|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
224-1578 |
0e+00 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 843.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 224 LLSKGTYWWMNAFIKTAHKKPI---DLRAIGK----LPIAMRALTNYQRLCEAFDAQ-------RKDIQGTQGAR----- 284
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsEMVVPVLVENWKKECKKTRKQpvsavygKKDPSKPKGSSqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 285 -----------------AIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLgkeNDVFQPKTQFlgvYFVSS 347
Cdd:TIGR00957 289 eevealivksphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFV---NDPMAPDWQG---YFYTG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 348 QEFLANAyvlavllflallLQRTFLQASYYVAIETGINLRGAIQTKIYNKImhLSTSNLSMGEMTAGQICNLVAIDTNQL 427
Cdd:TIGR00957 363 LLFVCAC------------LQTLILHQYFHICFVSGMRIKTAVMGAVYRKA--LVITNSARKSSTVGEIVNLMSVDAQRF 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 428 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 507
Cdd:TIGR00957 429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 508 LKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVT 587
Cdd:TIGR00957 509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 588 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIReeqcapheptPQGpaskyqavplrvVNRKrparedcrgltgplqslvP 667
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLSHEELE----------PDS------------IERR------------------T 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 668 SADGDADNccVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdsei 747
Cdd:TIGR00957 629 IKPGEGNS--ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------- 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 748 gedpsperetatdldiRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI 827
Cdd:TIGR00957 696 ----------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGV 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 828 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQ--AGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 905
Cdd:TIGR00957 760 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRILVTHGISYLPQVDVIIVMSGG 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 906 TI----------QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE-LEKE---TVTERKATEPPQGLSRAMSSRDGL 965
Cdd:TIGR00957 838 KIsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEaKLIEngmLVTDVVGKQLQRQLSASSSDSGDQ 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 966 LQDEEEEEEEAAESEEDDNLSSMLHQRAEIP-------WracaKYLSSAGILLLSLLVFSQLLKHMVLVAIDYWLAKWTD 1038
Cdd:TIGR00957 918 SRHHGSSAELQKAEAKEETWKLMEADKAQTGqvelsvyW----DYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTD 993
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1039 SALT-LTPAARNCSLSqectldqtVYAmvftvlcSLGI---VLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFET 1114
Cdd:TIGR00957 994 DPMVnGTQNNTSLRLS--------VYG-------ALGIlqgFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFER 1058
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1115 TPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDT 1194
Cdd:TIGR00957 1059 TPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESV 1138
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1195 TQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNslHRE 1274
Cdd:TIGR00957 1139 SRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVIS--RHS 1216
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1275 LSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNL 1349
Cdd:TIGR00957 1217 LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE------APWQIqetapPSGWPPRGRVEFRNY 1290
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1350 SVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPV 1429
Cdd:TIGR00957 1291 CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPV 1370
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1430 LFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1509
Cdd:TIGR00957 1371 LFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1510 SIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKdSVFASFVR 1578
Cdd:TIGR00957 1451 AVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
222-1579 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 739.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 222 VNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQRKDIQGtqgaraiW--QALSHAFGRRLV 299
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKP-------WllRALNNSLGGRFW 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 300 LSSTFRILADLLGFAGPLcifgIVDHLGKENDVFQPKTQ--------FLGVYFvssqeflanayvlavllflalllqRTF 371
Cdd:PLN03130 305 LGGFFKIGNDLSQFVGPL----LLNLLLESMQNGEPAWIgyiyafsiFVGVVL------------------------GVL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 372 LQASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 450
Cdd:PLN03130 357 CEAQYFQNVmRVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 451 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMT 530
Cdd:PLN03130 435 LYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELS 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 531 SLRAFAIYTSISIFMNTAIPIAAVLITFvGHVSFFKeADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLS 610
Cdd:PLN03130 515 WFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLG-GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 611 EFLSsAEIREEQcaphePTPqgpaskyqavplrvvnrkrparedcrgltgPLQSLVPSadgdadnccVQIMGGYFTWTPD 690
Cdd:PLN03130 593 ELLL-AEERVLL-----PNP------------------------------PLEPGLPA---------ISIKNGYFSWDSK 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 G-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAvfwssslpdseigedpsperetatdlDIRKRGPV 769
Cdd:PLN03130 628 AeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA--------------------------SVVIRGTV 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANV 849
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 850 VFLDDPFSALDIHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-------FQrsecQ 922
