRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLLNA-TVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHTNV 850
Cdd:COG4133 84 DGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1490492289 851 VFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTH 889
Cdd:COG4133 153 WLLDEPFTALDAAGVALL--AELIAAHLARGGAVLLTTH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1345-1571 |
6.97e-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: 90.47 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAF------------FRMVDMfegriiidgidiAK 1412
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsgevlVDGKDI------------TK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1413 LPLHTLRSRLSIILQDPV--LFSGTIR---------FNLDPEkkcsdstlwEALEIAQ--LKLVvkalpgGLDAIITEGG 1479
Cdd:COG1122 68 KNLRELRRKVGLVFQNPDdqLFAPTVEedvafgpenLGLPRE---------EIRERVEeaLELV------GLEHLADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1480 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAI 1557
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
250
....*....|....
gi 1490492289 1558 LEFDKPETLLNQKD 1571
Cdd:COG1122 213 VADGTPREVFSDYE 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
697-892 |
7.31e-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: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAVFWnslpdsEGEDPSSPEQETVAdsdVRTRgpVA 771
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLL------DGKDIYDLDVDVLE---LRRR--VG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLLNATVEENITF------ESPfNKQRYKMVIEACS---LQPDIDILPHGDQtqigerginLSGGQRQRISVAR 842
Cdd:cd03260 85 MVFQKPNPFPGSIYDNVAYglrlhgIKL-KEELDERVEEALRkaaLWDEVKDRLHALG---------LSGGQQQRLCLAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1490492289 843 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELlrDDKRTVVLVTHKLQ 892
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQ 201
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
691-915 |
7.44e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 96.33 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDgIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDPSSPEQetvadsdvrtrgpV 770
Cdd:TIGR00958 492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-------------V 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNATVEENITFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 849
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMaAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 850 VVFLDDPFSALDVHlSDHLMQagilELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 915
Cdd:TIGR00958 638 VLILDEATSALDAE-CEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
692-891 |
1.14e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdsegedpsspeqetvadsDVRTRGPVA 771
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------------------RRAGGARVA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQK---PWLLNATVEENITF-----ESPFNKQRY--KMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISVA 841
Cdd:NF040873 59 YVPQRsevPDSLPLTVRDLVAMgrwarRGLWRRLTRddRAAVDDALERVGLADLAG---RQLGE----LSGGQRQRALLA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTHKL 891
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDL 179
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1342-1582 |
1.21e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 96.25 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1342 QGKIQIQNLSVRYDSSLK-PVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDM---------------------- 1398
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1399 ---------------FEGRIIIDGIDIAKL-----------------PLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKc 1446
Cdd:PTZ00265 1243 qgdeeqnvgmknvneFSLTKEGGSGEDSTVfknsgkilldgvdicdyNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE- 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1447 sDSTLWE---ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 1523
Cdd:PTZ00265 1322 -DATREDvkrACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 1524 V--MTAFADRTVVTIAHRVHTILSADLVMVL----KRGAILEFDKP-ETLLNQKDSIFASFVRADK 1582
Cdd:PTZ00265 1401 IvdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAHGThEELLSVQDGVYKKYVKLAK 1466
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1345-1566 |
1.64e-19 |
|
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: 89.16 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRII--------IDGIDIAKLPLH 1416
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDegevlldgKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1417 tLRSRLSIILQDPVLFSGTIRFNLD--------PEKKCSDSTLWEALEIAQLKLVVKALPGGLDaiiteggenFSQGQRQ 1488
Cdd:cd03260 79 -LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1489 LFCLARAFVRKTSIFIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETL 1566
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
695-913 |
6.99e-19 |
|
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: 92.58 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQkvSGAVFWNslpdseGEDPSSPEQETVadsdvrtRGPVAY 772
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRILID------GQDIRDVTQASL-------RAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWLLNATVEENItfespfnkqRY----------KMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 842
Cdd:COG5265 437 VPQDTVLFNDTIAYNI---------AYgrpdaseeevEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 843 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSR-TERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
692-913 |
1.07e-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: 89.77 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSS--PEQetvadsdvrtRgP 769
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD------GRDVTGlpPEK----------R-N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRI 838
Cdd:COG3842 79 VGMVFQDyalfPHL---TVAENVAFglrmrgVPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKlQY--LPHADWIIAMKDGTIQREGT 913
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREE-MREELRRLQRELGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
687-913 |
1.10e-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: 92.31 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATLgeMQKVSGAVFWNSLPDSEgedpssPEQETVADSdv 764
Cdd:TIGR03796 485 FGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIakLVAGL--YQPWSGEILFDGIPREE------IPREVLANS-- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 765 rtrgpVAYASQKPWLLNATVEENITFESPFNKQryKMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISVA 841
Cdd:TIGR03796 555 -----VAMVDQDIFLFEGTVRDNLTLWDPTIPD--ADLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:TIGR03796 628 RALVRNPSILILDEATSALDP-----ETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
655-907 |
1.96e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.02 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 655 EEVRDLLGPLQRLTPSMDGD--ADNFCVQiiggfftwTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGemq 732
Cdd:COG4178 343 EAADALPEAASRIETSEDGAlaLEDLTLR--------TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 733 kvsgavFWN------SLPDSEGedpsspeqetvadsdvrtrgpVAYASQKPWLLNATVEENITF---ESPFNKQRYKMVI 803
Cdd:COG4178 412 ------LWPygsgriARPAGAR---------------------VLFLPQRPYLPLGTLREALLYpatAEAFSDAELREAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 804 EACSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRT 883
Cdd:COG4178 465 EAVGLG---HLAERLDEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--TT 536
|
250 260
....*....|....*....|....
gi 1490492289 884 VVLVTHKLQYLPHADWIIAMKDGT 907
Cdd:COG4178 537 VISVGHRSTLAAFHDRVLELTGDG 560
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1345-1580 |
2.09e-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: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPLHtLRS 1420
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMLAGLLKpdsgSILIDGEDVRKEPRE-ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1421 RLSIILQDPVLFSG-TIRFNLD---PEKKCSDSTLWEALEIaqlklVVKALpgGLDAIITEGGENFSQGQRQLFCLARAF 1496
Cdd:COG4555 75 QIGVLPDERGLYDRlTVRENIRyfaELYGLFDEELKKRIEE-----LIELL--GLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1497 VRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLNQ--KDS 1572
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEigEEN 227
|
....*...
gi 1490492289 1573 IFASFVRA 1580
Cdd:COG4555 228 LEDAFVAL 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
692-903 |
2.09e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.92 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWnslpdsEGEDPS--SPEqetvadsdvRTR 767
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLkiVASLISPT--SGTLLF------EGEDIStlKPE---------IYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 768 GPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQ----PDidilphgdqtQIGERGIN-LSGGQRQRISVAR 842
Cdd:PRK10247 81 QQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLErfalPD----------TILTKNIAeLSGGEKQRISLIR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 843 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 903
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
697-913 |
3.14e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.22 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDPSS-------PEQETVADsDVRTRGP 769
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLarrlallPQHHLTPE-GITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYAsQKPWLlnatveeniTFESPFNKQRYKMVIEACslqpdidilphgDQTQIGE----RGINLSGGQRQRISVARALY 845
Cdd:PRK11231 97 VAYG-RSPWL---------SLWGRLSAEDNARVNQAM------------EQTRINHladrRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 846 QHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
692-913 |
4.84e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 85.08 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeqetVADSDVRTRGpVA 771
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG------GED--------ATDVPVQERN-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 839
Cdd:cd03296 78 FVFQHYALFrHMTVFDNVAFglrvkprsERPPEaeiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKEL-RRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
674-908 |
5.00e-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: 89.74 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 674 DADNFCV--QIIGGFFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGeMQKVSGAVFWNslpdseGEDP 751
Cdd:COG4172 277 EARDLKVwfPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFD------GQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 752 SSPEQEtvADSDVRTRGPVA----YASQKPWLlnaTVEENIT------FESPFNKQRYKMVIEACS---LQPD-IDILPH 817
Cdd:COG4172 350 DGLSRR--ALRPLRRRMQVVfqdpFGSLSPRM---TVGQIIAeglrvhGPGLSAAERRARVAEALEevgLDPAaRHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 818 gdqtqigErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHKLQ- 892
Cdd:COG4172 425 -------E----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV-----QAQILDLLRDlqREHglAYLFISHDLAv 488
|
250
....*....|....*...
gi 1490492289 893 --YLphADWIIAMKDGTI 908
Cdd:COG4172 489 vrAL--AHRVMVMKDGKV 504
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
687-913 |
5.36e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.88 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgedpsspeqetVADSDVRT 766
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD-----------YSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RgpVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDIlPHGDQTQIGERGINLSGGQRQRISVARALY 845
Cdd:PRK11160 415 A--ISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 846 QHTNVVFLDDPFSALDVHLSDHlmqagILELLRD---DKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQ-----ILELLAEhaqNK-TVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1346-1555 |
9.08e-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: 83.67 E-value: 9.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1346 QIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSII 1425
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1426 LQDP--VLFSGTIR---------FNLDPEKkcSDSTLWEALEIAQLKLVVKALPggldaiiteggENFSQGQRQLFCLAR 1494
Cdd:cd03225 81 FQNPddQFFGPTVEeevafglenLGLPEEE--IEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1495 AFVRKTSIFIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILS-ADLVMVLKRG 1555
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
699-913 |
1.07e-17 |
|
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: 85.00 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPSSpeqetVADSDVRT--RGPVAYASQK 776
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI------DGQDIAA-----MSRKELRElrRKKISMVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLL-NATVEENITF------ESPFNKQRYKM-VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHT 848
Cdd:cd03294 111 FALLpHRTVLENVAFglevqgVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 849 NVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03294 180 DILLMDEAFSALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
692-912 |
1.47e-17 |
|
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: 83.07 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeqetVADSDVRTRGpVA 771
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG------GRD--------VTDLPPKDRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLL-NATVEENITFESPFNKQRyKMVIE------ACSLQpdIDILPHGDQTQigerginLSGGQRQRISVARAL 844
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVP-KDEIDervrevAELLQ--IEHLLDRKPKQ-------LSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 912
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
687-916 |
1.68e-17 |
|
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: 83.40 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMQKvSGAVFWNslpdseGEDPSspeqeTVADSDVR 765
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrCINGLERPT-SGSVLVD------GTDLT-----LLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 T-RGPVAYASQKPWLLNA-TVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 836
Cdd:cd03258 79 KaRRRIGMIFQHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 911
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
....*
gi 1490492289 912 GTLKD 916
Cdd:cd03258 223 GTVEE 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
699-921 |
1.78e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 83.27 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGED--PSSPEQetvadsdvrtRgPVAYASQK 776
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN------GQDltALPPAE----------R-PVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 ----PWLlnaTVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgDQtqigerginLSGGQRQRISVARALY 845
Cdd:COG3840 80 nnlfPHL---TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 846 QHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQE-MLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
701-912 |
1.86e-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: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 701 SIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeqetVADSDVRTRgPVAYASQKPWLL 780
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN------GVD--------VTAAPPADR-PVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 781 -NATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALYQHTNVVF 852
Cdd:cd03298 83 aHLTVEQNVGLGlspglklTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 853 LDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 912
Cdd:cd03298 152 LDEPFAALDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
693-908 |
2.63e-17 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 80.94 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQKVSGAVFWNslpdseGEDpsspeqetvadsdvrtrgpv 770
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMkiLS--GLYKPDSGEILVD------GKE-------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 ayasqkpwllnatveenITFESPFNKQRykmvieacslqpdidilphgdqtqigeRGIN----LSGGQRQRISVARALYQ 846
Cdd:cd03216 64 -----------------VSFASPRDARR---------------------------AGIAmvyqLSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
691-916 |
4.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.36 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPdsegEDPSspeqetvADSDVRTRGPV 770
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP----IDYS-------RKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISV 840
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSF-GAVNlklpedevRKRVDNALKRTGIEHLKDKPTHC-----------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 841 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL-LVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
692-916 |
5.06e-17 |
|
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: 81.90 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDpsspeqetVADSDVRTRgPVA 771
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL------DGKD--------ITNLPPHKR-PVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLL-NATVEENITF-----ESPFNKQRYKmVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRISVARAL 844
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFglrlkKLPKAEIKER-VAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHlMQagiLELLRDDKR---TVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKD-MQ---LELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1362-1510 |
5.28e-17 |
|
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: 79.61 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1362 LKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL 1440
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 1441 -------DPEKKCSDSTLWEALEiaqlKLvvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1510
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALE----KL---GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
699-920 |
6.16e-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: 86.48 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQKVSGAVFWNSLPDseGEDPSSPEQETVadsdvrtRGPVAYASQKPW 778
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLI----NLLQRVYDPTVGQILID--GIDINTVTRESL-------RKSIATVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 779 LLNATVEENITF--ESPFNKQRYKMViEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDP 856
Cdd:TIGR01192 420 LFNRSIRENIRLgrEGATDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 857 FSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:TIGR01192 499 TSALDVETEARVKNA--IDALRKN-RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
695-889 |
7.35e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.22 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQEtvadsdvrtRGPVAyas 774
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD------GVPVTGPGAD---------RGVVF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QK----PWLlnaTVEENITFESPFNK----QRYKMVIEACSLqpdIDiLPHGDQTQIGErginLSGGQRQRISVARALYQ 846
Cdd:COG4525 83 QKdallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VG-LADFARRRIWQ----LSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490492289 847 HTNVVFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTH 889
Cdd:COG4525 152 DPRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
697-892 |
8.58e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAVFWNslpdseGEDPSSPEQETVAdsdVRTRgpVA 771
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFH------GKNLYAPDVDPVE---VRRR--IG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLLNATVEENITFESPFNKQRYKM--VIEACSLQPdidILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 849
Cdd:PRK14243 95 MVFQKPNPFPKSIYDNIAYGARINGYKGDMdeLVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490492289 850 VVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHKLQ 892
Cdd:PRK14243 172 VILMDEPCSAL-----DPISTLRIEELMHELKEqyTIIIVTHNMQ 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
687-903 |
8.72e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.60 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---KVSGAVFWNslpdseGEDpsspeqetVADSD 763
Cdd:COG4136 7 LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLN------GRR--------LTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 764 VRTRGpVAYASQKPWLL-NATVEENITF---ESPFNKQRYKMVIEAcsLQpDIDiLPHgdqtqIGERGIN-LSGGQRQRI 838
Cdd:COG4136 73 AEQRR-IGILFQDDLLFpHLSVGENLAFalpPTIGRAQRRARVEQA--LE-EAG-LAG-----FADRDPAtLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 903
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQ-FREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1337-1552 |
9.51e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.62 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1337 KNWPDQGKIQIQNLSVRYDSSLK-PVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAK-LP 1414
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1415 LHTLRSRLSIILQDPVLFSGTIRFN----------------------------LDPEKKC--------------SDSTLW 1452
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdlealsnyynedgndsqenKNKRNSCrakcagdlndmsntTDSNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1453 -------------EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1516
Cdd:PTZ00265 535 iemrknyqtikdsEVVDVSKKVLIhdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270
....*....|....*....|....*....|....*...
gi 1490492289 1517 ENILQKVV--MTAFADRTVVTIAHRVHTILSADLVMVL 1552
Cdd:PTZ00265 615 EYLVQKTInnLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
691-889 |
9.99e-17 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 80.53 E-value: 9.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDPSSPEqetvadsdVRTRGPV 770
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPY--------LRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKpWLLNATVEENITF------ESPFN-KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARA 843
Cdd:cd03292 83 VFQDFR-LLPDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490492289 844 LYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD-DKR--TVVLVTH 889
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTT-----WEIMNLLKKiNKAgtTVVVATH 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
699-912 |
1.29e-16 |
|
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: 80.42 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPrGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLP--DSEGEDPSSPEQetvadsdvrtRGpVAYASQK 776
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfDSRKKINLPPQQ----------RK-IGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLL-NATVEENITFESPFNKQRYKMVIEAcslqpdiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTNVVFLD 854
Cdd:cd03297 84 YALFpHLNVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 855 DPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL---QYLphADWIIAMKDGTIQREG 912
Cdd:cd03297 157 EPFSALDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
693-917 |
1.41e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 80.56 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDpsspeqETVADSDVRTRGPVAY 772
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF------DGRD------ITGLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWLL-NATVEENITF-ESPFNKQRYKMVIE-ACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVARALYQHTN 849
Cdd:cd03224 80 VPEGRRIFpELTVEENLLLgAYARRRAKRKARLErVYELFPRL-------KERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 850 VVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 917
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEA--IRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
699-921 |
1.42e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPSSPEQETVAdsdvRTRGPVAYasqkpw 778
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL------DGEHIQHYASKEVA----RRIGLLAQ------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 779 llNATVEENITFESPFNKQRYKMvieacslQP--------DIDILPHGDQ----TQIGERGIN-LSGGQRQRISVARALY 845
Cdd:PRK10253 89 --NATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 846 QHTNVVFLDDPFSALDVhlsDHlmQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:PRK10253 160 QETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
.
gi 1490492289 921 E 921
Cdd:PRK10253 235 E 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
690-889 |
1.52e-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: 78.73 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdsegedpSSPEQETVAdsdvrtrgp 769
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------GMPEGEDLL--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 vaYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidILPHGDqtqigergiNLSGGQRQRISVARALYQHTN 849
Cdd:cd03223 68 --FLPQRPYLPLGTLREQL-------------------------IYPWDD---------VLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1490492289 850 VVFLDDPFSALDVHLSDHLMQagileLLRDDKRTVVLVTH 889
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGH 146
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
695-913 |
2.26e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.63 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQKVSgavfwnslpdsegeDPSSpEQETVADSDVRT------RG 768
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQRVF--------------DPQS-GRILIDGTDIRTvtraslRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 PVAYASQKPWLLNATVEENITFESPfNKQRYKMVIEACSLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 846
Cdd:PRK13657 410 NIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAA--LDELMKG-RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
695-913 |
3.14e-16 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 79.47 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnslpdsegedpsspeqetVADSDVRT-----RGP 769
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY-------------------INGYSIRTdrkaaRQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQK---PWLLnaTVEENITFESPF---NKQRYKMVIEA----CSLQPDIDilphgdqTQIGergiNLSGGQRQRIS 839
Cdd:cd03263 77 LGYCPQFdalFDEL--TVREHLRFYARLkglPKSEIKEEVELllrvLGLTDKAN-------KRAR----TLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRddKRTVVLVTHKLQ---YLphADWIIAMKDGTIQREGT 913
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDL-ILEVRK--GRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
697-921 |
3.61e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.83 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdSEGEDPSSPEQEtvaDSDVRT-RGPVAYASQ 775
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-------TIGERVITAGKK---NKKLKPlRKKVGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 KP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALY 845
Cdd:PRK13634 93 FPehQLFEETVEKDICF-GPMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 846 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLKD-FQRS 920
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEM-FYKLHKEKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREiFADP 237
|
.
gi 1490492289 921 E 921
Cdd:PRK13634 238 D 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
697-908 |
3.84e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDpsspeqetvadsdvRTRGPVAYASQK 776
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE--------------DTRLMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWllnATVEENITFESPFN-KQRYKMVIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQHTNVVFLDD 855
Cdd:PRK11247 94 PW---KKVIDNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 856 PFSALDVhLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 908
Cdd:PRK11247 160 PLGALDA-LTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
694-913 |
4.17e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 84.70 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQKVSGAVFWNSLPD------------------------SE 747
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVmsLLMRFYDLKNDHHIVFKNEHTNdmtneqdyqgdeeqnvgmknvnefSL 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 748 GEDPSSPEQETV--------------ADSDVRT-RGPVAYASQKPWLLNATVEENITF-ESPFNKQRYKMVIEACSLQPD 811
Cdd:PTZ00265 1261 TKEGGSGEDSTVfknsgkilldgvdiCDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFgKEDATREDVKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 812 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKL 891
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
250 260
....*....|....*....|....*..