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEElsnngplFQ----K 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 923 LFEHWKTLMNRQDQELEKE---TVTERKATEPPQGLSRAMSSRDGLLQDeeeeeeeaaeseeddnlSSMLHQRAE----- 994
Cdd:PLN03130 836 LMENAGKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSKKKSKEG-----------------KSVLIKQEEretgv 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 995 IPWRACAKYLSS-AGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLT--PAARNcslsqectldqTVYAMVftvlc 1071
Cdd:PLN03130 899 VSWKVLERYKNAlGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKThgPLFYN-----------LIYALL----- 962
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1072 SLGIVLclVTSVTVEW---TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLL 1148
Cdd:PLN03130 963 SFGQVL--VTLLNSYWlimSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQ 1040
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1149 CVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLE 1228
Cdd:PLN03130 1041 LLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGR 1120
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1229 YTDSNNIASLFLTAANRWLEVRMEYIGACVVLIA---AVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADME 1305
Cdd:PLN03130 1121 SMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTasfAVMQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAE 1200
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1306 LQLGAVKRIHGLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRT 1380
Cdd:PLN03130 1201 NSLNAVERVGTYIDLPSE------APLVIennrpPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRT 1274
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1381 GSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLK 1460
Cdd:PLN03130 1275 GAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLK 1354
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1461 LVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVH 1540
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLN 1434
|
1370 1380 1390
....*....|....*....|....*....|....*....
gi 1189438338 1541 TILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1579
Cdd:PLN03130 1435 TIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-1579 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 720.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPI--AMRALTNYQRLCEAFDAQRKDiqgtqgaRAIWQALSHAFGRRLVL 300
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQwdQTETLIKRFQRCWTEESRRPK-------PWLLRALNNSLGGRFWL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 301 SSTFRILADLLGFAGPLcifgIVDHLGKENDVFQPK--------TQFLGVYFvssqeflanayvlavllflalllqRTFL 372
Cdd:PLN03232 306 GGIFKIGHDLSQFVGPV----ILSHLLQSMQEGDPAwvgyvyafLIFFGVTF------------------------GVLC 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 373 QASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILL 451
Cdd:PLN03232 358 ESQYFQNVgRVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 452 YYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTS 531
Cdd:PLN03232 436 YQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSW 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 532 LRAFAIYTSISIFMNTAIPIAAVLITFvgHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSE 611
Cdd:PLN03232 516 FRKAQLLSAFNSFILNSIPVVVTLVSF--GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEE 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 612 FLSSaeirEEQCAPHEPtpqgpaskyqavplrvvnrkrparedcrgltgPLQSLVPSadgdadnccVQIMGGYFTW-TPD 690
Cdd:PLN03232 594 LLLS----EERILAQNP--------------------------------PLQPGAPA---------ISIKNGYFSWdSKT 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMqkvsgavfwssslpdseigedpSPERETATDLdirkRGPVA 770
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL----------------------SHAETSSVVI----RGSVA 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 850
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIY 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 851 FLDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEcQLFEHWKTL 930
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG-SLFKKLMEN 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 931 MNRQDQELEKETVTERKATEPP--------QGLSRAMSSRDGllqdeeeeeeeaaeseeddnlSSMLHQRAE-----IPW 997
Cdd:PLN03232 840 AGKMDATQEVNTNDENILKLGPtvtidvseRNLGSTKQGKRG---------------------RSVLVKQEEretgiISW 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 998 RACAKYLSS-AGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSAltlTPAARNCSLsqectldqtvYAMVFTVLCSLGIV 1076
Cdd:PLN03232 899 NVLMRYNKAvGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQS---TPKSYSPGF----------YIVVYALLGFGQVA 965
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1077 LCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVI 1156
Cdd:PLN03232 966 VTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALI 1045
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1157 SYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIA 1236
Cdd:PLN03232 1046 GTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRF 1125
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1237 SLFLTAANRWLEVRMEYIGACVVLIAAVTSI---SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKR 1313
Cdd:PLN03232 1126 TLANTSSNRWLTIRLETLGGVMIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVER 1205
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1314 IHGLLKTEAEsyegllAPSLIPKN-----WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS 1388
Cdd:PLN03232 1206 VGNYIDLPSE------ATAIIENNrpvsgWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSML 1279
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1389 LAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPG 1468
Cdd:PLN03232 1280 NALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPF 1359
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1469 GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLV 1548
Cdd:PLN03232 1360 GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKI 1439
|
1370 1380 1390
....*....|....*....|....*....|.