gi 1490492289 892 QYLPHADWIIAM----KDGT-IQREGT 913
Cdd:PTZ00265 1420 ASIKRSDKIVVFnnpdRTGSfVQAHGT 1446
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
697-910 |
4.35e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQKVSGAVFwnslpdsegedpsspeqeTVADSDVRTRGPVAYAS-- 774
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDKPTSGTY------------------RVAGQDVATLDADALAQlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 --------QKPWLL-NATVEENITFESPF-------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 838
Cdd:PRK10535 85 rehfgfifQRYHLLsHLTAAQNVEVPAVYaglerkqRLLRAQELLQRLGLEDRVEYQPS-----------QLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQR 910
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
691-916 |
4.95e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.12 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnslpdSEGEdpsspEQETVADSDVRTRGPV 770
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL------IKGE-----PIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 840
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAF-GPLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 841 ARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKE 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1345-1560 |
5.12e-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: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRY--DSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVD------MFEGRIIIDGIDIAKLPLh 1416
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiIFDGKDLLKLSRRLRKIR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1417 tlRSRLSIILQDPvlFSgtirfNLDPEKKCSDStLWEALEI--------AQLKLVVKALPG-GLDAII-----TEggenF 1482
Cdd:cd03257 81 --RKEIQMVFQDP--MS-----SLNPRMTIGEQ-IAEPLRIhgklskkeARKEAVLLLLVGvGLPEEVlnrypHE----L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1483 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVMVLKRGAI 1557
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
...
gi 1490492289 1558 LEF 1560
Cdd:cd03257 225 VEE 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
697-890 |
7.05e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.47 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQK---VSGAVFWNslpdsegEDPSSPEQetvadsdvrTRGPVAYA 773
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFN-------GQPRKPDQ---------FQKCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQKPWLL-NATVEENITFESPF-------NKQRYKMVieacslqpDIDILPHGDQTQIGERGI-NLSGGQRQRISVARAL 844
Cdd:cd03234 87 RQDDILLpGLTVRETLTYTAILrlprkssDAIRKKRV--------EDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHK 890
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1341-1573 |
7.29e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.65 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1341 DQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRS 1420
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1421 RLSIILQDP-VLFSGT-----IRFNLdpEKKCSDSTLWEALeIAQLKLVVkalpgGLDAIITEGGENFSQGQRQLFCLAR 1494
Cdd:PRK13632 84 KIGIIFQNPdNQFIGAtveddIAFGL--ENKKVPPKKMKDI-IDDLAKKV-----GMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1495 AFVRKTSIFIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQKDS 1572
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
.
gi 1490492289 1573 I 1573
Cdd:PRK13632 236 L 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
697-889 |
7.65e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnSLPDSEGEDPSSPEQetvadsdvrtrgpVAYASQ- 775
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI---KLDGGDIDDPDVAEA-------------CHYLGHr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 ---KPWLlnaTVEENITFESPFNKQRYKMV---IEACSLQPDIDiLPHGdqtqigergiNLSGGQRQRISVARALYQHTN 849
Cdd:PRK13539 82 namKPAL---TVAENLEFWAAFLGGEELDIaaaLEAVGLAPLAH-LPFG----------YLSAGQKRRVALARLLVSNRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490492289 850 VVFLDDPFSALDVH--------LSDHLMQAGIlellrddkrtVVLVTH 889
Cdd:PRK13539 148 IWILDEPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1345-1556 |
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 1490492289 1345 IQIQNLSVRYDSSLkPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRI--IIDGIDIAKLPLHTLRSRL 1422
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIIL--QDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1500
Cdd:cd03290 80 SVAYaaQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 1501 SIFIMDEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVMVLKRGA 1556
Cdd:cd03290 160 NIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
684-911 |
1.24e-15 |
|
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: 78.69 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 684 GGFFtWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPS--SPEQETVAD 761
Cdd:TIGR02769 15 GGLF-GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF------RGQDLYqlDRKQRRAFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 762 SDVRTRGPVAYASQKP-----WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQR 835
Cdd:TIGR02769 88 RDVQLVFQDSPSAVNPrmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 836 QRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQR 910
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
.
gi 1490492289 911 E 911
Cdd:TIGR02769 232 E 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
687-913 |
1.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.69 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMqkvsgavfwnsLPDSEGE-----DPSSPEQETVAD 761
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL-----------LPDDNPNskitvDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 762 sdVRTRGPVAYASQKPWLLNATVEENITFESPfNKQ--RYKMVIEACSLQPDIDILPHGDQTQIgergiNLSGGQRQRIS 839
Cdd:PRK13640 82 --IREKVGIVFQNPDNQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKL-IRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
697-916 |
2.26e-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: 77.38 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGED--PSSPEQETVAdsdvrtrgpvaYAS 774
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN------GKDitNLPPEKRDIS-----------YVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLL-NATVEENITF----ESPFNKQRYKMVIE-ACSLqpDIDILPHGDQTqigergiNLSGGQRQRISVARALYQHT 848
Cdd:cd03299 78 QNYALFpHMTVYKNIAYglkkRKVDKKEIERKVLEiAEML--GIDHLLNRKPE-------TLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 849 NVVFLDDPFSALDVHLSDHLMqagilELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLR-----EELKKIRKefgvTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
701-912 |
2.94e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.44 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 701 SIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLpDSEGEDPSspeqetvadsdvrtRGPVAYASQKPWLL 780
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ-SHTGLAPY--------------QRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 781 -NATVEENITFE-SPFNK----QRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRISVARALYQHTNVVF 852
Cdd:TIGR01277 83 aHLTVRQNIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRVALARCLVRPNPILL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 853 LDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 912
Cdd:TIGR01277 152 LDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
712-913 |
3.29e-15 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 78.69 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 712 IVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQEtvadsdvrtRGPVAYASQKPWLL-NATVEENITF 790
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLD------GEDVTNVPPH---------LRHINMVFQSYALFpHMTVEENVAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 791 ESPFNK----QRYKMVIEACSLqpdidilphgdqTQIGERG----INLSGGQRQRISVARALYQHTNVVFLDDPFSALDV 862
Cdd:TIGR01187 66 GLKMRKvpraEIKPRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 863 HLSDhLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 913
Cdd:TIGR01187 134 KLRD-QMQLELKTIQEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
697-912 |
4.57e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.93 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQKVS-GAVFWNS-----LPDSEGedpsspeQETVADSD----VRT 766
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFL-RCINFLEKPSeGSIVVNGqtinlVRDKDG-------QLKVADKNqlrlLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGPVAYASQKPWLlNATVEENItFESP-----FNKQRYKMviEACSLQPDIDIlphgDQTQIGERGINLSGGQRQRISVA 841
Cdd:PRK10619 93 RLTMVFQHFNLWS-HMTVLENV-MEAPiqvlgLSKQEARE--RAVKYLAKVGI----DERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 912
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
692-889 |
4.88e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.72 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPSS--PEQEtvadsdvrtrgP 769
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML------DGVDLSHvpPYQR-----------P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKPWLL-NATVEENITFESPFNK-------QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVA 841
Cdd:PRK11607 93 INMMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH 889
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDR-MQLEVVDILERVGVTCVMVTH 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
690-889 |
6.75e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 77.40 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDG-IPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQKVSGAVFWnslpdsEGEDPSS-PEQETvadSDV 764
Cdd:COG0444 13 TRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILF------DGEDLLKlSEKEL---RKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 765 RTRGpVAYASQKPwlLNA-----TVEENITfESPFN------KQRYKMVIEA---CSLQPDIDIL---PHgdqtqigerg 827
Cdd:COG0444 84 RGRE-IQMIFQDP--MTSlnpvmTVGDQIA-EPLRIhgglskAEARERAIELlerVGLPDPERRLdryPH---------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 828 iNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTH 889
Cdd:COG0444 150 -ELSGGMRQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITH 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
697-892 |
6.76e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLlATLGEM------QKVSGAVFWNslpdseGEDPSSPEQETVAdsdVRTRgpV 770
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLL-RCLNRMndlipgARVEGEILLD------GEDIYDPDVDVVE---LRRR--V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNATVEENITFESPFNKQRYKMVIEA--------CSLQPDI-DILphgdqtqiGERGINLSGGQRQRISVA 841
Cdd:COG1117 95 GMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVkDRL--------KKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD--DKRTVVLVTHKLQ 892
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPIST-----AKIEELILElkKDYTIVIVTHNMQ 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
692-889 |
7.53e-15 |
|
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: 74.70 E-value: 7.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDpsSPEQEtvadsdvrtrgpVA 771
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD--EPHEN------------IL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLLNA-TVEENITFESPFNKQRYKMVIEACslqpdidilphgdqTQIGERGIN------LSGGQRQRISVARAL 844
Cdd:TIGR01189 77 YLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARLW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 845 YQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 889
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
697-937 |
9.74e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLlatlgemQKVSGAVFWNSLPDSEGED-PSSPEQETVADSDVR-TRGPVAYAS 774
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKSAGSHIELlGRTVQREGRLARDIRkSRANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLLNA-TVEENITF----ESPFNKQRYKMVIEAcSLQPDIDILphgdqTQIG------ERGINLSGGQRQRISVARA 843
Cdd:PRK09984 93 QQFNLVNRlSVLENVLIgalgSTPFWRTCFSWFTRE-QKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 844 LYQHTNVVFLDDPFSALDVHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDFQ 918
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVM-----DTLRDinqnDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFD 241
|
250
....*....|....*....
gi 1490492289 919 RSEyqlFEHWKTLMNRQDQ 937
Cdd:PRK09984 242 NER---FDHLYRSINRVEE 257
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
692-913 |
1.04e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.38 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSegedpsspeqeTVADSDVRtRGpVA 771
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-----------SLSHSVLR-QG-VA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVV 851
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 852 FLDDPFSALDVHLSDHLMQAgiLELLRdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQA--LAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
691-912 |
1.53e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 74.70 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSspeqeTVADSDV----RT 766
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN------GQDLS-----RLKRREIpylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 RGPVAyasQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 838
Cdd:COG2884 81 IGVVF---QDFRLLpDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPHADW-IIAMKDGTIQREG 912
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSW-----EIMELLEEINRrgtTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
692-916 |
1.66e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPS--SPEQE---TVADSdvrt 766
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD------GQDIThvPAENRhvnTVFQS---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 rgpvaYAsqkpwLL-NATVEENITF-----ESPfNKQRYKMVIEA---CSLQPDIDILPHgdqtqigergiNLSGGQRQR 837
Cdd:PRK09452 95 -----YA-----LFpHMTVFENVAFglrmqKTP-AAEITPRVMEAlrmVQLEEFAQRKPH-----------QLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 838 ISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQ-MQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
687-917 |
1.70e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---KVSGAV-FWNslpdsegedpsspeqETVA 760
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELEsevRVEGRVeFFN---------------QNIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 761 DSDV---RTRGPVAYASQKPWLLNATVEENITFESPFNKQRYKM----VIEACSLQPDI-DILPHgdqtQIGERGINLSG 832
Cdd:PRK14258 78 ERRVnlnRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLwDEIKH----KIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLS---DHLMQAGILEllrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQ 909
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVSRLSDFTAFFKGNEN 229
|
....*...
gi 1490492289 910 REGTLKDF 917
Cdd:PRK14258 230 RIGQLVEF 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
692-892 |
3.41e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.35 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnSLPDSEGEDPSSpEQETVADSDvrtrgpva 771
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI---TLDGKPVEGPGA-ERGVVFQNE-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 yaSQKPWLlnaTVEENITFespfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTNV 850
Cdd:PRK11248 80 --GLLPWR---NVQDNVAF-----GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490492289 851 VFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 892
Cdd:PRK11248 150 LLLDEPFGALDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
696-892 |
4.07e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 696 TLSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---KVSGAVFWNslpdseGEDPSSPEQETVadsdvRTRGPV 770
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsINRMNDLNpevTITGSIVYN------GHNIYSPRTDTV-----DLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNATVEENITFESPFN----KQRYKMVIEACSLQPDI-----DILpHgdqtqigERGINLSGGQRQRISVA 841
Cdd:PRK14239 89 GMVFQQPNPFPMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdevkDRL-H-------DSALGLSGGQQQRVCIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 842 RALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELlrDDKRTVVLVTHKLQ 892
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQ 208
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
691-913 |
4.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.25 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLpdsEGEDPSSPEqetvadsDVRTRGPV 770
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGI---DTGDFSKLQ-------GIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNATVEENITFeSPFNkqrykmvieACslQPDIDILPHGDQTqIGERGI---------NLSGGQRQRISVA 841
Cdd:PRK13644 82 VFQNPETQFVGRTVEEDLAF-GPEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
685-903 |
4.75e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.00 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 685 GFFTwTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQKVSGAVFWNslpdseGEDPSSPEQETVADsd 763
Cdd:PRK11308 20 GLFK-PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIE-TPTGGELYYQ------GQDLLKADPEAQKL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 764 VRTR------GPvaYASQKP-WLLNATVEE----NITFESPFNKQRYKMVIEACSLQPD-IDILPHgdqtqigergiNLS 831
Cdd:PRK11308 90 LRQKiqivfqNP--YGSLNPrKKVGQILEEplliNTSLSAAERREKALAMMAKVGLRPEhYDRYPH-----------MFS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 832 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 903
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQelglSYVFISHDLSVVEHiADEVMVM 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
693-912 |
8.43e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdsegedpsspeqeTVADSDVRTRGPVAY 772
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-------------------LVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKpwllnATV--EENITFE-----------SPfNKQRYKMVIEACSLQPDiDILPHGDQTQIGERGI-NLSGGQRQRI 838
Cdd:PRK09536 76 SRRV-----ASVpqDTSLSFEfdvrqvvemgrTP-HRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHlsdHLMQAgiLELLR---DDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 912
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDIN---HQVRT--LELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAG 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1345-1569 |
8.72e-14 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 76.10 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLK---PVLKHVNALISPGQKIGICGRTGSGKSSFSLA------------FFRMVDMfegriiidgID 1409
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLllgllrptsgsiLFDGKDL---------TK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1410 IAKLPLHTLRSRLSIILQDPvlFSGtirfnLDPEKKCSDStLWEALEIAQL-------KLVVKAL------PGGLDAIIT 1476
Cdd:COG1123 332 LSRRSLRELRRRVQMVFQDP--YSS-----LNPRMTVGDI-IAEPLRLHGLlsraerrERVAELLervglpPDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1477 EggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLV 1549
Cdd:COG1123 404 E----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRV 475
|
250 260
....*....|....*....|
gi 1490492289 1550 MVLKRGAILEFDKPETLLNQ 1569
Cdd:COG1123 476 AVMYDGRIVEDGPTEEVFAN 495
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
693-921 |
1.18e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQKVSGAVFWNslpdseGE--DPSSPeqetvadSDVRTRG 768
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMkiLS--GVYQPDSGEILLD------GEpvRFRSP-------RDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 pVAYASQKPWLL-NATVEENITFESPFNK----QRYKMVIEACSL--QPDIDILPHgdqTQIGErginLSGGQRQRISVA 841
Cdd:COG1129 81 -IAIIHQELNLVpNLSVAENIFLGREPRRggliDWRAMRRRARELlaRLGLDIDPD---TPVGD----LSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAELTED 230
|
.
gi 1490492289 921 E 921
Cdd:COG1129 231 E 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
697-893 |
1.23e-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: 71.04 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQKVSGAVFWNSLPdsegEDPSSPeqetvadsdvrtRGPVAYAS 774
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLnaLAGRRTGLGVSGEVLINGRP----LDKRSF------------RKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLL-NATVEENITFespfnkqrykmvieACSLQpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFL 853
Cdd:cd03213 89 QDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1490492289 854 DDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY 893
Cdd:cd03213 136 DEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSS 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
695-927 |
1.27e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.13 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgedpsspeqETVADsdVRTRgpVAYAS 774
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE---------ETVWD--VRRQ--VGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKP--WLLNATVEENITF--EspfNKQ--RYKMV------IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 842
Cdd:PRK13635 88 QNPdnQFVGATVQDDVAFglE---NIGvpREEMVervdqaLRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 843 ALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKR-TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKdfqrse 921
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVL--ETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPE------ 225
|
....*.
gi 1490492289 922 yQLFEH 927
Cdd:PRK13635 226 -EIFKS 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
690-916 |
2.22e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.81 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSS-------LLLATLGEMQkvsgAVFWNSLPDSEGEDPSSPEQETVAD- 761
Cdd:PRK13651 16 LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIE----WIFKDEKNKKKTKEKEKVLEKLVIQk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 762 ---------SDVRTRGPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLqpDIDILPHGDqtqig 824
Cdd:PRK13651 92 trfkkikkiKEIRRRVGVVFQFAEYQLFEQTIEKDIIF-GPVSmgvskeeaKKRAAKYIELVGL--DESYLQRSP----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 825 ergINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAM 903
Cdd:PRK13651 164 ---FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTIFF 238
|
250
....*....|....*..
gi 1490492289 904 KDGTIQREG----TLKD 916
Cdd:PRK13651 239 KDGKIIKDGdtydILSD 255
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
697-908 |
2.43e-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: 70.64 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWNslpdseGEDPSSPEQETvadSDVRTRgpVAYAS 774
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTIIID------GLKLTDDKKNI---NELRQK--VGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLL-NATVEENITfESP---FNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNV 850
Cdd:cd03262 83 QQFNLFpHLTVLENIT-LAPikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 851 VFLDDPFSALDVHlsdhlMQAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:cd03262 157 MLFDEPTSALDPE-----LVGEVLDVMKDlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
688-891 |
2.63e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 688 TWTpDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAV--------------FWNSLPDSEGEDPSS 753
Cdd:PRK15056 15 TWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrqalqknLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 754 PeqetVADSDVRTRGPVAYASqkpWLLNAtveenitfespfnKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGG 833
Cdd:PRK15056 94 P----VLVEDVVMMGRYGHMG---WLRRA-------------KKRDRQIVTAALARVDMVEFRH---RQIGE----LSGG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 834 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL 891
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNL 202
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
695-908 |
3.05e-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: 71.48 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnslpdSEGEDPSSPEQETVadsdvrtRGPVAYAS 774
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV------IDGIDISKLPLHTL-------RSRLSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLD 854
Cdd:cd03288 102 QDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 855 DPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03288 182 EATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
692-889 |
3.18e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.21 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDPSSPEqetvadsdvrtrgpVA 771
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG--------------LL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLLNA-TVEENITFESPFNKQrykmviEACslqpdIDILPHGDQTQIGERGIN-LSGGQRQRISVARALYQHTN 849
Cdd:cd03231 77 YLGHAPGIKTTlSVLENLRFWHADHSD------EQV-----EEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490492289 850 VVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 889
Cdd:cd03231 146 LWILDEPTTALDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1342-1570 |
3.30e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.48 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1342 QGKIQIQNLSVRYDSSlkPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMF-----EGRIIIDGIDIAKLPLH 1416
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1417 TLRSRLSIILQDP------VLFSGT---IRFN-LDPEKKCSDSTLWEALEIAQLKLVVKalpGGLDAiiteGGENFSQGQ 1486
Cdd:PRK14247 79 ELRRRVQMVFQIPnpipnlSIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVK---DRLDA----PAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1487 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtilsADLVMVLKRGAILE- 1559
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEw 226
|
250
....*....|....*..
gi 1490492289 1560 ------FDKPETLLNQK 1570
Cdd:PRK14247 227 gptrevFTNPRHELTEK 243
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
684-903 |
3.32e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 72.46 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 684 GGFFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPSSPEQETVADsd 763
Cdd:COG4608 21 GGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF------DGQDITGLSGRELRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 764 VRTR------GPvaYASqkpwlLNA--TVEENItfESPF-------NKQRYKMV---IEACSLQPD-IDILPHgdqtqig 824
Cdd:COG4608 93 LRRRmqmvfqDP--YAS-----LNPrmTVGDII--AEPLrihglasKAERRERVaelLELVGLRPEhADRYPH------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 825 ErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADW 899
Cdd:COG4608 157 E----FSGGQRQRIGIARALALNPKLIVCDEPVSALDV--S---IQAQVLNLLEDLQDelglTYLFISHDLSVVRHiSDR 227
|
....