gi 1189438338 1549 IVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1579
Cdd:PLN03232 1440 LVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
368-1579 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 645.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 368 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDT---NQLMWFfflCPNLWAMPVQI 444
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVeriNSFMQY---CMYLWSSPMVL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 445 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETT 524
Cdd:PTZ00243 375 LLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 525 RRKEMTSLRAFAIYTSISIFMNTAIP---IAAVLITF--VGHvsffkeaDFSPSVAFASLSLFHILVTPLFLLSSVVRST 599
Cdd:PTZ00243 455 RARELRYLRDVQLARVATSFVNNATPtlmIAVVFTVYylLGH-------ELTPEVVFPTIALLGVLRMPFFMIPWVFTTV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 600 VKALVSVQKLSEFLSS-----------AEIREEQcAPHEPTPQGPA-------SKYQAVPL-RVVNRK-----RPAREDC 655
Cdd:PTZ00243 528 LQFLVSIKRISTFLECdnatcstvqdmEEYWREQ-REHSTACQLAAvlenvdvTAFVPVKLpRAPKVKtsllsRALRMLC 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 656 RGLTGPLQSLVP--------------SADGDADNCCVQIMGG------------------YFTWTPDGIptLSNITIRIP 703
Cdd:PTZ00243 607 CEQCRPTKRHPSpsvvvedtdygspsSASRHIVEGGTGGGHEatptsersaktpkmktddFFELEPKVL--LRDVSVSVP 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 704 RGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfWSsslpdseigedpspEREtatdldirkrgpVAYASQKPWLLNATV 783
Cdd:PTZ00243 685 RGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WA--------------ERS------------IAYVPQQAWIMNATV 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 784 EENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHL 863
Cdd:PTZ00243 738 RGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 864 SDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEcqLFEHWKT-LMNRQDQeleKET 942
Cdd:PTZ00243 818 GERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATLAAeLKENKDS---KEG 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 943 VTERKATEppqglsraMSSRDGLLQDEEEEEEEAAESEEDDNLSSM------LHQRAE-----IPWRACAKYLSSAG--- 1008
Cdd:PTZ00243 891 DADAEVAE--------VDAAPGGAVDHEPPVAKQEGNAEGGDGAALdaaagrLMTREEkasgsVPWSTYVAYLRFCGglh 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1009 --ILLLSLLVFSQLlkhmVLVAIDYWLAKWTdsaltltpaarncslSQECTLDQTVYAMVFtvlcsLGIVLCLVTSV--- 1083
Cdd:PTZ00243 963 aaGFVLATFAVTEL----VTVSSGVWLSMWS---------------TRSFKLSAATYLYVY-----LGIVLLGTFSVplr 1018
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1084 -TVEWTGLKV-AKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP 1161
Cdd:PTZ00243 1019 fFLSYEAMRRgSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQP 1098
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1162 VFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLT 1241
Cdd:PTZ00243 1099 FVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLEN 1178
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1242 AANRWLEVRMEYIGACVVLIAAVTSISNSLHRELS--AGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKR----IH 1315
Cdd:PTZ00243 1179 VANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERllyyTD 1258
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1316 GL-------LKTE---AESYEGLLA---------PSLIPKNWP---DQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQK 1373
Cdd:PTZ00243 1259 EVphedmpeLDEEvdaLERRTGMAAdvtgtvviePASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREK 1338
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1374 IGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEA 1453
Cdd:PTZ00243 1339 VGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAA 1418
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1454 LEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFI-MDEATASIDMATENILQKVVMTAFADRTV 1532
Cdd:PTZ00243 1419 LELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQATVMSAFSAYTV 1498
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*..
gi 1189438338 1533 VTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1579
Cdd:PTZ00243 1499 ITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1342-1581 |
3.90e-149 |
|
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: 455.91 E-value: 3.90e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1342 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1501
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1502 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1581
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
1014-1315 |
9.62e-145 |
|
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: 445.89 E-value: 9.62e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1014 LLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVA 1093
Cdd:cd18602 3 LVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1094 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1173
Cdd:cd18602 83 RRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1174 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1253
Cdd:cd18602 163 YYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 1254 IGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1315
Cdd:cd18602 243 LGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVL 304
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
678-906 |
4.40e-141 |
|
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: 432.53 E-value: 4.40e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 678 VQIMGGYFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPDSEigedpspereT 757
Cdd:cd03290 1 VQVTNGYFSWGS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEP----------S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 758 ATDLDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRI 837
Cdd:cd03290 70 FEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 838 SVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 906
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
300-609 |
4.69e-137 |
|
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: 425.50 E-value: 4.69e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 300 LSSTFRILADLLGFAGPLCIFGIVDHLGKENDVFQPKTQFLGVYFVSSQEFLANAYVLAVLLFLALLLQRTFLQASYYVA 379
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVSYVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 380 IETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 459
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 460 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYT 539
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 540 SISIFMNTAIPIAAVLITFVGHVsFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 609
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYP-YLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
223-1581 |
3.25e-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: 433.57 E-value: 3.25e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDaqrKDIQGTQGARAIWQALSHAFGRRLVLss 302
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWD---RELASAKKNPKLLNALRRCFFWRFVF-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 303 tfriladllgfagplciFGIVDHLGKENDVFQPktQFLGVYFVSSQEFLAN----AYVLAVLLFLALLLQRTFLQASYYV 378
Cdd:TIGR01271 85 -----------------YGILLYFGEATKAVQP--LLLGRIIASYDPFNAPereiAYYLALGLCLLFIVRTLLLHPAIFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 379 AIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVS 458
Cdd:TIGR01271 146 LHHLGMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 459 ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAiy 538
Cdd:TIGR01271 224 GFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 539 tSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHIL-VTPLFLLSSVVRSTVKALVSVQKLSEFLSSAE 617
Cdd:TIGR01271 302 -YLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 618 IR--EEQCAPHEPT--------PQGPASKYQAVPLRVVNRKRParedcrgltgplqslvpsaDGDAdnccvqimGGYFT- 686
Cdd:TIGR01271 381 YKtlEYNLTTTEVEmvnvtaswDEGIGELFEKIKQNNKARKQP-------------------NGDD--------GLFFSn 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 687 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwssslpdseigedpsperetatdlDIRKR 766
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG---------------------------KIKHS 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:TIGR01271 487 GRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKD 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE------ 920
Cdd:TIGR01271 567 ADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfssl 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 921 ---CQLFEHWK--------------------------------------------------------------------- 928
Cdd:TIGR01271 645 llgLEAFDNFSaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkfsfvqmgpqk 724
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 929 -------------------------------------------------------TLMNRQDQELEKETVTERKATEPPQ 953
Cdd:TIGR01271 725 aqattiedavrepserkfslvpedeqgeeslprgnqyhhglqhqaqrrqsvlqlmTHSNRGENRREQLQTSFRKKSSITQ 804
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 954 G---------LSRAMSSRDGLLQDEEEEEEEAAESEEDDnlssMLHQRAEIPWRACAKYLSSAG----ILLLSLLVF-SQ 1019
Cdd:TIGR01271 805 QnelaseldiYSRRLSKDSVYEISEEINEEDLKECFADE----RENVFETTTWNTYLRYITTNRnlvfVLIFCLVIFlAE 880
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1020 LLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLG---IVLCLVTSVTVEWTGLKVAKRL 1096
Cdd:TIGR01271 881 VAASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIITPTSAYYIFYIYVGTAdsvLALGFFRGLPLVHTLLTVSKRL 960