gi 1490492289 900 IIAM 903
Cdd:COG4608 228 VAVM 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
697-919 |
5.76e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.04 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeqetVADSDVRTRgPVAYASQK 776
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH------GTD--------VSRLHARDR-KVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPhgdqTQigerginLSGGQRQRISVARAL 844
Cdd:PRK10851 83 YALFrHMTVFDNIAFgltvlprrERPNAaaiKAKVTQLLEMVQLAHLADRYP----AQ-------LSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQR 919
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKEL-RRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
677-912 |
7.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 677 NFCVQIIGGFFTWtPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLG--EMQKVSGAVFwnslpdsegedpssp 754
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiyLPQRGRVKVM--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 755 EQETVADSDVRTRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqig 824
Cdd:PRK13647 66 GREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAF-GPVNmgldkdevERRVEEALKAVRMWDFRDKPPY------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 825 ergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAM 903
Cdd:PRK13647 138 ----HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVL 211
|
....*....
gi 1490492289 904 KDGTIQREG 912
Cdd:PRK13647 212 KEGRVLAEG 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
697-930 |
7.70e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAVfwnslpDSEGEDPSSPEQETVadsDVRTRGPVA 771
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEV------RLFGRNIYSPDVDPI---EVRREVGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLlNATVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVAR 842
Cdd:PRK14267 91 FQYPNPFP-HLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 843 ALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHK-LQYLPHADWIIAMKDGTIQREG-TLKDFQ 918
Cdd:PRK14267 163 ALAMKPKILLMDEPTANI-----DPVGTAKIEELLFELKKeyTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpTRKVFE 237
|
250
....*....|..
gi 1490492289 919 RSEYQLFEHWKT 930
Cdd:PRK14267 238 NPEHELTEKYVT 249
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
700-920 |
9.19e-13 |
|
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: 71.68 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 700 ISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWN--SLPDSEGEDPSSPEQETVAdsdvrtrgpvaYASQKP 777
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrTLFDSRKGIFLPPEKRRIG-----------YVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 778 WLL-NATVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHTNVV 851
Cdd:TIGR02142 85 RLFpHLSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 852 FLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1345-1569 |
1.00e-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: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrLSI 1424
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKS------------------------------TL---LKA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 IL--QDPVlfSGTIRFNLDPEKKcsdstlwEALEIA---QLKLVVKALP--------GGLD--------------AIITE 1477
Cdd:COG1121 52 ILglLPPT--SGTVRLFGKPPRR-------ARRRIGyvpQRAEVDWDFPitvrdvvlMGRYgrrglfrrpsradrEAVDE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1478 -----GGENF--------SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI 1543
Cdd:COG1121 123 alervGLEDLadrpigelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAV 202
|
250 260
....*....|....*....|....*..
gi 1490492289 1544 LS-ADLVMVLKRGaILEFDKPETLLNQ 1569
Cdd:COG1121 203 REyFDRVLLLNRG-LVAHGPPEEVLTP 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1345-1568 |
1.03e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.40 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSL---AFFRMVDMFEGRIIIDGIDIAKLPlhTLRSR 1421
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALhlnGLLRPQKGKVLVSGIDTGDFSKLQ--GIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1422 LSIILQDP-VLFSG-TIRFNL--DPEKKCSDSTlwealEIAqlKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAF 1496
Cdd:PRK13644 79 VGIVFQNPeTQFVGrTVEEDLafGPENLCLPPI-----EIR--KRVDRALAEiGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 1497 VRKTSIFIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLN 1568
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
699-925 |
1.06e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.29 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnslpdSEGEDpsspeqetVADSDVRTRGpVAYASQKPW 778
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF------IDGED--------VTHRSIQQRD-ICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 779 LL-NATVEENITF-------ESPFNKQRYKmviEACSLqpdIDILPHGDQ--TQIgerginlSGGQRQRISVARALYQHT 848
Cdd:PRK11432 89 LFpHMSLGENVGYglkmlgvPKEERKQRVK---EALEL---VDLAGFEDRyvDQI-------SGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 849 NVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRSEYQLF 925
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
697-930 |
1.34e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.56 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAVFWnslpdsEGEDPSSPEQetvadSDVRTRGPVA 771
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVYL------DGQDIFKMDV-----IELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPwLLNATVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVAR 842
Cdd:PRK14247 88 FQIPNP-IPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 843 ALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDdkRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKD-F 917
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD--MTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREvF 233
|
250
....*....|...
gi 1490492289 918 QRSEYQLFEHWKT 930
Cdd:PRK14247 234 TNPRHELTEKYVT 246
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
674-913 |
1.35e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 674 DADNFCVQIiggfftwtpDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSS 753
Cdd:PRK13548 4 EARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN------GRPLAD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 754 PEQETVAdsdvRTRgpvAYASQK-----PWllnaTVEENITF-ESPF--NKQRYKMVIEACSLQPDIDILPHGDQTQige 825
Cdd:PRK13548 69 WSPAELA----RRR---AVLPQHsslsfPF----TVEEVVAMgRAPHglSRAEDDALVAAALAQVDLAHLAGRDYPQ--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 826 rginLSGGQRQRISVARALYQHTN------VVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL---- 891
Cdd:PRK13548 135 ----LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLA---H--QHHVLRLARQlaheRGLAVIVVLHDLnlaa 205
|
250 260
....*....|....*....|..
gi 1490492289 892 QYlphADWIIAMKDGTIQREGT 913
Cdd:PRK13548 206 RY---ADRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
687-916 |
1.47e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 69.63 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 687 FTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLA--------------------TLGEMQKVSGAVFWNslP 744
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIskILTgllkpqsgeikidgitiskeNLKEIRKKIGIIFQN--P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 745 DSEgedpsspeqetvadsdvrtrgpvayasqkpwLLNATVEENITFeSPFNKQ--RYKM--VIEACSLQPDI-DILPHGD 819
Cdd:PRK13632 93 DNQ-------------------------------FIGATVEDDIAF-GLENKKvpPKKMkdIIDDLAKKVGMeDYLDKEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 820 QtqigergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADW 899
Cdd:PRK13632 141 Q--------NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI-MVDLRKTRKKTLISITHDMDEAILADK 211
|
250
....*....|....*..
gi 1490492289 900 IIAMKDGTIQREGTLKD 916
Cdd:PRK13632 212 VIVFSEGKLIAQGKPKE 228
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1065-1315 |
1.65e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 69.90 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1065 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1144
Cdd:cd18557 39 ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1145 RSTLLCVSA---LTVISY-VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQlddttQLPLLSHFA-ETVEGLTTIRAF-- 1217
Cdd:cd18557 119 RNILQVIGGliiLFILSWkLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQD-----ALAKAGQVAeESLSNIRTVRSFsa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1218 -RYE-ARFQQKLLEYTDSnNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSlhrELSAGLVGLGLTYALMVSNYL 1295
Cdd:cd18557 194 eEKEiRRYSEALDRSYRL-ARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSG---QLTVGELTSFILYTIMVASSV 269
|
250 260
....*....|....*....|
gi 1490492289 1296 NWMVRNLADMEIQLGAVKRI 1315
Cdd:cd18557 270 GGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1064-1315 |
1.74e-12 |
|
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: 69.89 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1064 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1143
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1144 SRSTLLCVSALTVISYVTPV-FLVALLPLAVVCYFIQKYF---RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1219
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWKlTLVALLLLPLYVLILRYFRrriRKASREVRESLAE----LSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1220 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELSAGlvglGLTYALMVSNYLNWMV 1299
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG----ELVAFLAYLGMLFGPI 272
|
250 260
....*....|....*....|
gi 1490492289 1300 RNLADM--EIQ--LGAVKRI 1315
Cdd:cd07346 273 QRLANLynQLQqaLASLERI 292
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1329-1565 |
2.32e-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: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1329 LLA--PSLIPKNWPDQGK--IQIQNLSVRYD---SSLKPVLKHVNAL------ISPGQKIGICGRTGSGKSSFSLAFFRM 1395
Cdd:COG4172 256 LLAaePRGDPRPVPPDAPplLEARDLKVWFPikrGLFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1396 VD-----MFEGRIIIDGIDIAKLPlhtLRSRLSIILQDPvlFSgtirfNLDPEKKCSDsTLWEALEIAQLKL-------- 1462
Cdd:COG4172 336 IPsegeiRFDGQDLDGLSRRALRP---LRRRMQVVFQDP--FG-----SLSPRMTVGQ-IIAEGLRVHGPGLsaaerrar 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1463 VVKAL------PGGLDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFA------- 1529
Cdd:COG4172 405 VAEALeevgldPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehg 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 1530 --------DRTVV-TIAHRvhtilsadlVMVLKRGAILE-------FDKPET 1565
Cdd:COG4172 477 laylfishDLAVVrALAHR---------VMVMKDGKVVEqgpteqvFDAPQH 519
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1340-1539 |
2.34e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1340 PDQGKIQIQNLSVRyDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKLPLH--- 1416
Cdd:COG4178 358 SEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAI--------------AGLWPYgsg 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1417 --TLRSRLSIIL--QDPVLFSGTIRFNL---DPEKKCSDSTLWEALEIAQLKlvvkALPGGLDAIiTEGGENFSQGQRQL 1489
Cdd:COG4178 419 riARPAGARVLFlpQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLG----HLAERLDEE-ADWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1490 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1539
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1346-1557 |
2.75e-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: 67.56 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1346 QIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRM-----------VDMFEGRIIIDGIDIAKLP 1414
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTL----LKAilgllkptsgsIRVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1415 LHTLRSRLS-IILQDPVLFSGTIRFNLDPEKKCSDstlWEALEIAqLKLVvkalpgGLDAI----ITEggenFSQGQRQL 1489
Cdd:cd03235 75 QRRSIDRDFpISVRDVVLMGLYGHKGLFRRLSKAD---KAKVDEA-LERV------GLSELadrqIGE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1490 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-SADLVMVLKRGAI 1557
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLeYFDRVLLLNRTVV 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
697-914 |
3.06e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgedpsspeQETVADSDVRTRgPVAYASQK 776
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK--------LSSAAKAELRNQ-KLGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLL-NATVEENITFESPFNKQRYKMVIEACSlqpdiDILPH-GDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLD 854
Cdd:PRK11629 96 HHLLpDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 855 DPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 914
Cdd:PRK11629 171 EPTGNLDARNADSIFQL-LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1345-1568 |
3.16e-12 |
|
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: 68.29 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSL--KPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPvlfsgtiRFNLDPEKKCsDSTLWEALEIAQLKLVVKALPGGLDAIiteG-GENF--------SQGQRQLFCLA 1493
Cdd:COG1124 82 QMVFQDP-------YASLHPRHTV-DRILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1494 RAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1346-1558 |
3.17e-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: 66.69 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1346 QIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLRSRLSII 1425
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKS------------------------------TLLKTLAGL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1426 LQdpvLFSGTIRFNLDPEKKcsdstlWEALEIAQLKLVV----KALpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1501
Cdd:cd03214 49 LK---PSSGEILLDGKDLAS------LSPKELARKIAYVpqalELL--GLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1502 IFIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILSADLVMVLKRGAIL 1558
Cdd:cd03214 118 ILLLDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
700-903 |
3.46e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.74 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 700 ISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGED--PSSPEQETVADSDVRT--RGPVAyaSQ 775
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL------GKDllGMKDDEWRAVRSDIQMifQDPLA--SL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 KPWLlnaTVEENI-----TFESPFNKQ----RYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVARALY 845
Cdd:PRK15079 112 NPRM---TIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 846 QHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 903
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1345-1568 |
3.73e-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: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKL----------- 1413
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTL----LRAL--------------AGLlkpssgevlld 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1414 --PLHTLRSR-----LSIILQDPVL-FSGTIR--------------FNLDPE-KKCSDSTLwEALEIAQLKlvvkalpgg 1470
Cdd:COG1120 62 grDLASLSRRelarrIAYVPQEPPApFGLTVRelvalgryphlglfGRPSAEdREAVEEAL-ERTGLEHLA--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1471 lDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILS 1545
Cdd:COG1120 132 -DRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARY 204
|
250 260
....*....|....*....|...
gi 1490492289 1546 ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:COG1120 205 ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1083-1315 |
3.90e-12 |
|
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: 68.99 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1083 SVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYV-- 1160
Cdd:cd18552 60 TYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdw 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1161 --TPVFLVALLPLAVVCYFIQKYFRVASRDLQ-QLDDttqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSN--- 1234
Cdd:cd18552 140 klTLIALVVLPLAALPIRRIGKRLRKISRRSQeSMGD-----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLrrl 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1235 NIASLFLTAANRWLevrMEYIGACVVLIAAATSISNSLHRELSAG-LVGLgLTYALMVSNYLnwmvRNLADM--EIQ--L 1309
Cdd:cd18552 215 SMKIARARALSSPL---MELLGAIAIALVLWYGGYQVISGELTPGeFISF-ITALLLLYQPI----KRLSNVnaNLQrgL 286
|
....*.
gi 1490492289 1310 GAVKRI 1315
Cdd:cd18552 287 AAAERI 292
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
697-916 |
4.02e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.54 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSpeqETVADSDVRTRgpVAYASQK 776
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID------GVDITD---KKVKLSDIRKK--VGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 P--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDI--DILPhgdqtqigergINLSGGQRQRISVARAL 844
Cdd:PRK13637 92 PeyQLFEETIEKDIAF-GPINlglseeeiENRVKRAMNIVGLDYEDykDKSP-----------FELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1345-1554 |
4.37e-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: 67.11 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSS--LKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAKlPLHTLRSRL 1422
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLERPTSGEVLVDGE-PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFS-GTIRFN--LDPEKKCSDSTlwEALEIAQ--LKLVvkalpgGLdaiitEGGENF-----SQGQRQLFCL 1492
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGLELQGVPKA--EARERAEelLELV------GL-----SGFENAyphqlSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1493 ARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILSADLVMVLKR 1554
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1360-1556 |
6.23e-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: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1360 PVLKHVNALISPGQKIGICGRTGSGKSSFslaffRMVDMFEGRIIIDGIDiaklplHTlrSRLSIILQDPVLFSGTIRFN 1439
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSL-----LMLILGELEPSEGKIK------HS--GRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1440 LDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEN- 1518
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKe 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490492289 1519 ILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGA 1556
Cdd:cd03291 198 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
688-891 |
9.04e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 688 TWTPDGIPTLSNISIRipRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGED--PSSPEQEtvadsdvr 765
Cdd:PRK10771 8 TWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN------GQDhtTTPPSRR-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 trgPVAYASQKPWLLN-ATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQR 837
Cdd:PRK10771 72 ---PVSMLFQENNLFShLTVAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 838 ISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHKL 891
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDPAL-----RQEMLTLVSQvcQERqlTLLMVSHSL 190
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
690-925 |
1.01e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.95 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAV----FWNSLPDSEGEDPSSPEQETVADSDvR 765
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSKKIKNFK-E 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 TRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQ 834
Cdd:PRK13631 114 LRRRVSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 835 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagileLLRDDK---RTVVLVTHKL-QYLPHADWIIAMKDGTIQR 910
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-----LILDAKannKTVFVITHTMeHVLEVADEVIVMDKGKILK 256
|
250
....*....|....*
gi 1490492289 911 EGTlkdfqrsEYQLF 925
Cdd:PRK13631 257 TGT-------PYEIF 264
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
690-922 |
1.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.45 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSegedpSSPEQETVadSDVRTRGP 769
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVS-----STSKQKEI--KPVRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKPWLLNATVEENITFeSPFNKQRYKMVIEACSLQpDIDILphGDQTQIGERG-INLSGGQRQRISVARALYQHT 848
Cdd:PRK13643 88 VVFQFPESQLFEETVLKDVAF-GPQNFGIPKEKAEKIAAE-KLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 849 NVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRSEY 922
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDvFQEVDF 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
697-914 |
1.17e-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: 65.04 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEmqkvSGAVFWNSLPdsegedPSSPEQETVA-DSdvrtrgpvayasq 775
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFL------PKFSRNKLIFiDQ------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 kpwlLNATVEENITFespfnkqrykmvieacslqpdidiLPHGDQTQigergiNLSGGQRQRISVARALYQHT-NVVF-L 853
Cdd:cd03238 68 ----LQFLIDVGLGY------------------------LTLGQKLS------TLSGGELQRVKLASELFSEPpGTLFiL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 854 DDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 914
Cdd:cd03238 114 DEPSTGLHQQDINQLL--EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKV 172
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
690-924 |
1.21e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgedpsspeqeTVADSDVRT-RG 768
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH----------KTKDKYIRPvRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 PVAYASQKP--WLLNATVEENITFeSPFNkqrYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARALY 845
Cdd:PRK13646 86 RIGMVFQFPesQLFEDTVEREIIF-GPKN---FKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 846 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSEYQL 924
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRL-LKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
695-916 |
1.22e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.03 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKS-------SLLLATlgemqkvSGAVFWNSLPDSEGEDPSspeqetvadsDVRTR 767
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKStiakhmnALLIPS-------EGKVYVDGLDTSDEENLW----------DIRNK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 768 GPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 839
Cdd:PRK13633 87 AGMVFQNPDNQIVATIVEEDVAF-GPENlgippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
698-898 |
1.37e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 698 SNISIRIPRGQLTMIVGQVGCGKSSLL--LATLgeMQKVSGAVFWNSLPDSEGEDpsspeqetvadsdvrtrgpvAYASQ 775
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLriLAGL--ARPDAGEVLWQGEPIRRQRD--------------------EYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 KPWL--LNA-----TVEENITFespfnkqrykmvieACSLQPDIDilphGDQT-----QIGERGI------NLSGGQRQR 837
Cdd:PRK13538 76 LLYLghQPGiktelTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQRR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 838 ISVARALYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTHklQYLPHAD 898
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH--QDLPVAS 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1345-1539 |
1.45e-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: 64.48 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVdmfegriiidgidiAKL-PLHT------ 1417
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRAL--------------AGLwPWGSgrigmp 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1418 LRSRLSIILQDPVLFSGTIRfnldpekkcsdstlwealeiaqlklvvkalpgglDAIITEGGENFSQGQRQLFCLARAFV 1497
Cdd:cd03223 62 EGEDLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490492289 1498 RKTSIFIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1539
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
690-913 |
1.61e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdsegeDPSSPEQETVADSDVRTRGP 769
Cdd:PRK13645 20 TPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG--------DYAIPANLKKIKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKP--WLLNATVEENITFeSPFN-----KQRYKMVIEACSLQPdidiLPhgdQTQIGERGINLSGGQRQRISVAR 842
Cdd:PRK13645 92 IGLVFQFPeyQLFQETIEKDIAF-GPVNlgenkQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 843 ALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1345-1561 |
1.82e-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: 65.23 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPLHtlRS 1420
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLERpdsgEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1421 RLSIILQDPVLFS-----GTIRFNLD----PEKKCSDSTLwEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1491
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKlrgvPKAEIRARVR-ELLELVGLEGLLNRYPHEL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 1492 LARAFVRKTSIFIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFD 1561
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1345-1555 |
1.91e-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: 64.34 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSfslaffrmvdmfegriiidgidiaklplhTLRSRLSI 1424
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTT-----------------------------LIKIILGL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDpvlfSGTIR-FNLDPEKkcsdstlwealEIAQLKLVVKALPGGlDAIITE--GGEN--FSQGQRQLFCLARAFVRK 1499
Cdd:cd03230 50 LKPD----SGEIKvLGKDIKK-----------EPEEVKRRIGYLPEE-PSLYENltVRENlkLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 1500 TSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILS-ADLVMVLKRG 1555
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1345-1555 |
2.10e-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: 64.13 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYdsSLKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEG------RIIIDGIDIAKLPLHTL 1418
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAGLEEpdsgsiLIDGEDLTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1419 RSRLSIILQDPVLFSG-TIRFNLdpekkcsdstlwealeiaqlklvvkALPggldaiiteggenFSQGQRQLFCLARAFV 1497
Cdd:cd03229 75 RRRIGMVFQDFALFPHlTVLENI-------------------------ALG-------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 1498 RKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVMVLKRG 1555
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1345-1559 |
3.02e-11 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 64.91 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLK--PVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFE-------GRIIIDGIDIAKLPL 1415
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsgsvLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1416 HTLRSRLSIILQDPVLFS-----GTIRFNLD---PEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQR 1487
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 1488 QLFCLARAFVRKTSIFIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVMVLKRGAILE 1559
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
697-917 |
3.13e-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: 65.02 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWNslpdseGEDPSSPEQETVAdsdVRTRgpVAYAS 774
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTITVD------GEDLTDSKKDINK---LRRK--VGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QK----PwllNATVEENITfESP-----FNKQrykmviEACSLQpdIDILphgDQTQIGERG----INLSGGQRQRISVA 841
Cdd:COG1126 84 QQfnlfP---HLTVLENVT-LAPikvkkMSKA------EAEERA--MELL---ERVGLADKAdaypAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 917
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELV-----GEVLDVMRDlakEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
830-935 |
3.37e-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: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
90 100
....*....|....*....|....*..
gi 1490492289 909 QREGTLKdfqrseyQLFEHWKTLMNRQ 935
Cdd:PRK11264 223 VEQGPAK-------ALFADPQQPRTRQ 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1345-1577 |
3.52e-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: 64.83 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSF--SLA----------FFRMVDMFEGRIIIdgidiak 1412
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLlrLIVgllrpdsgevLIDGEDISGLSEAE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1413 lpLHTLRSRLSIILQDPVLFSG-TIR----FNLDPEKKCSDSTLweaLEIAQLKLVVKALPGGLDAIITEggenFSQGQR 1487
Cdd:cd03261 72 --LYRLRRRMGMLFQSGALFDSlTVFenvaFPLREHTRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE----LSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1488 QLFCLARAFVRKTSIFIMDEATASID-MATENI------LQKVVmtafaDRTVVTIAHRVHTILS-ADLVMVLKRGAILE 1559
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDpIASGVIddlirsLKKEL-----GLTSIMVTHDLDTAFAiADRIAVLYDGKIVA 217
|
250
....*....|....*...
gi 1490492289 1560 FDKPETLLNQKDSIFASF 1577
Cdd:cd03261 218 EGTPEELRASDDPLVRQF 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1345-1571 |
4.66e-11 |
|
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: 64.51 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP---LHTLRSR 1421
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1422 LSIILQDpvlfsgtirFNLDPEK---------KCSDSTLWEAL-------EIAQ----LKLVvkalpgGLDAIITEGGEN 1481
Cdd:cd03256 80 IGMIFQQ---------FNLIERLsvlenvlsgRLGRRSTWRSLfglfpkeEKQRalaaLERV------GLLDKAYQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1482 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILS-ADLVMVLKR 1554
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGLKD 220
|
250
....*....|....*..
gi 1490492289 1555 GAILeFDKPETLLNQKD 1571
Cdd:cd03256 221 GRIV-FDGPPAELTDEV 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
693-921 |
7.47e-11 |
|
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: 64.00 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDpsspeqETVADSDVRTRGPVAY 772
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD------GED------ITGLPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWLL-NATVEENI----------TFESPFNKQRYKMVIEACSlqpdiDILphgDQTQIGERG----INLSGGQRQR 837
Cdd:cd03219 80 TFQIPRLFpELTVLENVmvaaqartgsGLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 838 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKD 916
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDE 229
|
....*
gi 1490492289 917 FQRSE 921
Cdd:cd03219 230 VRNNP 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
699-916 |
1.01e-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: 65.12 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdsegedpsspeQETVADSDVRT-----RGPVAYA 773
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG--------------GEVLQDSARGIflpphRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQK----PWLlnaTVEENITF---ESPFNKQRYKM--VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARAL 844
Cdd:COG4148 83 FQEarlfPHL---SVRGNLLYgrkRAPRAERRISFdeVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKL---QYLphADWIIAMKDGTIQREGTLKD 916
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEILP--YLERLRDELDIpILYVSHSLdevARL--ADHVVLLEQGRVVASGPLAE 220
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1067-1227 |
1.13e-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: 64.46 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1067 VFTV--LCSLGIVLCLVTSvtvewtGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1144
Cdd:cd18573 50 VFVVgaAANFGRVYLLRIA------GERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1145 RSTLLCVSALTVISYVTP-VFLVALL---PLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPllshfAETVEGLTTIRAF-- 1217
Cdd:cd18573 124 RSLVSGVGGIGMMLYISPkLTLVMLLvvpPIAVGAVFYGRYVRKLSKQVQDaLADATKVA-----EERLSNIRTVRAFaa 198
|
170
....*....|..
gi 1490492289 1218 -RYE-ARFQQKL 1227
Cdd:cd18573 199 eRKEvERYAKKV 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1270-1568 |
1.29e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1270 NSLHRELSAGLvglgltyaLMVSNYLNwMVRNLAD--MEIQLGAV---KRIHALLKTEAESY-EGLLA--PSLIPKNWPD 1341
Cdd:PRK15134 200 RELQQELNMGL--------LFITHNLS-IVRKLADrvAVMQNGRCveqNRAATLFSAPTHPYtQKLLNsePSGDPVPLPE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1342 QGK--IQIQNLSV---------RYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVD-----MFEGRIII 1405
Cdd:PRK15134 271 PASplLDVEQLQVafpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINsqgeiWFDGQPLH 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1406 DGIDIAKLPlhtLRSRLSIILQDPvlfSGTIRFNLDPEKkcsdsTLWEALEIAQLKL--------VVKALPG-GLDAII- 1475
Cdd:PRK15134 351 NLNRRQLLP---VRHRIQVVFQDP---NSSLNPRLNVLQ-----IIEEGLRVHQPTLsaaqreqqVIAVMEEvGLDPETr 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1476 ----TEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASID-------MATENILQKVVMTAFadrtvVTIAHRVHTIL 1544
Cdd:PRK15134 420 hrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY-----LFISHDLHVVR 490
|
330 340
....*....|....*....|....*
gi 1490492289 1545 S-ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:PRK15134 491 AlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1345-1513 |
1.41e-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: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMV----DMFEGRIIIDGIDIAKLPLHtLRS 1420
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllPPSAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1421 RLSIILQDPVLFSG-TIRFNLD-----PEKKCSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLFCLAR 1494
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALAR 144
|
170
....*....|....*....
gi 1490492289 1495 AFVRKTSIFIMDEATASID 1513
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALD 163
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1064-1315 |
1.50e-10 |
|
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: 64.10 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1064 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1143
Cdd:cd18572 38 AVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1144 SRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLpllshfAETVEGL-TTIRAF 1217
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQDaLAEANQV------AEEALSNiRTVRSF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1218 ---RYEA-RFQQKLLEYTDSN---NIASLFLTAANRWLevrmEYIGACVVLIAAATSIsnsLHRELSAG-LVGLGLtYAL 1289
Cdd:cd18572 192 ateEREArRYERALDKALKLSvrqALAYAGYVAVNTLL----QNGTQVLVLFYGGHLV---LSGRMSAGqLVTFML-YQQ 263
|
250 260
....*....|....*....|....*.
gi 1490492289 1290 MVSNYLNWMVRNLADMEIQLGAVKRI 1315
Cdd:cd18572 264 QLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
697-903 |
1.51e-10 |
|
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: 63.05 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATL-GEMQK-----VSGAV--FWNSLPDS-----EGEDPS-SPEQETVADS 762
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyAEGQRryvesLSAYArqFLGQMDKPdvdsiEGLSPAiAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 763 DVRTRGPVAYASQKPWLLNATVeeNItfespfnKQRYKMVIEacslqpdidilphgdqtqIG------ERGIN-LSGGQR 835
Cdd:cd03270 91 PRSTVGTVTEIYDYLRLLFARV--GI-------RERLGFLVD------------------VGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 836 QRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 903
Cdd:cd03270 144 QRIRLATQIgSGLTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1345-1538 |
1.55e-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: 60.93 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslaffrmvdmfegriiidgidiaklplhtlrsrLSI 1424
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPVLFSGTIRFNldpekkcsdstlwEALEIAQLklvvkalpggldaiiteggENFSQGQRQLFCLARAFVRKTSIFI 1504
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490492289 1505 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1538
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
699-912 |
1.59e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.67 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVF-----WNSLPDSEgedpsspeqetvadsdvRTRGPV--A 771
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekrMNDVPPAE-----------------RGVGMVfqS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQkPWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARAL 844
Cdd:PRK11000 84 YALY-PHL---SVAENMSFglklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 845 YQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 912
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1345-1569 |
1.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.67 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSlaffRMVDMF----EGRIIIDGIDIAKLPLHTL-- 1418
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIS----KLINGLllpdDNPNSKITVDGITLTAKTVwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1419 -RSRLSIILQDP-VLFSGT-----IRFNLD----PEKKcsdstlwealeiaQLKLVVKALP--GGLDAIITEGgENFSQG 1485
Cdd:PRK13640 82 iREKVGIVFQNPdNQFVGAtvgddVAFGLEnravPRPE-------------MIKIVRDVLAdvGMLDYIDSEP-ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1486 QRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKP 1563
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
....*.
gi 1490492289 1564 ETLLNQ 1569
Cdd:PRK13640 228 VEIFSK 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
692-950 |
3.69e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQKVSGAVFWN----------SLPDSEGEdPSSPEQETV 759
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvLRGMDQYEPTSGRIIYHvalcekcgyvERPSKVGE-PCPVCGGTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 760 ADSDV-----------RTRGPVAYASQKPWLL--NATVEENITfeSPFNKQRYKmviEACSLQPDIDILphgDQTQIGER 826
Cdd:TIGR03269 90 EPEEVdfwnlsdklrrRIRKRIAIMLQRTFALygDDTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EMVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 827 ----GINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWII 901
Cdd:TIGR03269 162 ithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1490492289 902 AMKDGTIQREGTLKDFQRSEYQLFEhwktlmnrqdqELEKETVLERKAP 950
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFMEGVS-----------EVEKECEVEVGEP 278
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
379-611 |
3.74e-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: 62.95 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 379 YVAIETGINLRGAIQTKIYNKIMQLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYIL 457
Cdd:cd07346 61 YLAARLGQRVVFDLRRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIGALVILFYLN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 458 GVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWE----NIFCSRVEMTRKKEMTS 533
Cdd:cd07346 139 WKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 534 LRAFAVYTSISIFMNTaipIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 611
Cdd:cd07346 219 ARLSALFSPLIGLLTA---LGTALVLLYG-GYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
690-890 |
3.98e-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: 64.77 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSlLLATLGEMQKVSGAVFwnslpdsegedpSSPEqetvadsdvrtRGP 769
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGRL------------TKPA-----------KGK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKPWLLNATVEENITF-ESPFNKQRYKMvieacSLQPDIDILPHGDQTQIGERGIN----------LSGGQRQRI 838
Cdd:TIGR00954 517 LFYVPQRPYMTLGTLRDQIIYpDSSEDMKRRGL-----SDKDLEQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 839 SVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHK 890
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVD-----VEGYMYRLCREFGITLFSVSHR 638
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
697-912 |
4.81e-10 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 61.05 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGqLTMIVGQVGCGKSSLL--LATLgeMQKVSGAVFWNslpdseGEDPSSPEQETvadsdvrtRGPVAYAS 774
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMriLATL--TPPSSGTIRID------GQDVLKQPQKL--------RRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKP-WLLNATVEENITF-------ESPFNKQRYKMVIEAcslqpdIDILPHGDQtQIGErginLSGGQRQRISVARALYQ 846
Cdd:cd03264 79 QEFgVYPNFTVREFLDYiawlkgiPSKEVKARVDEVLEL------VNLGDRAKK-KIGS----LSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 847 HTNVVFLDDPFSALD----VHLSDHLMQAGilellrdDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 912
Cdd:cd03264 148 DPSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
692-913 |
8.58e-10 |
|
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: 60.46 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSL--LLATLgemqkvsgavfwnsLPDSEGEdpsspeqETVADSDVR---- 765
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTikMLTTL--------------LKPTSGR-------ATVAGHDVVrepr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 -TRGPVAYASQKPWLLNA-TVEENIT-------FESPFNKQRYKMVIEAcslqpdIDILPHGDqtqigERGINLSGGQRQ 836
Cdd:cd03265 70 eVRRRIGIVFQDLSVDDElTGWENLYiharlygVPGAERRERIDELLDF------VGLLEAAD-----RLVKTYSGGMRR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREG 912
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEG 214
|
.
gi 1490492289 913 T 913
Cdd:cd03265 215 T 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1345-1543 |
9.14e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRM------------VDMFEGRIIIDgidiaK 1412
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesevrvegrVEFFNQNIYER-----R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1413 LPLHTLRSRLSIILQDPVLFSGTI---------------RFNLDP--EKKCSDSTLWEalEIAQlKLVVKALpggldaii 1475
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVydnvaygvkivgwrpKLEIDDivESALKDADLWD--EIKH-KIHKSAL-------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 1476 teggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1543
Cdd:PRK14258 150 -----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1345-1568 |
1.43e-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: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSF-SLAFFRM-----------------VDMFEgriiid 1406
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLpptygndvrlfgerrggEDVWE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1407 gidiaklplhtLRSRLSII---LQDPVLFSGTIR-------FnldpekkcsDST-LWEALEIAQLKLVVKALPG-GLDAI 1474
Cdd:COG1119 76 -----------LRKRIGLVspaLQLRFPRDETVLdvvlsgfF---------DSIgLYREPTDEQRERARELLELlGLAHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1475 ItegGENF---SQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILSA- 1546
Cdd:COG1119 136 A---DRPFgtlSQGEQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGi 210
|
250 260
....*....|....*....|..
gi 1490492289 1547 DLVMVLKRGAILEFDKPETLLN 1568
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVLT 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
697-916 |
1.50e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSlpdsegedpsspeqETVADSDVR-TRGPVAYASQ 775
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG--------------EPITKENIReVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 KP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 845
Cdd:PRK13652 86 NPddQIFSPTVEQDIAF-GPINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 846 QHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEE 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1345-1570 |
1.63e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.24 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLkpVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------- 1417
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpdvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1418 LRSRLSIILQDPVLFSG-TIRFN----------LDPEKKCSDSTLWeALEIAQLKLVVKALpggldaiITEGGENFSQGQ 1486
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNvaigvklnglVKSKKELDERVEW-ALKKAALWDEVKDR-------LNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1487 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILSADLVMVLKRGAILE------ 1559
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgptrk 234
|
250
....*....|..
gi 1490492289 1560 -FDKPETLLNQK 1570
Cdd:PRK14267 235 vFENPEHELTEK 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
697-927 |
1.86e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.47 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLP----DSEGEDPSSPEQETV---ADSDVRTRGP 769
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklNRAQRKAFRRDIQMVfqdSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKPW--LLNATVEENItfespfnkQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVARALYQ 846
Cdd:PRK10419 108 VREIIREPLrhLLSLDKAERL--------ARASEMLRAVDLDDSVlDKRPP-----------QLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 847 HTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRse 921
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQqfgtACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLT-- 241
|
....*.
gi 1490492289 922 yqlFEH 927
Cdd:PRK10419 242 ---FSS 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1345-1557 |
1.96e-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: 58.21 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlkPVLKHVNALISPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrLSI 1424
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKS------------------------------TL---MKI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 I--LQDPVlfSGTIRFNldpEKKCSDSTLWEALE-----IAQLklvvkalpggldaiiteggenfSQGQRQLFCLARAFV 1497
Cdd:cd03216 46 LsgLYKPD--SGEILVD---GKEVSFASPRDARRagiamVYQL----------------------SVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1498 RKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRGAI 1557
Cdd:cd03216 99 RNARLLILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
692-921 |
1.98e-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: 59.61 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGED--PSSPEQetvadsdvRTRGP 769
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD------GEDitGLPPHR--------IARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQK----PWLlnaTVEENIT--FESPFNKQRYKMVIEACslqpdIDILPhgdqtQIGER----GINLSGGQRQRIS 839
Cdd:COG0410 80 IGYVPEGrrifPSL---TVEENLLlgAYARRDRAEVRADLERV-----YELFP-----RLKERrrqrAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDFQ 918
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFE--IIRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELL 224
|
...
gi 1490492289 919 RSE 921
Cdd:COG0410 225 ADP 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
697-889 |
2.17e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.86 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMqkvsgavfwnslPDS-----EGEDPSS-PEQETVAdsdvrTRGP 769
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrCINLLER------------PTSgsvlvDGVDLTAlSERELRA-----ARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 770 VAYASQKPWLLNA-TVEENITFesPF------NKQRYKMVIEACSLqpdIDILPHGDQ--TQigerginLSGGQRQRISV 840
Cdd:COG1135 84 IGMIFQHFNLLSSrTVAENVAL--PLeiagvpKAEIRKRVAELLEL---VGLSDKADAypSQ-------LSGGQKQRVGI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 841 ARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTH 889
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTR-----SILDLLKDINRelglTIVLITH 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1345-1543 |
2.39e-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: 58.96 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLkPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP---LHTLRSR 1421
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1422 LSIILQDpvlfsgtirFNLDPEKKCSDSTLWeALEIAQL--KLVVKALPGGLDAIITEGGEN-----FSQGQRQLFCLAR 1494
Cdd:cd03292 80 IGVVFQD---------FRLLPDRNVYENVAF-ALEVTGVppREIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1495 AFVRKTSIFIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRVHTI 1543
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHRVIAL 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1349-1555 |
3.83e-09 |
|
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: 57.95 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1349 NLSVRYDSSL----KPVLKHVNALISPGQKIGICGRTGSGKSSF--SLAFFRMVdmfEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:cd03213 8 NLTVTVKSSPsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTG---LGVSGEVLINGRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFsgtirfnldpekkcSDSTLWEALEI-AQLKlvvkalpgGLdaiiteggenfSQGQRQLFCLARAFVRKTS 1501
Cdd:cd03213 85 GYVPQDDILH--------------PTLTVRETLMFaAKLR--------GL-----------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 1502 IFIMDEATASIDMATENILQKVVMtAFAD--RTVVTIAHRVHTIL--SADLVMVLKRG 1555
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
831-908 |
3.90e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL---QYLPHAdwIIAM 903
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225
|
....*
gi 1490492289 904 KDGTI 908
Cdd:PRK11701 226 KQGRV 230
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1068-1315 |
3.99e-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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 59.81 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1068 FTVLCSLGIVLCLVTSV---TVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1144
Cdd:cd18575 39 FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1145 RSTLLCVSALTVISYVTP---VFLVALLPLAVV-CYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAFRY 1219
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQdRLADLS-----AFAEETLSAIKTVQAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1220 EARFQQKLLEYTDSNniaslfLTAANRWLEVRMEYIGACVVLIAAATS------ISNSLHRELSAGLVGLGLTYALMVSN 1293
Cdd:cd18575 194 EDAERQRFATAVEAA------FAAALRRIRARALLTALVIFLVFGAIVfvlwlgAHDVLAGRMSAGELSQFVFYAVLAAG 267
|
250 260
....*....|....*....|..
gi 1490492289 1294 YLNWMVRNLADMEIQLGAVKRI 1315
Cdd:cd18575 268 SVGALSEVWGDLQRAAGAAERL 289
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
697-916 |
4.25e-09 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 58.94 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL-LATlGEMQKVSGA---VFwnslpdseGEDPsspEQETVADsdVRTR-GPVA 771
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLsLIT-GDLPPTYGNdvrLF--------GERR---GGEDVWE--LRKRiGLVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLLNATVEENIT---FESPFNKQRY--KMVIEACSLQPDIDILPHGDQTqIGErginLSGGQRQRISVARALYQ 846
Cdd:COG1119 85 PALQLRFPRDETVLDVVLsgfFDSIGLYREPtdEQRERARELLELLGLAHLADRP-FGT----LSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP----HAdwiIAMKDGTIQREGTLKD 916
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLAL-LDKLAAEGAPTLVLVTHHVEEIPpgitHV---LLLKDGRVVAAGPKEE 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
695-921 |
4.47e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.36 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnslpdSEGEDPSspeQETVADsdvrTRGPVAYAS 774
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII------IDGDLLT---EENVWD----IRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKP--WLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHT 848
Cdd:PRK13650 88 QNPdnQFVGATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDF-----KEREPAR---LSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 849 NVVFLDDPFSALDvhlsdhlmQAGILELLRDDKR-------TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRS 920
Cdd:PRK13650 160 KIIILDEATSMLD--------PEGRLELIKTIKGirddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSRG 231
|
.