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1097 HRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYF 1176
Cdd:TIGR01271 961 HEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIM 1040
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1177 IQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF----RYEARFQQKLLEYTdsnniASLFLTAAN-RWLEVRM 1251
Cdd:TIGR01271 1041 LRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFgrqsYFETLFHKALNLHT-----ANWFLYLSTlRWFQMRI 1115
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1252 EYIgaCVVLIAAVTSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAESYE----- 1326
Cdd:TIGR01271 1116 DII--FVFFFIAVTFIAIGTNQD-GEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRpsggg 1192
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1327 --GLLAPSLIPKN------WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTf 1398
Cdd:TIGR01271 1193 gkYQLSTVLVIENphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST- 1271
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1399 EGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGG 1478
Cdd:TIGR01271 1272 EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG 1351
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE 1558
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
1530 1540
....*....|....*....|...
gi 1189438338 1559 FDKPEKLLSRKDSVFASFVRADK 1581
Cdd:TIGR01271 1432 YDSIQKLLNETSLFKQAMSAADR 1454
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1342-1562 |
4.37e-111 |
|
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: 350.64 E-value: 4.37e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1342 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1501
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 1502 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKP 1562
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
678-906 |
3.22e-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: 325.19 E-value: 3.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 678 VQIMGGYFTWTPDGI---PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSlpdseigedpspe 754
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 755 retatdldirkrgpVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 834
Cdd:cd03250 68 --------------IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 835 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 906
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1063-1579 |
4.53e-95 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 319.42 E-value: 4.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1063 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1142
Cdd:COG1132 63 LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1143 SRSTLLCVSALAVISYVTP----VFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1218
Cdd:COG1132 143 VRSVVTLIGALVVLFVIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAE----LNGRLQESLSGIRVVKAFGR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1219 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMV 1298
Cdd:COG1132 219 EERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1299 RNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIPknwpDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICG 1378
Cdd:COG1132 299 NVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPP----VRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1379 RTGSGKSSF-SLaFFRM------------VDTfeghiiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPE 1442
Cdd:COG1132 374 PSGSGKSTLvNL-LLRFydptsgrilidgVDI------------RDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1443 RkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 1522
Cdd:COG1132 441 A--TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 1523 VMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLsRKDSVFASFVRA 1579
Cdd:COG1132 519 LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL-ARGGLYARLYRL 574
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
1008-1315 |
2.69e-87 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 286.71 E-value: 2.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1008 GILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSAltltpaarncslsqecTLDQTVYAMVFTVLCSLG-IVLCLVTSVTVE 1086
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSP----------------NSSSGYYLGVYAALLVLAsVLLVLLRWLLFV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1087 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVA 1166
Cdd:cd18580 65 LAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1167 LLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRW 1246
Cdd:cd18580 145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1247 LEVRMEYIGACVVLIAAVTSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1315
Cdd:cd18580 225 LGLRLDLLGALLALVVALLAV--LLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERIL 291
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
1014-1315 |
1.42e-83 |
|
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: 276.28 E-value: 1.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1014 LLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNcslsqectlDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVA 1093
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTE---------QRDYRLGVYGALGLGQAIFVFLGSLALALGCVRAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1094 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1173