gi 1490492289 921 E 921
Cdd:PRK13650 232 N 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
700-912 |
4.99e-09 |
|
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: 58.15 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 700 ISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpDSEGEDPSSPEQEtvadsdVRTRGPVAYASQK--P 777
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------TVDGFDVVKEPAE------ARRRLGFVSDSTGlyD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 778 WLlnaTVEENITFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARALYQHTNV 850
Cdd:cd03266 92 RL---TARENLEYFAGLYglkgdelTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 851 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 912
Cdd:cd03266 158 LLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
693-955 |
5.51e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.81 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQKVSGAVFWNslpdseGEDPSS-PEQETVadsdvRTRGPV 770
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrCINLLE-RPTSGRVLVD------GQDLTAlSEKELR-----KARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPWLLNA-TVEENITFespfnkqrykmvieacSLQpdidiLPHGDQTQIGER--------GI---------NLSG 832
Cdd:PRK11153 85 GMIFQHFNLLSSrTVFDNVAL----------------PLE-----LAGTPKAEIKARvtellelvGLsdkadrypaQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGT 907
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVIDAGR 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 908 IQREGTLkdfqrseYQLFEHWKTLMNRQ------DQELEkETVLERKAPEPSQG 955
Cdd:PRK11153 219 LVEQGTV-------SEVFSHPKHPLTREfiqstlHLDLP-EDYLARLQAEPTTG 264
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
830-917 |
6.17e-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: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL----QYlphADWII 901
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLgvvrRF---ADRVA 228
|
90
....*....|....*.
gi 1490492289 902 AMKDGTIQREGTLKDF 917
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
697-913 |
6.58e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.05 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgedpsspeqetVADSDVRT--RGPVAYAS 774
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK-----------ISDAELREvrRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLL-NATVEENITFESPFN----KQRYKMVIEACSlQPDIDILPHGDQTQigerginLSGGQRQRISVARALYQHTN 849
Cdd:PRK10070 113 QSFALMpHMTVLDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 850 VVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
686-908 |
6.80e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.56 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 686 FFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLAtlgemqkVSGAVfwnsLPDSeGedpsspeQETVADSDVr 765
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA-------IAGSL----PPDS-G-------SILIDGKDV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 TRGPV----AYAS---QKPwLL----NATVEENI----------TFESPFNKQRYKMVIEACSlqpDIDI-LPHGDQTQI 823
Cdd:COG1101 71 TKLPEykraKYIGrvfQDP-MMgtapSMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLA---TLGLgLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 824 GergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagiL--ELLRDDKRTVVLVTHKLQY-LPHADWI 900
Cdd:COG1101 147 G----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRL 219
|
....*...
gi 1490492289 901 IAMKDGTI 908
Cdd:COG1101 220 IMMHEGRI 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
699-920 |
9.96e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGeMQKVSGAVFWNSLpDSEGED---PSSPEQETVADSDVrtrgpvAYASQ 775
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMAEKL-EFNGQDlqrISEKERRNLVGAEV------AMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 KPWL-LNA--TVEENI-----TFESPFNKQRYKMVIEACSLQ--PD----IDILPHgdqtqigergiNLSGGQRQRISVA 841
Cdd:PRK11022 97 DPMTsLNPcyTVGFQImeaikVHQGGNKKTRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 842 RALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELL----RDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDV-----TIQAQIIELLlelqQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHD 240
|
....
gi 1490492289 917 FQRS 920
Cdd:PRK11022 241 IFRA 244
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
697-913 |
1.12e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ----KVSGAVFWNSlpdsegedpsspeQETVADSDVRTRGPV 770
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYdskiKVDGKVLYFG-------------KDIFQIDAIKLRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKP-WLLNATVEENITFesPF------NKQRYKMVIEACSLQPDIDILPHgdqTQIGERGINLSGGQRQRISVARA 843
Cdd:PRK14246 93 GMVFQQPnPFPHLSIYDNIAY--PLkshgikEKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 844 LYQHTNVVFLDDPFSALDVhLSDHLMQAGILELlrDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 913
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDI-VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
689-908 |
1.21e-08 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 57.44 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 689 WTPDGIPT-LSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGemQKVSGAVFWNslpdseGEDPSSPEQETVADsdVR 765
Cdd:COG4181 19 GTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLglLAGLD--RPTSGTVRLA------GQDLFALDEDARAR--LR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 TRGpVAYASQKPWLLNA-TVEENITFESPFN-----KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRIS 839
Cdd:COG4181 89 ARH-VGFVFQSFQLLPTlTALENVMLPLELAgrrdaRARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQ-----IIDLLFELNRergtTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1345-1573 |
1.30e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.84 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPV-LFSGTI-----RFNLD----PEKKCSdSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLAR 1494
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLEnhavPYDEMH-RRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1495 AFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLNQKDS 1572
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
.
gi 1490492289 1573 I 1573
Cdd:PRK13648 236 L 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
697-908 |
1.39e-08 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 56.29 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGED--PSSPEQetvadsdvRTRGPVAYAS 774
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD------GKPvtRRSPRD--------AIRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 ----QKPWLLNATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQHTNV 850
Cdd:cd03215 82 edrkREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 851 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
697-906 |
1.40e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 57.54 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSL--LLAtlGEMQKVSGAVFWNSLPDSEG-------------EDPSS---PEQet 758
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLakMLA--GIIEPTSGEILINGHKLEYGdykyrckhirmifQDPNTslnPRL-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 759 vadsdvrTRGPVAYAsqkPWLLNATVEEnitfespfnKQRYKMVIEACS---LQPD-IDILPHgdqtqigergiNLSGGQ 834
Cdd:COG4167 105 -------NIGQILEE---PLRLNTDLTA---------EEREERIFATLRlvgLLPEhANFYPH-----------MLSSGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 835 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 906
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINL-MLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1345-1559 |
1.53e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRY---DSSLKPVLKHVNAL--IS----PGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLP- 1414
Cdd:PRK10261 314 LQVRNLVTRFplrSGLLNRVTREVHAVekVSfdlwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1415 --LHTLRSRLSIILQDPVLfsgtirfNLDPEKKCSDSTLwEALEIAQLkLVVKALPGGLDAIITEGG----------ENF 1482
Cdd:PRK10261 394 gkLQALRRDIQFIFQDPYA-------SLDPRQTVGDSIM-EPLRVHGL-LPGKAAAARVAWLLERVGllpehawrypHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1483 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NI---LQKVVMTAFA----DRTVVT-IAHRVHTILSADLVM 1550
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLlldLQRDFGIAYLfishDMAVVErISHRVAVMYLGQIVE 544
|
....*....
gi 1490492289 1551 VLKRGAILE 1559
Cdd:PRK10261 545 IGPRRAVFE 553
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
697-921 |
1.57e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQKVS-GAVFWNSLPDSEGEDPSSPEQetvadsdvrtrgpVAYASQ 775
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPPSeGEILLDAQPLESWSSKAFARK-------------VAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 K-PWLLNATVEENITF-ESP-------FNKQRYKMVIEACSLqpdIDILPhgdqtqIGERGIN-LSGGQRQRISVARALY 845
Cdd:PRK10575 93 QlPAAEGMTVRELVAIgRYPwhgalgrFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 846 QHTNVVFLDDPFSALDV-HLSDHLmqAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
694-911 |
1.59e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEDPSSPEQETVADSDVRTRGPVAYA 773
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL------VGQPLHQMDEEARAKLRAKHVGFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQKPWLLNATveENITFESPFNKQRykmviEACSLQPDIDILphgDQTQIGER----GINLSGGQRQRISVARALYQHTN 849
Cdd:PRK10584 97 FMLIPTLNAL--ENVELPALLRGES-----SRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 850 VVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 911
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADL-LFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
697-928 |
2.13e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL-------LATLGEMQkVSGAVFwnslpdsegeDPSSPEQEtvadSDVRT-RG 768
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLrvlnlleMPRSGTLN-IAGNHF----------DFSKTPSD----KAIRElRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 PVAYASQK----PWLlnaTVEENITfESPFN---------KQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQR 835
Cdd:PRK11124 83 NVGMVFQQynlwPHL---TVQQNLI-EAPCRvlglskdqaLARAEKLLERLRLKPYADRFP-----------LHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 836 QRISVARALYQHTNVVFLDDPFSALD-------VHLSDHLMQAGIlellrddkrTVVLVTHKLQYLPH-ADWIIAMKDGT 907
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETGI---------TQVIVTHEVEVARKtASRVVYMENGH 218
|
250 260
....*....|....*....|.
gi 1490492289 908 IQREGTLKDFQRSEYQLFEHW 928
Cdd:PRK11124 219 IVEQGDASCFTQPQTEAFKNY 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
697-921 |
2.21e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpDSEGEdpsspeqETVADSDVRTRGPVAYASQK 776
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV------KIDGE-------LLTAENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 P--WLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHTNV 850
Cdd:PRK13642 90 PdnQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDF-----KTREPAR---LSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 851 VFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 921
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRV-IHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSElFATSE 232
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1064-1226 |
2.52e-08 |
|
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: 57.40 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1064 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1143
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1144 SRSTLLCVSALTVISYV----TPVFLVALLPLAVVCYFIQKYFRVASRDL-QQLDDttqlpLLSHFAETVEGLTTIRAFR 1218
Cdd:cd18544 123 IGDLLLLIGILIAMFLLnwrlALISLLVLPLLLLATYLFRKKSRKAYREVrEKLSR-----LNAFLQESISGMSVIQLFN 197
|
....*...
gi 1490492289 1219 YEARFQQK 1226
Cdd:cd18544 198 REKREFEE 205
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
692-907 |
2.66e-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: 54.38 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSlpdsegedpsspeqetvadsdvrtRGPVA 771
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVV 851
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 852 FLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGT 907
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEA-----LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
693-912 |
3.14e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLlatlgemqKV-SGavfwNSLPDSeGEdpsspeqetvadsdVRTRG-PV 770
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLL--------KIlSG----NYQPDA-GS--------------ILIDGqEM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPwLLNA---------------TVEENI---TFESPFNKQRYKMVIEACSLQPD---IDILPhgdQTQIGErgin 829
Cdd:PRK11288 69 RFASTTA-ALAAgvaiiyqelhlvpemTVAENLylgQLPHKGGIVNRRLLNYEAREQLEhlgVDIDP---DTPLKY---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLqylphaDWIIAMKDG-TI 908
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTV 212
|
....
gi 1490492289 909 QREG 912
Cdd:PRK11288 213 FKDG 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
690-922 |
3.25e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 690 TPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSlpdsegedpsspeQETVADS---DVRT 766
Cdd:PRK13649 16 TPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD-------------TLITSTSknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 767 -RGPVAYASQKP--WLLNATVEENITFeSPFNKQRYKmvIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 843
Cdd:PRK13649 83 iRKKVGLVFQFPesQLFEETVLKDVAF-GPQNFGVSQ--EEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 844 LYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRSE 921
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDiFQDVD 237
|
.
gi 1490492289 922 Y 922
Cdd:PRK13649 238 F 238
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
697-913 |
3.84e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.47 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQKVSGAVFWNSL----PDSEGEDPSS-PEQ 756
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLEHIDKVividQSPIGRTPRSnPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 757 ETVADSDVRT------RGP--------VAYASQK-PWLLNATVEENITFESPFNKQRYKmvieacsLQPDIDIlphG-DQ 820
Cdd:cd03271 91 YTGVFDEIRElfcevcKGKrynretleVRYKGKSiADVLDMTVEEALEFFENIPKIARK-------LQTLCDV---GlGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 821 TQIGERGINLSGGQRQRISVARALYQ---HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHA 897
Cdd:cd03271 161 IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLE--VLQRLVDKGNTVVVIEHNLDVIKCA 238
|
250 260
....*....|....*....|..
gi 1490492289 898 DWIIAM------KDGTIQREGT 913
Cdd:cd03271 239 DWIIDLgpeggdGGGQVVASGT 260
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
689-910 |
3.85e-08 |
|
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: 56.40 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 689 WTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATL------GEMQkVSGaVFWNSLPDSEgedpsspeqetvads 762
Cdd:cd03289 12 YTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQ-IDG-VSWNSVPLQK--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 763 dvrTRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 842
Cdd:cd03289 75 ---WRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 843 ALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQR 910
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
695-919 |
3.92e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.25 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEM----QKVSGAVFWNSLPdsegedpsspeqetVADSDVRTRgPV 770
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKP--------------VAPCALRGR-KI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQKPwllnatveenitfESPFNKQRyKM---VIEAC---SLQPDIDILPH-------GDQTQIGER-GINLSGGQRQ 836
Cdd:PRK10418 82 ATIMQNP-------------RSAFNPLH-TMhthARETClalGKPADDATLTAaleavglENAARVLKLyPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRT----VVLVTHKLQYLPH-ADWIIAMKDGTIQRE 911
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDV-----VAQARILDLLESIVQKralgMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
....*....
gi 1490492289 912 GTLKD-FQR 919
Cdd:PRK10418 223 GDVETlFNA 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1345-1582 |
4.02e-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: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPVLFSG-TIRFN--LDP--EKkcsdstlWEALEIAQ-----LKLVvkalpgGLDaiITEGGENF----SQGQRQLF 1490
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPklLK-------WPKEKIREradelLALV------GLD--PAEFADRYphelSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1491 CLARAFVRKTSIFIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILSADLVMVLKRGAILEFDKP 1563
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTP 220
|
250 260
....*....|....*....|
gi 1490492289 1564 ETLL-NQKDSIFASFVRADK 1582
Cdd:cd03295 221 DEILrSPANDFVAEFVGADR 240
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
697-921 |
6.17e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ--------KVSGAVFWNslpdseGEdpssPEQETVADSDVRTRG 768
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN------GE----PLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 PVAYASQKPWLLnaTVEENITFespfnkQRYKMVIEACSL-QPDIDILPH-----GDQTQIGERGINLSGGQRQRISVAR 842
Cdd:PRK13547 87 VLPQAAQPAFAF--SAREIVLL------GRYPHARRAGALtHRDGEIAWQalalaGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 843 ALYQ---------HTNVVFLDDPFSALDV-HlsDHLMQAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQRE 911
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLaH--QHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVAH 236
|
250
....*....|
gi 1490492289 912 GTLKDFQRSE 921
Cdd:PRK13547 237 GAPADVLTPA 246
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1091-1227 |
6.78e-08 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 55.91 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1091 LKVAKRLHHSLL----NCIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPST-LECLSRSTLLCVSALTVISYVTPVFL 1165
Cdd:cd18570 67 LKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1166 VALLPL---AVVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFRYEARFQQKL 1227
Cdd:cd18570 146 ITLLIIplyILIILLFNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKKI 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
697-942 |
7.71e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 57.00 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQKVSGAVFWNS------LPDsegEDPSSPEQ---ETVADSDVR 765
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLkiLA--GELEPDSGEVSIPKglrigyLPQ---EPPLDDDLtvlDTVLDGDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 TRGPVA---YASQKPWLLNATVEENITFESPFNkqrykmVIEACSLQPDIDI------LPHGDQTQ-IGErginLSGGQR 835
Cdd:COG0488 89 LRALEAeleELEAKLAEPDEDLERLAELQEEFE------ALGGWEAEARAEEilsglgFPEEDLDRpVSE----LSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 836 QRISVARALYQHTNVVFLDDPFSALDVHlsdhlmqaGIL---ELLRDDKRTVVLVTH------KLqylphADWIIAMKDG 906
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLE--------SIEwleEFLKNYPGTVLVVSHdryfldRV-----ATRILELDRG 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 1490492289 907 TIQR-EGTLKDFQRSEYQLFEHWKTLMNRQDQELEKE 942
Cdd:COG0488 226 KLTLyPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKE 262
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
704-900 |
7.81e-08 |
|
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: 55.45 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 704 IPR-GQLTMIVGQVGCGKSSLLLATLGEMQ----KVSGAVFWNSLPD----SEGEDpsspEQETVADSDVRTRGPVAYAS 774
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKpnlgKFDDPPDWDEILDefrgSELQN----YFTKLLEGDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKPWLLNATVEENITFESPFNKQRYkmVIEACSLQPdidilphgdqtqIGERGI-NLSGGQRQRISVARALYQHTNVVFL 853
Cdd:cd03236 98 LIPKAVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490492289 854 DDPFSALDVHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWI 900
Cdd:cd03236 164 DEPSSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
692-861 |
7.97e-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: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLA---TLGEMQKVSGAVFWNSLPdsegedpsspeqetVADSDVRTRG 768
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYNGIP--------------YKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 PVAYASQK----PWLlnaTVEENITFespfnkqrykmvieACSLQpdidilphGDQTQigeRGInlSGGQRQRISVARAL 844
Cdd:cd03233 84 EIIYVSEEdvhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEAL 133
|
170
....*....|....*..
gi 1490492289 845 YQHTNVVFLDDPFSALD 861
Cdd:cd03233 134 VSRASVLCWDNSTRGLD 150
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1083-1230 |
8.54e-08 |
|
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: 55.57 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1083 SVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP 1162
Cdd:cd18576 57 IYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 1163 ---VFLVALLP-LAVVCYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAF---RYEA-RFQQKLLEY 1230
Cdd:cd18576 137 kltLLMLATVPvVVLVAVLFGRRIRKLSKKVQdELAEAN-----TIVEETLQGIRVVKAFtreDYEIeRYRKALERV 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1364-1557 |
8.87e-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: 54.42 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1364 HVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAKLPLHTLRSR--LSIILQDPVLFSG-TIRFNL 1440
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL----LNLIAGFETPQSGRVLINGVDVTAAPPADrpVSMLFQENNLFAHlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1441 D----PEKKcsdstlweaLEIAQLKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA 1515
Cdd:cd03298 92 GlglsPGLK---------LTAEDRQAIEVALARvGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490492289 1516 TENILQKVVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRGAI 1557
Cdd:cd03298 163 LRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1345-1538 |
8.91e-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: 54.42 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRY--DSSLKPVLKHVNALISPGQKIGICGRTGSGKSsfslaffrmvdmfegriiidgidiaklplhTLrsrL 1422
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS------------------------------TL---L 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SII--LQDPVlfSGTIRFNLDPEKKCSDSTLWE--------------------ALEIAQLKLVVKALPG----------- 1469
Cdd:cd03255 48 NILggLDRPT--SGEVRVDGTDISKLSEKELAAfrrrhigfvfqsfnllpdltALENVELPLLLAGVPKkerreraeell 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 1470 ---GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAH 1538
Cdd:cd03255 126 ervGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTH 199
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1344-1564 |
9.72e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.41 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1344 KIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSlaffRMVD-MFEGRIIIDGIDIAKLPLHT---LR 1419
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLA----KLLNgLLLPEAGTITVGGMVLSEETvwdVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1420 SRLSIILQDP-VLFSGT-----IRFNLDpEKKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1493
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGAtvqddVAFGLE-NIGVPREEMVERVDQA-LRQV------GMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 1494 RAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPE 1564
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1345-1558 |
9.73e-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: 54.30 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPV--LKHVNALISPGQKIGICGRTGSGKSSfslaffrmvdmfegriiidgidiaklplhTLRSRL 1422
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTT-----------------------------TLRMLA 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDP--VLFSGtIRFNLDP-EKK-----CSDS-------TLWEALEI---------AQLKLVVKALPGGLD--AIIT 1476
Cdd:cd03266 53 GLLEPDAgfATVDG-FDVVKEPaEARrrlgfVSDStglydrlTARENLEYfaglyglkgDELTARLEELADRLGmeELLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1477 EGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKR 1554
Cdd:cd03266 132 RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHR 211
|
....
gi 1490492289 1555 GAIL 1558
Cdd:cd03266 212 GRVV 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
830-912 |
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 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
|
....
gi 1490492289 909 QREG 912
Cdd:PRK09493 215 AEDG 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1345-1538 |
1.04e-07 |
|
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: 54.07 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSF--SLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDpvlfsgtirFNLDPE--------------KKCSDStlwEALEIAQ--LKLVvkalpgGLDAIITEGGENFSQGQ 1486
Cdd:cd03262 79 GMVFQQ---------FNLFPHltvlenitlapikvKGMSKA---EAEERALelLEKV------GLADKADAYPAQLSGGQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 1487 RQLFCLARAFVRKTSIFIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAH 1538
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTH 193
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
692-919 |
1.09e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.61 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdsegedpsspeqETVAdsdvrtrgpVA 771
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------------ETVK---------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKPWLL--NATVEENItfeSPFNKQRYKMVIEACsLQpdiDILPHGDQ--TQIGergiNLSGGQRQRISVARALYQH 847
Cdd:COG0488 382 YFDQHQEELdpDKTVLDEL---RDGAPGGTEQEVRGY-LG---RFLFSGDDafKPVG----VLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 848 TNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ-REGTLKDFQR 919
Cdd:COG0488 451 PNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHdryfldRV-----ATRILEFEDGGVReYPGGYDDYLE 519
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
697-889 |
1.19e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsLPDSEgedpsSPEQETVADsDVRTRGPVAYASQk 776
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQ-----FGREASLID-AIGRKGDFKDAVE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 pwLLNAT-VEENITFESPFNkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLDD 855
Cdd:COG2401 118 --LLNAVgLSDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 1490492289 856 PFSALDVHLSdHLMQAGILELLRDDKRTVVLVTH 889
Cdd:COG2401 163 FCSHLDRQTA-KRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1362-1568 |
1.27e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.81 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1362 LKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRS----RLSIILQDpvlfsgtir 1437
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1438 FNLDPEKKCSDSTLWeALEIAQLKLVVKAlPGGLDAIITEGGENF--------SQGQRQLFCLARAFVRKTSIFIMDEAT 1509
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 1510 ASID--MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1359-1570 |
1.44e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.67 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1359 KPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIA------KLPLHTLRSRLSIILQDPVLF 1432
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1433 SG-TIRFNLD-PEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1510
Cdd:PRK14246 103 PHlSIYDNIAyPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 1511 SIDMATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILE-------FDKPETLLNQK 1570
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKNELTEK 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
694-920 |
1.74e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDPSSPEQETVADSDVRTRGP-VAY 772
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRGAdMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWL-LNA--TVEENITfESPFNKQ---RYKMVIEACSLQPDIDIlPHGdQTQIGERGINLSGGQRQRISVARALYQ 846
Cdd:PRK10261 109 IFQEPMTsLNPvfTVGEQIA-ESIRLHQgasREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 847 HTNVVFLDDPFSALDVhlsdhLMQAGILELLR----DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:PRK10261 186 RPAVLIADEPTTALDV-----TIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1345-1568 |
1.82e-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: 55.58 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFsLAFFRMVDMFEGRIIIDGIDIAKLP---------- 1414
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEPTSGRIIYHVALCEkcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1415 --------------------------LHTLRSRLSIILQDPvlfsgtirFNLDPEKKCSDSTLwEALEIAQLKlVVKALP 1468
Cdd:TIGR03269 78 vgepcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRT--------FALYGDDTVLDNVL-EALEEIGYE-GKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1469 GGLDAI--------ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH 1538
Cdd:TIGR03269 148 RAVDLIemvqlshrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSH 227
|
250 260 270
....*....|....*....|....*....|.
gi 1490492289 1539 RVHTILS-ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:TIGR03269 228 WPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
697-906 |
2.12e-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: 53.44 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPdsegedpsspeqetvADSDVRTRgpVAYASQK 776
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP---------------LDIAARNR--IGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWL-LNATVEENITFESpfnkQRYKMVIEACSLQPD-----IDILPHGDQtQIGErginLSGGQRQRISVARALYQHTNV 850
Cdd:cd03269 79 RGLyPKMKVIDQLVYLA----QLKGLKKEEARRRIDewlerLELSEYANK-RVEE----LSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 851 VFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 906
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDV-IRE-LARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
694-892 |
2.59e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 53.49 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSSPEQETVAdsdvRTRGPVAYA 773
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA------GLVPWKRRKKFLR----RIGVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQKPWLLNA----TVEENITFESPFnkqRYKMVIEACSlqpdiDILPHGDQTQIGERgiNLSGGQRQRISVARALYQHTN 849
Cdd:cd03267 104 TQLWWDLPVidsfYLLAAIYDLPPA---RFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490492289 850 VVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQ 892
Cdd:cd03267 174 ILFLDEPTIGLDVV-AQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
692-906 |
2.78e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLlatlgemqKV----------SGAVFWnslpdsEGEdpssPEQ-ETVA 760
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLM--------KVlsgvyphgtyEGEIIF------EGE----ELQaSNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 761 DSDvrtRGPVAYASQKPWLL-NATVEENItF---E-SPFNKQRY-KMVIEACSL--QPDIDILPHgdqTQIGergiNLSG 832
Cdd:PRK13549 78 DTE---RAGIAIIHQELALVkELSVLENI-FlgnEiTPGGIMDYdAMYLRAQKLlaQLKLDINPA---TPVG----NLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLmqagiLELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 906
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVL-----LDIIRDLKAhgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1345-1559 |
2.80e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.13 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlKPVLKHVNALISPGQKIGICGRTGSGKSSF---------------SLAFFRMVDMfegriiidgiD 1409
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLlkllygeerptsgqvLVNGQDLSRL----------K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1410 IAKLPLhtLRSRLSIILQDpvlfsgtirFNLDPEKkcsdsTLWE----ALEIAQ-------------LKLV-----VKAL 1467
Cdd:COG2884 71 RREIPY--LRRRIGVVFQD---------FRLLPDR-----TVYEnvalPLRVTGksrkeirrrvrevLDLVglsdkAKAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1468 PGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTI 1543
Cdd:COG2884 135 PHEL-----------SGGEQQRVAIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELV 200
|
250
....*....|....*..
gi 1490492289 1544 LSADL-VMVLKRGAILE 1559
Cdd:COG2884 201 DRMPKrVLELEDGRLVR 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
684-882 |
3.98e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 684 GGFFTWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWN-----SLPDSEGEDPSSPEQET 758
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridTLSPGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 759 VAD--SDVRTRGPVAYASQKPWLLNATVEENITfespfnKQRYKMVIEACSLQPDIDI-LPHgdqtqigergiNLSGGQR 835
Cdd:PRK10261 407 FQDpyASLDPRQTVGDSIMEPLRVHGLLPGKAA------AARVAWLLERVGLLPEHAWrYPH-----------EFSGGQR 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490492289 836 QRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR 882
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSI-----RGQIINLLLDLQR 511
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
692-912 |
4.38e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.14 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 692 DGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGemqkvsgavfwnsLPDSEgedpsspeqetvadsdvRTRGPVA 771
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-------------HPKYE-----------------VTEGEIL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YASQKpwLLNATVEEN------ITFESPfnkqrykMVIEACSLqpdIDILphgdqtqigeRGIN--LSGGQRQRISVARA 843
Cdd:cd03217 61 FKGED--ITDLPPEERarlgifLAFQYP-------PEIPGVKN---ADFL----------RYVNegFSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 844 LYQHTNVVFLDDPFSALDVhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADWIIAMKDGTIQREG 912
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSG 187
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1344-1568 |
4.88e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.86 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1344 KIQIQNLSVRYDSSLkpVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIdgidiAKLPLH------- 1416
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVE-----GKVTFHgknlyap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1417 -----TLRSRLSIILQDPVLFSGTI-------------RFNLDP--EKKCSDSTLWEALEiAQLKlvvkalpggldaiit 1476
Cdd:PRK14243 83 dvdpvEVRRRIGMVFQKPNPFPKSIydniaygaringyKGDMDElvERSLRQAALWDEVK-DKLK--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1477 EGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVHTI---LSAD 1547
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMtafFNVE 226
|
250 260
....*....|....*....|..
gi 1490492289 1548 LVMVLKR-GAILEFDKPETLLN 1568
Cdd:PRK14243 227 LTEGGGRyGYLVEFDRTEKIFN 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
697-891 |
4.94e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSL--LLAtlGEMQKVSGAVFWNslpdseGE--DPSSPeqetvadSDVRTRGpVAY 772
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLmkILY--GLYQPDSGEILID------GKpvRIRSP-------RDAIALG-IGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWLLNA-TVEENI------TFESPFNKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISVARALY 845
Cdd:COG3845 85 VHQHFMLVPNlTVAENIvlglepTKGGRLDRKAARARIRELSERYGLDVDPD---AKVED----LSVGEQQRVEILKALY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1490492289 846 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL 891
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKL 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
688-906 |
5.94e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.06 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 688 TWTPDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQKVSGAVFWNslpdsegedpsspEQETVADS--D 763
Cdd:TIGR02633 8 VKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWS-------------GSPLKASNirD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 764 VRTRGPVAYASQKPWLLNATVEENI----TFESPFNKQRYKMVIEACS---LQPDIDILPhgDQTQIGERGinlsGGQRQ 836
Cdd:TIGR02633 75 TERAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKnllRELQLDADN--VTRPVGDYG----GGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 906
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTEKETE-----ILLDIIRDLKAhgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
694-913 |
7.62e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSlPDSEGEDPSSPEQETVAdsdVRTRGPVAYA 773
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG-KDITDWQTAKIMREAVA---IVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQkpwllnaTVEENITFESPF-NKQRYKMVIEACslqpdIDILPHGDQTQIgERGINLSGGQRQRISVARALYQHTNVVF 852
Cdd:PRK11614 94 RM-------TVEENLAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 853 LDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFD--TIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
830-913 |
8.38e-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: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTI 908
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
....*
gi 1490492289 909 QREGT 913
Cdd:PRK11650 214 EQIGT 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
831-894 |
9.31e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 9.31e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 831 SGGQRQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRtvvlvTHKLQYL 894
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSL-----DKTVQAQILALLKSLQQ-----KHQLAYL 480
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
697-922 |
9.53e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpDSEGEDPSSpeqETVADSDVRTRGPVAYASQK 776
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI------TIAGYHITP---ETGNKNLKKLRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 P--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALYQ 846
Cdd:PRK13641 94 PeaQLFENTVLKDVEF-GPKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQagileLLRDDKR---TVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRSE 921
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQ-----LFKDYQKaghTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKEiFSDKE 237
|
.
gi 1490492289 922 Y 922
Cdd:PRK13641 238 W 238
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1345-1573 |
9.95e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.04 E-value: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDS-SLKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVD-MFEGRIIIDGIDIAKLPLHT---LR 1419
Cdd:PRK13650 5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDgLLEAESGQIIIDGDLLTEENvwdIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1420 SRLSIILQDP-VLFSGT-----IRFNLDpEKKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1493
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGAtveddVAFGLE-NKGIPHEEMKERVNEA-LELV------GMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1494 RAFVRKTSIFIMDEATASID--------MATENILQKVVMtafadrTVVTIAHRVHTILSADLVMVLKRGAILEFDKPET 1565
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQM------TVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
....*...
gi 1490492289 1566 LLNQKDSI 1573
Cdd:PRK13650 227 LFSRGNDL 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1347-1388 |
1.08e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.14 E-value: 1.08e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1490492289 1347 IQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSF 1388
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL 40
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1345-1570 |
1.14e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.05 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKpVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDP--VLFSGTI-------RFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARA 1495
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1496 FVRKTSIFIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLNQ 1569
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
.
gi 1490492289 1570 K 1570
Cdd:PRK13647 229 D 229
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
706-889 |
1.43e-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: 49.68 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 706 RGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDPSSPEQETvadsdvrtrgpvayasqkpwllnatve 785
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 786 enitfespfnkqrykmvieacslqpdidilphgdqtqIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLS 865
Cdd:smart00382 54 -------------------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
170 180
....*....|....*....|....*...
gi 1490492289 866 DHLMQAGILELL----RDDKRTVVLVTH 889
Cdd:smart00382 97 ALLLLLEELRLLlllkSEKNLTVILTTN 124
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1109-1226 |
1.70e-06 |
|
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: 51.64 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1109 PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-LVALL--PLAVVC-YFI----QK 1180
Cdd:cd18547 92 PLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtLIVLVtvPLSLLVtKFIakrsQK 171
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1490492289 1181 YFRVASRDLQQLDdttqlpllSHFAETVEGLTTIRAFRYEARFQQK 1226
Cdd:cd18547 172 YFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEE 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
693-921 |
1.76e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLllatlgeMQKVSGAVfwnsLPDSeGEdpsspeqetvadsdVRTRG-PVA 771
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTL-------MKIIAGIV----PPDS-GT--------------LEIGGnPCA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 772 YAS-------------QKPWLL-NATVEENITFESPFNKQRYKMVIE-----ACSLQPDIdilphgdqtQIGergiNLSG 832
Cdd:PRK15439 77 RLTpakahqlgiylvpQEPLLFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDS---------SAG----SLEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 911
Cdd:PRK15439 144 ADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALS 221
|
250
....*....|
gi 1490492289 912 GTLKDFQRSE 921
Cdd:PRK15439 222 GKTADLSTDD 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1345-1567 |
2.46e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.86 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYD-SSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 1423
Cdd:PRK13642 5 LEVENLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1424 IILQDP------VLFSGTIRFNLDPEKKCSDSTLweaLEIAQLKLVVKALPggldaIITEGGENFSQGQRQLFCLARAFV 1497
Cdd:PRK13642 85 MVFQNPdnqfvgATVEDDVAFGMENQGIPREEMI---KRVDEALLAVNMLD-----FKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 1498 RKTSIFIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLL 1567
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
645-891 |
2.46e-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: 52.71 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 645 KVVNRKRPAREEVRDLLGP-------LQRLTPsmdGDADNFCVQIIGGFFTwtPDGIPTLSNISIRIPRGQLTMIVGQVG 717
Cdd:TIGR01257 892 RALEKTEPLTEEMEDPEHPegindsfFERELP---GLVPGVCVKNLVKIFE--PSGRPAVDRLNITFYENQITAFLGHNG 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 718 CGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPsspeqETVADSdvrTRGPVAYASQKPWLLN-ATVEENITFESPFNK 796
Cdd:TIGR01257 967 AGKTTTLSILTGLLPPTSGTVLVG------GKDI-----ETNLDA---VRQSLGMCPQHNILFHhLTVAEHILFYAQLKG 1032
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 797 QRYkmviEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILEL 876
Cdd:TIGR01257 1033 RSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY-----SRRSIWDL 1103
|
250
....*....|....*..
gi 1490492289 877 LRDDK--RTVVLVTHKL 891
Cdd:TIGR01257 1104 LLKYRsgRTIIMSTHHM 1120
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
830-906 |
2.52e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 904
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 1490492289 905 DG 906
Cdd:PRK15134 232 NG 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1345-1568 |
3.20e-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: 49.74 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlkPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTlRSRLSI 1424
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 IL--QDPVLFSG-TIRfnldpekkcsdstlwEALEIAQLKLVVKALPGGLDAII-----------TEGGeNFSQGQRQLF 1490
Cdd:cd03224 78 GYvpEGRRIFPElTVE---------------ENLLLGAYARRRAKRKARLERVYelfprlkerrkQLAG-TLSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1491 CLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1345-1538 |
3.37e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 50.16 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------- 1417
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSprtdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1418 LRSRLSIILQDPVLFSGTI--------RFNLDPEKKCSDSTLWEALEIAQLKLVVKAlpggldaIITEGGENFSQGQRQL 1489
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490492289 1490 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1538
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
822-913 |
4.68e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.55 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 822 QIGERGINLSGGQRQRISVARALYQ---HTNVVFLDDPFSALdvHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPH 896
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKT 897
|
90 100
....*....|....*....|...
gi 1490492289 897 ADWII------AMKDGTIQREGT 913
Cdd:TIGR00630 898 ADYIIdlgpegGDGGGTVVASGT 920
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1359-1540 |
4.96e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.09 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1359 KPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHT------LRSRLSIILQDPVLF 1432
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyrdvleFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1433 SGTIRFN---------LDPEKkcsdstlwEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 1503
Cdd:PRK14271 114 PMSIMDNvlagvrahkLVPRK--------EFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490492289 1504 IMDEATASIDMATENILQKVVMTaFADR-TVVTIAHRV 1540
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRS-LADRlTVIIVTHNL 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1345-1578 |
5.32e-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: 49.64 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlkpVLKHVNALISPGQKIGICGRTGSGKSSF--SLAFFRMVD----MFEGRIIIdgidiaklPLHTL 1418
Cdd:cd03299 1 LKVENLSKDWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLleTIAGFIKPDsgkiLLNGKDIT--------NLPPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1419 RSRLSIILQDPVLFSG-----TIRFNLDPEKKCSDSTLWEALEIAQLKlvvkalpgGLDAIITEGGENFSQGQRQLFCLA 1493
Cdd:cd03299 70 KRDISYVPQNYALFPHmtvykNIAYGLKKRKVDKKEIERKVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1494 RAFVRKTSIFIMDEATASIDMAT-ENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLNQ 1569
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
250
....*....|
gi 1490492289 1570 -KDSIFASFV 1578
Cdd:cd03299 221 pKNEFVAEFL 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1343-1578 |
6.01e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 50.46 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1343 GKIQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSfslaffrmvdmfegriiidgidiaklplhTLRsrl 1422
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKST-----------------------------LLR--- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 sII--LQDPVlfSGTIRFN------LDPEK-----------------------------KCS----DSTLWEALEIAQLK 1461
Cdd:COG3839 48 -MIagLEDPT--SGEILIGgrdvtdLPPKDrniamvfqsyalyphmtvyeniafplklrKVPkaeiDRRVREAAELLGLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1462 LVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVVMTafadrTV 1533
Cdd:COG3839 125 DLLDRKPKQL-----------SGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TI 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 1534 -VTiahrvH------TIlsADLVMVLKRGAILEFDKPETLLNQKDSIF-ASFV 1578
Cdd:COG3839 189 yVT-----HdqveamTL--ADRIAVMNDGRIQQVGTPEELYDRPANLFvAGFI 234
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1059-1246 |
6.67e-06 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 49.73 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1059 LDQSVYAMVFTVLCSLGIVLCL------VTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTI 1132
Cdd:cd18554 37 LDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1133 DQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVA---LLPLAVVC-YFIQKYFRVASRDLQQLDDTTQlpllSHFAETV 1208
Cdd:cd18554 117 KDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFYILAvKYFFGRLRKLTKERSQALAEVQ----GFLHERI 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490492289 1209 EGLTTIRAFRYEARFQQkllEYTDSNNiasLFLTAANR 1246
Cdd:cd18554 193 QGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
699-916 |
7.13e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEGEDPSSPEQETVADSDVRTR-GPVAYASQkp 777
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSlNPRQRISQ-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 778 wLLNATVEENITFESPFNKQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQRQRISVARALYQHTNVVFLDDP 856
Cdd:PRK15112 109 -ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 857 FSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:PRK15112 177 LASLDMSMRSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1345-1552 |
1.18e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.32 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYD------------SSLKPVlKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAK 1412
Cdd:PRK15079 9 LEVADLKVHFDikdgkqwfwqppKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1413 L---PLHTLRSRLSIILQDPvLFSgtirfnLDPEKKCSD------STLWEALEIAQLKLVVKAL---PGGLDAIITEGGE 1480
Cdd:PRK15079 88 MkddEWRAVRSDIQMIFQDP-LAS------LNPRMTIGEiiaeplRTYHPKLSRQEVKDRVKAMmlkVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1481 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKV--------VMTAFaDRTVVT-IAHRVhtilsad 1547
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNLLQQLqremglslIFIAH-DLAVVKhISDRV------- 232
|
....*
gi 1490492289 1548 LVMVL 1552
Cdd:PRK15079 233 LVMYL 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1453-1579 |
1.23e-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: 48.79 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1453 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-- 1530
Cdd:cd03294 143 EALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElq 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 1531 RTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLNQ-KDSIFASFVR 1579
Cdd:cd03294 212 KTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNpANDYVREFFR 262
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1058-1243 |
1.26e-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: 49.02 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1058 ALDQSVYAMVFTVL--CSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILA--------PMRFFETTPLGSILNRFSS 1127
Cdd:cd18546 25 GIDSGVRAGDLGVLllAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRvfahlqrlSLDFHERETSGRIMTRMTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1128 DCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFiqkyFRVASRDLQQLDDTTQLPLLSH 1203
Cdd:cd18546 105 DIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRW----FRRRSSRAYRRARERIAAVNAD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490492289 1204 FAETVEGLTTIRAFRYEARFQQKLLEYTDSN---NIASLFLTA 1243
Cdd:cd18546 181 LQETLAGIRVVQAFRRERRNAERFAELSDDYrdaRLRAQRLVA 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
697-889 |
1.39e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.66 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQK---VSGAVFWNslpdseGEDPSSPEQETVAdsdvrtrgpvAYA 773
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLN------GMPIDAKEMRAIS----------AYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQKPWLLNA-TVEENITFESPF----------NKQRYKMVIEACSLQPDIDILphgdqTQIGERGINLSGGQRQRISVAR 842
Cdd:TIGR00955 105 QQDDLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCANTR-----IGVPGRVKGLSGGERKRLAFAS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490492289 843 ALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTH 889
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
697-861 |
1.44e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ----KVSGAVFWNSLPDSEGEDpsspeqetvadsdvRTRGPVAY 772
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKK--------------HYRGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQK----PWLlnaTVEENITF----ESPFNkqRYKMVIEACSLQPDIDI------LPHGDQTQIGE---RGInlSGGQR 835
Cdd:TIGR00956 143 NAETdvhfPHL---TVGETLDFaarcKTPQN--RPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRGV--SGGER 215
|
170 180
....*....|....*....|....*.