Cdd:cd18603 74 RNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1174 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1253
Cdd:cd18603 154 YFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEF 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1254 IGACVVLIAAVTSIsnsLHRE-LSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1315
Cdd:cd18603 234 LGNLIVLFAALFAV---LSRDsLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIK 293
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
1009-1318 |
1.26e-80 |
|
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: 267.80 E-value: 1.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1009 ILLLSLLVFSQLLkhmvLVAIDYWLAKWT---DSALTLTPAARNcslsqectldQTVYAMVFTVLCSLGIVLCLVTSVTV 1085
Cdd:cd18604 2 ALLLLLFVLSQLL----SVGQSWWLGIWAsayETSSALPPSEVS----------VLYYLGIYALISLLSVLLGTLRYLLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1086 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLV 1165
Cdd:cd18604 68 FFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1166 ALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANR 1245
Cdd:cd18604 148 PAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1246 WLEVRMEYIGACVVLIAAVTSISNslhRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLL 1318
Cdd:cd18604 228 WLSVRIDLLGALFSFATAALLVYG---PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1061-1569 |
1.06e-79 |
|
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: 279.03 E-value: 1.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1061 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLE 1140
Cdd:COG2274 196 WVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1141 CLSRSTLLCVSALAVISY----VTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAF 1216
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFysppLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQ----SLLVETLRGIETIKAL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1217 RYEARFQQK-------LLEYTDSNNIASLFLTAANRWLEVrmeyIGACVVLIAAVTSIsnsLHRELSAGlvglGLTYALM 1289
Cdd:COG2274 351 GAESRFRRRwenllakYLNARFKLRRLSNLLSTLSGLLQQ----LATVALLWLGAYLV---IDGQLTLG----QLIAFNI 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1290 VSNYLNWMVRNLADM--ELQ--LGAVKRIHGLLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSLKPVLKHVN 1365
Cdd:COG2274 420 LSGRFLAPVAQLIGLlqRFQdaKIALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGDSPPVLDNIS 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1366 ALIAPGQKIGICGRTGSGKSSFS---LAFFR------MVDTFEGhiiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIR 1436
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLkllLGLYEptsgriLIDGIDL---------RQIDPASLRRQIGVVLQDVFLFSGTIR 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1437 FNL---DPERkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDM 1513
Cdd:COG2274 567 ENItlgDPDA--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1514 ATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1569
Cdd:COG2274 645 ETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1338-1562 |
2.88e-78 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 257.34 E-value: 2.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1338 WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTL 1417
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1418 RSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEiaqlklvvkalpggldaiITEGGENFSQGQRQLFCLARAFVR 1497
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 1498 KTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKP 1562
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
1009-1315 |
9.76e-75 |
|
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: 250.91 E-value: 9.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1009 ILLLSLLVFSQllkhmvlVAIDYWLAKWTDSAltltpaarNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWT 1088
Cdd:cd18605 5 LLSLILMQASR-------NLIDFWLSYWVSHS--------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1089 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALL 1168
Cdd:cd18605 70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1169 PLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLE 1248
Cdd:cd18605 150 PLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1249 VRMEYIGACVVLIAAVTSI-SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1315
Cdd:cd18605 230 IRLQLLGVLIVTFVALTAVvQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVR 297
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
300-609 |
1.51e-72 |
|
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: 244.32 E-value: 1.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 300 LSSTFRILADLLGFAGPLCIFGIVDHLGKENDvfQPKTQ-------FLGVYFVSSqeflanayvlavllflalllqrTFL 372
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD--EPLSEgyllalaLFLVSLLQS----------------------LLL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 373 QASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 452
Cdd:cd18579 57 HQYFFLSFRLGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 453 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSL 532
Cdd:cd18579 135 RLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKAL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 533 RAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEadFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 609
Cdd:cd18579 215 RKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNP--LTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