gi 1490492289 836 QRISVARALYQHTNVVFLDDPFSALD 861
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
693-916 |
1.53e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLpDSEGEDPSSPEQETVAdsdvrtrgpVAY 772
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-NYNKLDHKLAAQLGIG---------IIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 asQKPWLLNA-TVEENI--------------TFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQR 837
Cdd:PRK09700 87 --QELSVIDElTVLENLyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 838 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSD 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
831-891 |
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 1490492289 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTHKL 891
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
699-889 |
1.55e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.65 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnSLPDsegedpsspeqETVADSDVRTRGPVAYASQKPW 778
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI---SLCG-----------EPVPSRARHARQRVGVVPQFDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 779 L-LNATVEENI-TFESPFN------KQRYKMVIEACSLQPDIDilphgdqTQIGErginLSGGQRQRISVARALYQHTNV 850
Cdd:PRK13537 91 LdPDFTVRENLlVFGRYFGlsaaaaRALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVNDPDV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1490492289 851 VFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 889
Cdd:PRK13537 160 LVLDEPTTGLDPQ-ARHLMWERLRSLLARGK-TILLTTH 196
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1453-1578 |
1.57e-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: 49.03 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1453 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVV 1524
Cdd:TIGR01187 83 EALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkTIQEQLG 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 1525 MtafadrTVVTIAH-RVHTILSADLVMVLKRGAILEFDKPETLLNQKDSIF-ASFV 1578
Cdd:TIGR01187 152 I------TFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1345-1388 |
1.90e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.29 E-value: 1.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSF 1388
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
825-921 |
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 1490492289 825 ERGIN-LSGGQRQRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWII 901
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGL--HQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|....*.
gi 1490492289 902 AM------KDGTIQREGTLKDFQRSE 921
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILANP 586
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
697-893 |
2.56e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdsegedpsspeqetvadsDVRTRGPVAYASQK 776
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------------------HCGTKLEVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLLNA--TVEENITfESpfnKQ------RYKMVIEacSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQHT 848
Cdd:PRK11147 391 RAELDPekTVMDNLA-EG---KQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490492289 849 NVVFLDDPFSALDVHLSDHLMqagilELLRDDKRTVVLVTHKLQY 893
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLE-----ELLDSYQGTVLLVSHDRQF 499
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1063-1303 |
2.59e-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: 47.85 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1063 VYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC 1142
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLIN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1143 LSRSTLLCVSALTVISYVTPVF-LVAL--LP-LAVVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFR 1218
Cdd:cd18545 121 LIPDLLTLVGIVIIMFSLNVRLaLVTLavLPlLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSFA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1219 YE----ARFQQKLLEYTDSNNIASLFLTAANRWLEVrMEYIGACVVLIAAATSIsnsLHRELSAGLVGLGLTYA------ 1288
Cdd:cd18545 197 REdeneEIFDELNRENRKANMRAVRLNALFWPLVEL-ISALGTALVYWYGGKLV---LGGAITVGVLVAFIGYVgrfwqp 272
|
250
....*....|....*.
gi 1490492289 1289 -LMVSNYLNWMVRNLA 1303
Cdd:cd18545 273 iRNLSNFYNQLQSAMA 288
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1109-1240 |
3.95e-05 |
|
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: 47.41 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1109 PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-LVALLPL---AVVCYFIQKYFRV 1184
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLtLIALLPLpllALLVYRLGKKIHK 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 1185 ASRDLQQ----LDDTTQlpllshfaETVEGLTTIRAF----RYEARFQQKLLEYTDSNN----IASLF 1240
Cdd:cd18541 167 RFRKVQEafsdLSDRVQ--------ESFSGIRVIKAFvqeeAEIERFDKLNEEYVEKNLrlarVDALF 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1345-1569 |
4.00e-05 |
|
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: 48.26 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPVLKHVNAL---ISPGQKIGICGRTGSGKSSFS--LA----------FFRM----VDMFEgriii 1405
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSkiIAgvleptsgevNVRVgdewVDMTK----- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1406 dgidiaklPLHTLRSR----LSIILQDPVLFsgtirfnldPEKKCSDStLWEAL------EIAQLKLVVKALPGGLD--- 1472
Cdd:TIGR03269 355 --------PGPDGRGRakryIGILHQEYDLY---------PHRTVLDN-LTEAIglelpdELARMKAVITLKMVGFDeek 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1473 --AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-AD 1547
Cdd:TIGR03269 417 aeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCD 496
|
250 260
....*....|....*....|..
gi 1490492289 1548 LVMVLKRGAILEFDKPETLLNQ 1569
Cdd:TIGR03269 497 RAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
828-889 |
4.18e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 4.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 828 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTH 889
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE-----GILRLFEEFNRvgvTVLMATH 195
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1345-1578 |
4.33e-05 |
|
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: 46.85 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAK----LPLHtlRS 1420
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFETPTSGEILLDGKditnLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1421 RLSIILQDPVLF-----SGTIRFNLDpEKKCSDSTLWEALEiAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARA 1495
Cdd:cd03300 73 PVNTVFQNYALFphltvFENIAFGLR-LKKLPKAEIKERVA-EALDLV------QLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1496 FVRKTSIFIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILSADLVMVLKRGAILEFDKPETLLNQKD 1571
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
....*...
gi 1490492289 1572 SIF-ASFV 1578
Cdd:cd03300 224 NRFvADFI 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
697-861 |
4.66e-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: 46.38 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGEDPSS-PEQEtvadsdvRTRGPVAYASQ 775
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD------GQDITKlPMHK-------RARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 776 KPWLL-NATVEENI--TFESpFNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVF 852
Cdd:cd03218 83 EASIFrKLTVEENIlaVLEI-RGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLL 156
|
....*....
gi 1490492289 853 LDDPFSALD 861
Cdd:cd03218 157 LDEPFAGVD 165
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
691-900 |
5.00e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.01 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQkvsgavfwnslpDSEGEDPSSP-------EQETVADSD 763
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------------DFNGEARPQPgikvgylPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 764 VRTRGPVAYA-SQKPWLLNATVEENITFESP---FNKQRYKM-----VIEAC---SLQPDIDI------LPHGDQtQIGe 825
Cdd:TIGR03719 83 KTVRENVEEGvAEIKDALDRFNEISAKYAEPdadFDKLAAEQaelqeIIDAAdawDLDSQLEIamdalrCPPWDA-DVT- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 826 rgiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWI 900
Cdd:TIGR03719 161 ---KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPGTVVAVTHDRYFLDNvAGWI 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1345-1577 |
6.48e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 47.14 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlkPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDPVL---FSG-----------TIRFnlDPEKKCSDSTLWEALEiaqlklvvkalPGGLDAIITEGGENFSQGQRQLF 1490
Cdd:PRK09536 82 VPQDTSLsfeFDVrqvvemgrtphRSRF--DTWTETDRAAVERAME-----------RTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1491 CLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLSA---DLVMVLKRGAILEFDKPETL 1566
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPPADV 226
|
250
....*....|.
gi 1490492289 1567 LNqKDSIFASF 1577
Cdd:PRK09536 227 LT-ADTLRAAF 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1345-1566 |
6.73e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYdsSLKPVLKHVNALISPGQKIGICGRTGSGKSSFS--LAFFRMVDMFEGRIIIDGIDIAKlPLHTLRSRL 1422
Cdd:PRK15439 12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLFSG-TIRFNL--------DPEKKCSDstLWEALEiAQLKLVVKAlpGGLDAiiteggenfsqGQRQLFCLA 1493
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENIlfglpkrqASMQKMKQ--LLAALG-CQLDLDSSA--GSLEV-----------ADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490492289 1494 RAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETL 1566
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
700-908 |
7.09e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 700 ISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsLPDSEGEDPSSPEQETVAD-----SDVRTRGPVAYAS 774
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV----YLDGKPIDIRSPRDAIRAGimlcpEDRKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 qkpwllnatVEENITFESPFNKQRYKMVI----EACSLQPDIDIL----PHGDQtQIGergiNLSGGQRQRISVARALYQ 846
Cdd:PRK11288 348 ---------VADNINISARRHHLRAGCLInnrwEAENADRFIRSLniktPSREQ-LIM----NLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 847 HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 908
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYN--VIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1345-1559 |
7.80e-05 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 45.80 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDS--SLKPVLKHVNALISPGQKIGICGRTGSGKSSF----------------------------SLAFFR 1394
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnilggldrptsgevlidgqdisslserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1395 mvdmfegriiidgidiaklplhtlRSRLSIILQDpvlfsgtirFNLDPE-----------------KKCSDSTLWEALEI 1457
Cdd:COG1136 85 ------------------------RRHIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLER 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1458 AQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFAD---RTV 1533
Cdd:COG1136 132 VGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTI 198
|
250 260
....*....|....*....|....*.
gi 1490492289 1534 VTIAHRVHTILSADLVMVLKRGAILE 1559
Cdd:COG1136 199 VMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
820-912 |
7.98e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 820 QTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD--DKRTVVLVTHKL-QYLPH 896
Cdd:PRK14271 154 KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-----IEEFIRSlaDRLTVIIVTHNLaQAARI 228
|
90
....*....|....*.
gi 1490492289 897 ADWIIAMKDGTIQREG 912
Cdd:PRK14271 229 SDRAALFFDGRLVEEG 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
699-914 |
8.31e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNS--LPDSEGEDPSSPEQETVAdsdvrtrgpvaYASQK 776
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvLFDAEKGICLPPEKRRIG-----------YVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 777 PWLL-NATVEENITFE-SPFNKQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQRQRISVARALYQHTNVVFLD 854
Cdd:PRK11144 85 ARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 855 DPFSALDVHLSDHLMQagILELLRDDKRTVVL-VTHKLQYLPH-ADWIIAMKDGTIQREGTL 914
Cdd:PRK11144 154 EPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPL 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1345-1572 |
1.13e-04 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 45.52 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslkpVLKHVNALISPGQKIGICGRTGSGKSSFS--LAFFRMVD---MFEGRIIIDGIDIAKLPLhtlr 1419
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLnlIAGFLPPDsgrILWNGQDLTALPPAERPV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1420 srlSIILQDPVLFSG-TIRFN----LDPEKKCSD---STLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1491
Cdd:COG3840 74 ---SMLFQENNLFPHlTVAQNiglgLRPGLKLTAeqrAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1492 LARAFVRKTSIFIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
....
gi 1490492289 1569 QKDS 1572
Cdd:COG3840 220 GEPP 223
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1061-1233 |
1.23e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 45.89 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1061 QSVYAMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1140
Cdd:cd18551 37 GLLALLVALFL--LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1141 ECLSRSTLLCVSALTVISYVTPV-FLVAL--LPLAVVC-YFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1215
Cdd:cd18551 115 PQLVTGVLTVVGAVVLMFLLDWVlTLVTLavVPLAFLIiLPLGRRIRKASKRAQD-----ALGELSAALErALSAIRTVK 189
|
170
....*....|....*...
gi 1490492289 1216 AFRYEARFQQKLLEYTDS 1233
Cdd:cd18551 190 ASNAEERETKRGGEAAER 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
693-892 |
1.28e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 45.27 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnslpdsegedpsspeqeTVADSDV-------R 765
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-------------------IIDDEDIsllplhaR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 TRGPVAYASQKPWL---------LNATVE--ENITFESpfNKQRYKMVIEACSLQPDIDILphgdqtqigerGINLSGGQ 834
Cdd:PRK10895 76 ARRGIGYLPQEASIfrrlsvydnLMAVLQirDDLSAEQ--REDRANELMEEFHIEHLRDSM-----------GQSLSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 835 RQRISVARALYQHTNVVFLDDPFSALD-VHLSDhlmQAGILELLRDDKRTVVLVTHKLQ 892
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
828-891 |
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 1490492289 828 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL 891
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA-IRRLSEEGKKTALVVEHDL 132
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
830-889 |
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 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 889
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
709-889 |
3.17e-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: 43.80 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 709 LTMIVGQVGCGKSSLLLAtlgemqkVSGAVFwnslpdseGEDPSSPEQEtvADSDVRtrgpvayasqkpwllnATVEE-- 786
Cdd:cd03279 30 LFLICGPTGAGKSTILDA-------ITYALY--------GKTPRYGRQE--NLRSVF----------------APGEDta 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 787 NITFESPFNKQRYKmVIEACSLQPD----IDILPHGDQTQIGERGI-NLSGGQRQRISVARAL------YQHTNVV---- 851
Cdd:cd03279 77 EVSFTFQLGGKKYR-VERSRGLDYDqftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevlQNRGGARleal 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490492289 852 FLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTH 889
Cdd:cd03279 156 FIDEGFGTLDPEALEAVATA--LELIRTENRMVGVISH 191
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
783-861 |
3.19e-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: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 783 TVEENI-----TFESPFNKQRYKMVieacSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVFLDDPF 857
Cdd:COG1137 94 TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
....
gi 1490492289 858 SALD 861
Cdd:COG1137 165 AGVD 168
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1335-1578 |
4.11e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 44.44 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1335 IPKNWPDQGK-----IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGID 1409
Cdd:PRK11607 5 IPRPQAKTRKaltplLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1410 IAKLPLHT--LRSRLSIILQDPVLF-----SGTIRFNLDPEKKCSD---STLWEALEIAQLKLVVKALPGGLdaiitegg 1479
Cdd:PRK11607 79 DGVDLSHVppYQRPINMMFQSYALFphmtvEQNIAFGLKQDKLPKAeiaSRVNEMLGLVHMQEFAKRKPHQL-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1480 enfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKV----VMTAFADRTVVTIAHRvhtilsad 1547
Cdd:PRK11607 151 ---SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrMQLEvvDILERVgvtcVMVTHDQEEAMTMAGR-------- 219
|
250 260 270
....*....|....*....|....*....|..
gi 1490492289 1548 lVMVLKRGAILEFDKPETLLNQKDSIF-ASFV 1578
Cdd:PRK11607 220 -IAIMNRGKFVQIGEPEEIYEHPTTRYsAEFI 250
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
830-904 |
4.15e-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: 4.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 830 LSGGQRQRISVARAL----YQHTNVVFLDDPFSALDvhLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMK 904
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLD--PRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
694-912 |
4.35e-04 |
|
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: 44.79 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 694 IPTLSNISIRIPRGQLTMIVGQVGCGKSSLllatlgemQKVSGAVfwnsLPDSEGEDPSSPEQETVadsDVRTRGPVAYA 773
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTL--------SKIIAGV----LEPTSGEVNVRVGDEWV---DMTKPGPDGRG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 774 SQKPWL----------LNATVEENIT----FESPFNKQRYKMVI----------EACSLqpdIDILPHgdqtqigergiN 829
Cdd:TIGR03269 362 RAKRYIgilhqeydlyPHRTVLDNLTeaigLELPDELARMKAVItlkmvgfdeeKAEEI---LDKYPD-----------E 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALD----VHLSDHLMQAGIlELlrddKRTVVLVTHKLQY-LPHADWIIAMK 904
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKARE-EM----EQTFIIVSHDMDFvLDVCDRAALMR 502
|
....*...
gi 1490492289 905 DGTIQREG 912
Cdd:TIGR03269 503 DGKIVKIG 510
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1371-1564 |
4.48e-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: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1371 PGQKIGICGRTGSGKSSFSLAFFRMVDmfegriiidgidiaklplhtlRSRLSIILQDPVLFSGTIRFNLdpekkcsdst 1450
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG---------------------PPGGGVIYIDGEDILEEVLDQL---------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1451 lwealeiaqlklvvkalpggLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAF-- 1528
Cdd:smart00382 50 --------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1490492289 1529 -----ADRTVVTIAHRVHTILSADLVMVLKRgaILEFDKPE 1564
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRRRFDR--RIVLLLIL 148
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
693-906 |
4.56e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 693 GIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnslpdsEGEdpsspeqetvadsdvrtrgPVAY 772
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF------QGK-------------------EIDF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 773 ASQKPWLLNA--------------TVEENITF-----ESPFNKQRyKMVIEACSL--QPDIDILPHgdqtqigERGINLS 831
Cdd:PRK10982 65 KSSKEALENGismvhqelnlvlqrSVMDNMWLgryptKGMFVDQD-KMYRDTKAIfdELDIDIDPR-------AKVATLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 832 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDG 906
Cdd:PRK10982 137 VSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1369-1515 |
4.63e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.42 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1369 ISPGQKIGICGRTGSGKSSF-SL-AFFRMVD---MFEGRIIIDGIDIAKLPLhtlrsrlSIILQDPVLFSG-TIRFN--- 1439
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLlNLiAGFLTPAsgsLTLNGQDHTTTPPSRRPV-------SMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1440 -LDPEKKCSDSTLWEALEIAQ---LKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA 1515
Cdd:PRK10771 95 gLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1345-1571 |
4.74e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.88 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSL---KPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFR---------MVDMFEGRIIidgidiaK 1412
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkptsgkiIIDGVDITDK-------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1413 LPLHTLRSRLSIILQDP--VLFSGT----IRF---NLDPEKKCSDSTLWEALEIAQLKlvvkalpggLDAIITEGGENFS 1483
Cdd:PRK13637 76 VKLSDIRKKVGLVFQYPeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1484 QGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEF 1560
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQ 226
|
250
....*....|.
gi 1490492289 1561 DKPETLLNQKD 1571
Cdd:PRK13637 227 GTPREVFKEVE 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
699-889 |
5.22e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 699 NISIRIPRGQLTMIVGQVGCGKSSlllaTlgeMQKVSGAvfwnsLPDSEGE--------DPSspeqetvadsDVRTRGPV 770
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKST----T---MKMLTGL-----LPASEGEawlfgqpvDAG----------DIATRRRV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 771 AYASQkpwllnA-------TVEENIT-----FESPFNK--QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 836
Cdd:NF033858 342 GYMSQ------AfslygelTVRQNLElharlFHLPAAEiaARVAEMLERFDLADVADALPD-----------SLPLGIRQ 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTH 889
Cdd:NF033858 405 RLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL-LIELSREDGVTIFISTH 456
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1362-1571 |
5.27e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 43.66 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1362 LKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMV----DMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGT 1435
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpssGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1436 IRFNLDPEKKCSDSTLWEALEIAqLKLVVKAlpGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-M 1514
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKA-LKWLKKV--GLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 1515 ATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLNQKD 1571
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
697-863 |
5.38e-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: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnSLPDS----------EGEDPSSPEQETVAD-SDVR 765
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI---EIGETvklayvdqsrDALDPNKTVWEEISGgLDII 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 766 TRGPV-----AYASQkpwllnatveenitfespFNkqrYKmvieacslqpdidilpHGDQTQ-IGErginLSGGQRQRIS 839
Cdd:TIGR03719 415 KLGKReipsrAYVGR------------------FN---FK----------------GSDQQKkVGQ----LSGGERNRVH 453
|
170 180
....*....|....*....|....