1009-1315 |
2.42e-69 |
|
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: 235.06 E-value: 2.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1009 ILLLSLLVFSQLLKhmvlVAIDYWLAKWTDSALTLTpaarncslsqectldQTVYAMVFTVLCSLGIVLCLVTSVTVEWT 1088
Cdd:cd18606 2 PLLLLLLILSQFAQ----VFTNLWLSFWTEDFFGLS---------------QGFYIGIYAGLGVLQAIFLFLFGLLLAYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1089 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALL 1168
Cdd:cd18606 63 GIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1169 PLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASlFLTAAN-RWL 1247
Cdd:cd18606 143 PLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAY-FLTIANqRWL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1248 EVRMEYIGACVVLIAAVTSISNSLHreLSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1315
Cdd:cd18606 222 AIRLDLLGSLLVLIVALLCVTRRFS--ISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLL 287
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
1008-1315 |
4.53e-69 |
|
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: 235.15 E-value: 4.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1008 GILLLSLLVFSQLLKHMVLVAIDYWLAKW------TDSALTLTPAARNCSLSQECTLD--QTVYAMVFTVLcslgIVLCL 1079
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgNTTNNVDNSTVDSGNISDNPDLNfyQLVYGGSILVI----LLLSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1080 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV 1159
Cdd:cd18599 77 IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1160 TPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLF 1239
Cdd:cd18599 157 FPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1240 LTAANRWLEVRMEYIGACVVLIAAVTSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1315
Cdd:cd18599 237 FNCAMRWLAVRLDILAVLITLITALLVV--LLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERIL 310
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1342-1570 |
2.27e-61 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 209.77 E-value: 2.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1342 GKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLFSGTIRFNLDPERKCSDSTLW-EALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1501 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1570
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
296-912 |
6.82e-61 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 220.04 E-value: 6.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 296 RRLVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDvFQPKTQFLGVYFVSsqeFLANAyvlavllflalllqrTFLQAS 375
Cdd:COG1132 21 GLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD-LSALLLLLLLLLGL---ALLRA---------------LLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 376 YYVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFF-FLCPNLWAMPVQIIVGVILLYYI 454
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 455 LGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FRTRVETTRRKEMT 530
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 531 SLRAFAIYTSISIFMNTaipIAAVLITFVGhVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLS 610
Cdd:COG1132 240 AARLSALFFPLMELLGN---LGLALVLLVG-GLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 611 EFLSSAEIREEQCAPHEPTPQGPASKYQAVplrvvnrkrparedcrgltgplqslvpsadgdadnccvqimggYFTWtPD 690
Cdd:COG1132 316 ELLDEPPEIPDPPGAVPLPPVRGEIEFENV-------------------------------------------SFSY-PG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLaaLGEMQKVSGAVFwssslpdseIGedpsperetatDLDIRK--- 765
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLvnLL--LRFYDPTSGRIL---------ID-----------GVDIRDltl 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 ---RGPVAYASQKPWLLNATVEENIifespfnkqRY-------KMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGG 832
Cdd:COG1132 410 eslRRQIGVVPQDTFLFSGTIRENI---------RYgrpdatdEEVEEAAkaaQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 833 QRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1089-1569 |
7.38e-61 |
|
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: 219.63 E-value: 7.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1089 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP----VFL 1164
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWlsglILL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1165 VA--LLPLAIVcyFIQKYFRVASRdlQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASL---- 1238
Cdd:COG4988 166 VTapLIPLFMI--LVGKGAAKASR--RQWRALARLS--GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMkvlr 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1239 --FLTAAnrwleVrME---YIGACVVLIAAVTSisnslhreLSAGLVGL--GLTYALMVSNYLNWMvRNL-----ADMEL 1306
Cdd:COG4988 240 vaFLSSA-----V-LEffaSLSIALVAVYIGFR--------LLGGSLTLfaALFVLLLAPEFFLPL-RDLgsfyhARANG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1307 qLGAVKRIHGLLKTEAESyeglLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSS 1386
Cdd:COG4988 305 -IAAAEKIFALLDAPEPA----APAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKST 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1387 FSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPERkcSDSTLWEALEIAQLKLVV 1463
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPDA--SDEELEAALEAAGLDEFV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1464 KALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL 1543
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
490 500
....*....|....*....|....*.