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVH 863
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1062-1181 |
5.39e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 44.00 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1062 SVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTID----QHIP 1137
Cdd:cd18577 47 NKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQdgigEKLG 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 1138 STLECLSrstlLCVSALtVISYV---------TPVFLVALLPLAVVCYFIQKY 1181
Cdd:cd18577 127 LLIQSLS----TFIAGF-IIAFIyswkltlvlLATLPLIAIVGGIMGKLLSKY 174
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
697-890 |
5.45e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.49 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 697 LSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQK--VSGAVFWNSlpdsegedpSSPEQETVADSDVRTRGPVAYas 774
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANN---------RKPTKQILKRTGFVTQDDILY-- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 qkPWLlnaTVEENITFES----PFNKQRYKMVIEACSLQPDIDiLPHGDQTQIGE---RGInlSGGQRQRISVARALYQH 847
Cdd:PLN03211 153 --PHL---TVRETLVFCSllrlPKSLTKQEKILVAESVISELG-LTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLIN 224
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490492289 848 TNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHK 890
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLT--LGSLAQKGKTIVTSMHQ 265
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1470-1558 |
5.69e-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: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1470 GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-AD 1547
Cdd:cd03219 132 GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlAD 211
|
90
....*....|.
gi 1490492289 1548 LVMVLKRGAIL 1558
Cdd:cd03219 212 RVTVLDQGRVI 222
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1058-1226 |
6.09e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 43.78 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1058 ALDQSVYAMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIP 1137
Cdd:cd18780 40 ALNQAVLILLGVVL--IGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1138 STLECLSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLT 1212
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWkltlVMLSVVPPLSIGAVIYGKYVRKLSKKFQD-----ALAAASTVAEeSISNIR 192
|
170
....*....|....
gi 1490492289 1213 TIRAFRYEARFQQK 1226
Cdd:cd18780 193 TVRSFAKETKEVSR 206
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1359-1562 |
6.51e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.49 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1359 KPVLKHVNALISPGQKIGICGRTGSGKSSF--SLAFFRMVDMFEGRIIIDGIDIAKlplHTLRsRLSIILQDPVLFSG-T 1435
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYPHlT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1436 IRFNLdpeKKCSDSTLWEALEiAQLKLVVKalpgglDAIITEGG----EN----------FSQGQRQLFCLARAFVRKTS 1501
Cdd:PLN03211 157 VRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 1502 IFIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILsaDLVMVLKRGAILEFDK 1562
Cdd:PLN03211 227 LLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGK 290
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1065-1279 |
7.28e-04 |
|
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: 43.60 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1065 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECLS 1144
Cdd:cd18567 45 AIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1145 RSTLLCVSALTVI-SYVTPVFLVALLplAVVCYFI-----QKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 1218
Cdd:cd18567 124 LDGLMAILTLVMMfLYSPKLALIVLA--AVALYALlrlalYPPLRRATEEQIVASAKEQ----SHFLETIRGIQTIKLFG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 1219 YEARFQQKLLE-YTDSNN------IASLFLTAANRWLeVRMEYIgacVVLIAAATSIsnsLHRELSAG 1279
Cdd:cd18567 198 REAEREARWLNlLVDAINadirlqRLQILFSAANGLL-FGLENI---LVIYLGALLV---LDGEFTVG 258
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1076-1290 |
7.41e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 43.45 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1076 IVLCLVTSVTVEWTGLK------VAKRLHHSLLNC----IILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSR 1145
Cdd:cd18784 40 IIMGLLAIASSVAAGIRgglftlAMARLNIRIRNLlfrsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1146 STllcVSALTVIsyvtpVFLVAL-----------LPL-AVVCYFIQKYFRVASRDLQqlddtTQLPLLSHFA-ETVEGLT 1212
Cdd:cd18784 120 SL---VKAIGVI-----VFMFKLswqlslvtligLPLiAIVSKVYGDYYKKLSKAVQ-----DSLAKANEVAeETISSIR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1213 TIRAF--------RYEARFQQ-------KLLEYTDSNNIASLFLTAanrwLEVRMEYIGACVVLIAAATS---ISNSLHR 1274
Cdd:cd18784 187 TVRSFanedgeanRYSEKLKDtyklkikEALAYGGYVWSNELTELA----LTVSTLYYGGHLVITGQISGgnlISFILYQ 262
|
250
....*....|....*...
gi 1490492289 1275 -ELSAGLVGLGLTYA-LM 1290
Cdd:cd18784 263 lELGSCLESVGSVYTgLM 280
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
446-562 |
9.33e-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: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 446 IIVGVILLYY--ILGVSALIGAAVIILLApvqYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAW 515
Cdd:cd18555 130 VIYLIYMLYYspLLTLIVLLLGLLIVLLL---LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKslgsekniYKKW 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1490492289 516 ENIFCSRVEMTRKKEMTSlrafAVYTSISIFMNTAIPIaavLITFVG 562
Cdd:cd18555 207 ENLFKKQLKAFKKKERLS----NILNSISSSIQFIAPL---LILWIG 246
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1345-1578 |
9.74e-04 |
|
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: 42.71 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSlkPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEGRIIIDGIDIAK-LPLHTLRSR-L 1422
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAGLERPDSGTILFGGEdATDVPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDPVLF-----SGTIRFNLDPEKKcsdSTLWEALEIAQ-----LKLVvkalpgGLDAIITEGGENFSQGQRQLFCL 1492
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRVKPR---SERPPEAEIRAkvhelLKLV------QLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1493 ARAFVRKTSIFIMDEATASIDMATENILQKVVmTAFADRTVVT---IAHRVHTILS-ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 1490492289 1569 QKDSIF-ASFV 1578
Cdd:cd03296 227 HPASPFvYSFL 237
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1065-1315 |
1.10e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 42.88 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1065 AMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1144
Cdd:cd18563 48 GLAGAYV--LSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1145 RSTLLCVSALTVISYVTPVF-LVALLPLAVVCYFIQKYFRVASRDLQQL----DDTTqlpllSHFAETVEGLTTIRAF-- 1217
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLaLLVLIPVPLVVWGSYFFWKKIRRLFHRQwrrwSRLN-----SVLNDTLPGIRVVKAFgq 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1218 -RYE-ARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEyIGACVVLIAAATSIsnsLHRELSAGLVGLGLTYALMVSNYL 1295
Cdd:cd18563 201 eKREiKRFDEANQELLDANIRAEKLWATFFPLLTFLTS-LGTLIVWYFGGRQV---LSGTMTLGTLVAFLSYLGMFYGPL 276
|
250 260
....*....|....*....|
gi 1490492289 1296 NWMVRNLADMEIQLGAVKRI 1315
Cdd:cd18563 277 QWLSRLNNWITRALTSAERI 296
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1345-1571 |
1.11e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.87 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKpVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSI 1424
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1425 ILQDP--VLFS---------GTIRFNLDPEkkcsdsTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1493
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEE------TVAHRVSSA-LHML------GLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1494 RAFVRKTSIFIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLN 1568
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 1490492289 1569 QKD 1571
Cdd:PRK13652 228 QPD 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1345-1386 |
1.15e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.38 E-value: 1.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 1345 IQIQNLSVRY------DSSLK--------------PVLKHVNALISPGQKIGICGRTGSGKS 1386
Cdd:COG1134 5 IEVENVSKSYrlyhepSRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKS 66
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1335-1573 |
1.19e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1335 IPKNWPDQGKIQIQNLSVRYDS---SLKPVlkhvNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIA 1411
Cdd:PRK10522 313 RPQAFPDWQTLELRNVTFAYQDngfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1412 KLPLHTLRSRLSIILQDPVLFSGTirfnLDPEKKCSDSTLWEA-LEIAQLKlvvkalpgglDAIITEGGE----NFSQGQ 1486
Cdd:PRK10522 389 AEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMA----------HKLELEDGRisnlKLSKGQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1487 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVMVLKRGAILEFDKPE 1564
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEE 534
|
....*....
gi 1490492289 1565 TLLNQKDSI 1573
Cdd:PRK10522 535 RDAASRDAV 543
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
779-914 |
1.34e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 779 LLNATVEE-NITFesPFNKQrykmvIEAcSLQPDIDI----LPhgdqtqIGERGINLSGGQRQRISVARALY---QHTNV 850
Cdd:PRK00635 1658 LLQTPIEEvAETF--PFLKK-----IQK-PLQALIDNglgyLP------LGQNLSSLSLSEKIAIKIAKFLYlppKHPTL 1723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 851 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 914
Cdd:PRK00635 1724 FLLDEIATSLDNQQKSALLV--QLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKI 1785
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
829-891 |
1.59e-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: 1.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 829 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSDHLMQAGILELLRDDKRTVVLVTHKL 891
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
695-921 |
1.71e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 695 PTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnSLpDSEGEDPSSPeQETVADSdvrtrgpVAYAS 774
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYV---TL-DGHEVVTRSP-QDGLANG-------IVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QKP----WLLNATVEENIT------FESPFNKQRYKMVIEACSlqpD-IDIL----PHGDQtQIGergiNLSGGQRQRIS 839
Cdd:PRK10762 334 EDRkrdgLVLGMSVKENMSltalryFSRAGGSLKHADEQQAVS---DfIRLFniktPSMEQ-AIG----LLSGGNQQKVA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREgtlkdFQ 918
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQ--LINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRISGE-----FT 478
|
...
gi 1490492289 919 RSE 921
Cdd:PRK10762 479 REQ 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
700-909 |
1.80e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.65 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 700 ISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSLPDSEgEDPSSPEQETVAD-SDV----RTRGPVAYAS 774
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKLFSAVfTDFhlfdQLLGPEGKPA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 775 QK----PWLLNATVEENITFEspfnkqrykmvieacslqpDIDILphgdqtqigerGINLSGGQRQRISVARALYQHTNV 850
Cdd:PRK10522 421 NPalveKWLERLKMAHKLELE-------------------DGRIS-----------NLKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 851 VFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQ 909
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1344-1570 |
1.89e-03 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 41.92 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1344 KIQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLS 1423
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1424 IILQDPVLFSG-TIRfNLDPEKKCSDSTLWEALEIAQLKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1501
Cdd:PRK11231 80 LLPQHHLTPEGiTVR-ELVAYGRSPWLSLWGRLSAEDNARVNQAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490492289 1502 IFIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVMVLKRGAILEFDKPETLLNQK 1570
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1109-1227 |
1.92e-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: 42.08 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1109 PMRFFETTPLGSILNRFSSDCNTIdQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRV 1184
Cdd:cd18543 86 DGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPplalVALASLPPLVLVARRFRRRYFP 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1490492289 1185 ASRDLQQL--DDTTqlpllsHFAETVEGLTTIRAFRYEARFQQKL 1227
Cdd:cd18543 165 ASRRAQDQagDLAT------VVEESVTGIRVVKAFGRERRELDRF 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1558 |
2.15e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.00 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1344 KIQIQNLSVRYDSSLKPVLK---HVNALISPGQKIGICGRTGSGKSSF-------------SLAFFRMVDMFEGRIIIDG 1407
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFiehlnalllpdtgTIEWIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1408 IDIAKLPLHT-----------LRSRLSIILQ--DPVLFSGTIR---------FNLDPEkkcsdstlwEALEIAQ--LKLV 1463
Cdd:PRK13651 82 KVLEKLVIQKtrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEkdiifgpvsMGVSKE---------EAKKRAAkyIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1464 vkalpgGLD-AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVH 1541
Cdd:PRK13651 153 ------GLDeSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
250
....*....|....*...
gi 1490492289 1542 TILS-ADLVMVLKRGAIL 1558
Cdd:PRK13651 227 NVLEwTKRTIFFKDGKII 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1480-1565 |
2.24e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.31 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1480 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVMVLKRG 1555
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDG 216
|
90
....*....|.
gi 1490492289 1556 A-ILEFDKPET 1565
Cdd:COG1129 217 RlVGTGPVAEL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
691-908 |
2.26e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.32 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 691 PDGIPTLSNISIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNslpdseGED--PSSPEQetvadsdVRTRG 768
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD------GEDitGLSPRE-------RRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 769 pVAYASQKPW----LLNATVEENITFES----PFNK----QRYKMVIEACSLQPDIDILPHGDQTQIGergiNLSGGQRQ 836
Cdd:COG3845 335 -VAYIPEDRLgrglVPDMSVAENLILGRyrrpPFSRggflDRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490492289 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTI 908
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQR-LLE-LRDAGAAVLLISEDLDeILALSDRIAVMYEGRI 480
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
830-913 |
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 1490492289 830 LSGGQRQRISVA---------RALYqhtnvvFLDDPFSAL---DVHlsdHLMQagILELLRDDKRTVVLVTHKLQYLPHA 897
Cdd:PRK00349 831 LSGGEAQRVKLAkelskrstgKTLY------ILDEPTTGLhfeDIR---KLLE--VLHRLVDKGNTVVVIEHNLDVIKTA 899
|
90 100
....*....|....*....|..
gi 1490492289 898 DWIIAM------KDGTIQREGT 913
Cdd:PRK00349 900 DWIIDLgpeggdGGGEIVATGT 921
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
817-936 |
2.62e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 817 HGDQ-TQIGERginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHKLQYL- 894
Cdd:PRK10636 420 QGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVSHDRHLLr 491
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1490492289 895 PHADWIIAMKDGTIQR-EGTLKDFQRseyqlfehWKTLMNRQD 936
Cdd:PRK10636 492 STTDDLYLVHDGKVEPfDGDLEDYQQ--------WLSDVQKQE 526
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1345-1559 |
2.74e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.76 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKpVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMF--EGRIIIDGIDIAKLPLHTLRSRL 1422
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSsgRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1423 SIILQDP--VLFSGTIR-------FNLD-PEKKCSdstlwealeiaqlKLVVKALP-GGLDAIITEGGENFSQGQRQLFC 1491
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKlPEDEVR-------------KRVDNALKrTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490492289 1492 LARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LSADLVMVLKRG-AILE 1559
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGrVILQ 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1345-1388 |
2.93e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 41.30 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSF 1388
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTL 44
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
825-901 |
3.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 825 ERGIN-LSGGQRQRISVARALYQHTNVV--FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWII 901
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
831-894 |
3.56e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 3.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490492289 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVH----LSDHLMQAgilellrddKRTVVLVTHKLQYL 894
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKW---------PKTFIVVSHAREFL 404
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1087-1234 |
3.61e-03 |
|
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: 41.26 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1087 EWTGLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-L 1165
Cdd:cd18542 64 EKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLtL 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1166 VALLPLAVVCYFIQKYFRVASRDLQQLDDttQLPLLSHFA-ETVEGLTTIRAF---RYE-ARFQQKLLEYTDSN 1234
Cdd:cd18542 144 ISLAIIPFIALFSYVFFKKVRPAFEEIRE--QEGELNTVLqENLTGVRVVKAFareDYEiEKFDKENEEYRDLN 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1345-1391 |
4.57e-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: 40.20 E-value: 4.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFSLA 1391
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKT 45
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1345-1561 |
5.31e-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: 39.93 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSslKPVLKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLPlhtLRS 1420
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEptsgRIYIGGRDVTDLP---PKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1421 R-LSIILQDPVLFS-----GTIRFNLD----PEKKCSDSTLWEAlEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLF 1490
Cdd:cd03301 72 RdIAMVFQNYALYPhmtvyDNIAFGLKlrkvPKDEIDERVREVA-ELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490492289 1491 CLARAFVRKTSIFIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILSADLVMVLKRGAILEFD 1561
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
818-906 |
5.66e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 818 GDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHA 897
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGIT 458
|
....*....
gi 1490492289 898 DWIIAMKDG 906
Cdd:PRK10982 459 DRILVMSNG 467
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1345-1559 |
7.54e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 40.45 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPV--LKHVNALISPGQKIGICGRTGSGKSSfsLAffRMVDMFEG----RIIIDGIDIAKLP---L 1415
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKST--LI--RCINLLERptsgSVLVDGVDLTALSereL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1416 HTLRSRLSIILQDpvlfsgtirFNLDPEKkcsdsTLWE----ALEIAQ-------------LKLV-----VKALPGGLda 1473
Cdd:COG1135 78 RAARRKIGMIFQH---------FNLLSSR-----TVAEnvalPLEIAGvpkaeirkrvaelLELVglsdkADAYPSQL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1474 iiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENIL---QKVvmtafADR---TVVTIAHRVHTILS- 1545
Cdd:COG1135 142 ---------SGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIVLITHEMDVVRRi 207
|
250
....*....|....
gi 1490492289 1546 ADLVMVLKRGAILE 1559
Cdd:COG1135 208 CDRVAVLENGRIVE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1345-1557 |
7.71e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.07 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRY----DSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRM---------VDMFEGRIIIDgidia 1411
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlipsegkvyVDGLDTSDEEN----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1412 klpLHTLRSRLSIILQDP------------VLFSGTirfNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLdaiitegg 1479
Cdd:PRK13633 80 ---LWDIRNKAGMVFQNPdnqivativeedVAFGPE---NLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1480 enfSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILSADLVMVLK 1553
Cdd:PRK13633 146 ---SGGQKQRVAIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIVMD 218
|
....
gi 1490492289 1554 RGAI 1557
Cdd:PRK13633 219 SGKV 222
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1090-1234 |
7.78e-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: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1090 GLKVAKRLHHSLLNCIILAPMRFFETTPLGSILNRFSSDCntidQHIPSTLE-CLS---RSTLL---CVSALTVISYVTP 1162
Cdd:cd18574 70 GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV----QEFKSSFKqCVSqglRSVTQtvgCVVSLYLISPKLT 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490492289 1163 VFLVALLPLAVVC-YFIQKYFRVASRDLQQLDDTTqlplLSHFAETVEGLTTIRAFRYEAR----FQQKLLEYTDSN 1234
Cdd:cd18574 146 LLLLVIVPVVVLVgTLYGSFLRKLSRRAQAQVAKA----TGVADEALGNIRTVRAFAMEDRelelYEEEVEKAAKLN 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1352-1552 |
8.88e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 39.70 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1352 VRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVL 1431
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1432 FSGTIRFNL-----------DPEKKCSDstlwealeiaqlkLVVKALPgglDAIITEGGENFSQGQRQLFCLARAFVRKT 1500
Cdd:PRK10247 93 FGDTVYDNLifpwqirnqqpDPAIFLDD-------------LERFALP---DTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490492289 1501 SIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVMVL 1552
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1345-1570 |
9.49e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.17 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1345 IQIQNLSVRYDSSLKPV--LKHVNALISPGQKIGICGRTGSGKSSFslafFRMVDMFEG----RIIIDGIDIAKLP---L 1415
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLLERptsgRVLVDGQDLTALSekeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1416 HTLRSRLSIILQdpvlfsgtiRFNLdpekkCSDSTLWE----ALEIAQ-------------LKLVvkalpgGLDAIITEG 1478
Cdd:PRK11153 78 RKARRQIGMIFQ---------HFNL-----LSSRTVFDnvalPLELAGtpkaeikarvtelLELV------GLSDKADRY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 1479 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvvMTAFADR----TVVTIAHRVHTILS-ADLVMVL 1552
Cdd:PRK11153 138 PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAtTRSILE---LLKDINRelglTIVLITHEMDVVKRiCDRVAVI 214
|
250 260
....*....|....*....|....*
gi 1490492289 1553 KRGAILE-------FDKPETLLNQK 1570
Cdd:PRK11153 215 DAGRLVEqgtvsevFSHPKHPLTRE 239
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| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
392-609 |
9.90e-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: 39.71 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 392 IQTKIYNKIMQLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYI---LGVSALIGAAV 467
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTsALTVLVRDPLTVIGLLGVLFYLdwkLTLIALVVLPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490492289 468 IILlaPVQYFvATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FCSRVEMTRKKEMTSLRAFAVYTSI 543
Cdd:cd18552 152 AAL--PIRRI-GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490492289 544 SIFMnTAIPIAAVLItFVGHVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 609
Cdd:cd18552 229 MELL-GAIAIALVLW-YGGYQVI--SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
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