gi 1189438338 1544 SADLVIVLKRGAILEFDKPEKLLSRK 1569
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
300-609 |
2.14e-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: 209.25 E-value: 2.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 300 LSSTFRILADLLGFAGPLcIFGIVDHLGKENDVFQPKTQFLGVYFvssqeFLANayvlavllflalLLQRTFLQASYYVA 379
Cdd:cd18595 1 LAALLKLLSDILLFASPQ-LLKLLINFVEDPDEPLWKGYLYAVLL-----FLVS------------IIQSLLLHQYFHRC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 380 IETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 459
Cdd:cd18595 63 FRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 460 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYT 539
Cdd:cd18595 141 LAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLN 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 540 SISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 609
Cdd:cd18595 221 AVSSFLWTCAPFLVSLATFATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
1008-1314 |
8.15e-60 |
|
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: 208.71 E-value: 8.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1008 GILLLSLLVFSQLLKHMVLVAIDYWLAKWTDS-----ALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTS 1082
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLeeklnDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1083 VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPV 1162
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1163 FLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIA-SLFLT 1241
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAwFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1242 aANRWLEVRMEYIgaCVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1314
Cdd:cd18601 241 -TSRWLAVRLDAL--CALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
370-912 |
6.85e-55 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 205.45 E-value: 6.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 370 TFLQASYYVAIETGINLRgaIQTKIYNKIMHLSTSNL---SMGEMTA-----GQICNLVaidTNQLMWFFFLCPnlwamp 441
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDLASrfrdvESIREFL---TGSLLTALLDLL------ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 442 vQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRV 521
Cdd:COG2274 282 -FVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRW 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 522 ETTRRKEM-TSLRAFAIYTSISIFMNTAIPIAAVLITFVGhVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTV 600
Cdd:COG2274 361 ENLLAKYLnARFKLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 601 KALVSVQKLSEFLSsaeireeqcAPHEPTPqgpaskyqavplrvvnrkrparedcrgltGPLQSLVPSADGDadnccVQI 680
Cdd:COG2274 440 DAKIALERLDDILD---------LPPEREE-----------------------------GRSKLSLPRLKGD-----IEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 681 MGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssslpdseIGedpsperetatD 760
Cdd:COG2274 477 ENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL---------ID-----------G 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 761 LDIRKRGP------VAYASQKPWLLNATVEENIIFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLS 830
Cdd:COG2274 537 IDLRQIDPaslrrqIGVVLQDVFLFSGTIRENITLGDPdATDEE---IIEAArlaGLHDFIEALPMGYDTVVGEGGSNLS 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 831 GGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 910
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
..
gi 1189438338 911 GT 912
Cdd:COG2274 691 GT 692
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1080-1575 |
1.26e-53 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 198.40 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1080 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISY- 1158
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYy 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1159 ---VTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTtqlplLSHFA-ETVEGLTTIRAFRYEARFQQKLLEYTDSNN 1234
Cdd:TIGR02203 153 swqLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQ-----VTTVAeETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1235 IASLFLTAANRWLEVRMEYIG----ACVVLIAAVTSISNSLhrelSAG-LVGLGLTYALMVSNylnwmVRNLAD----ME 1305
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIAslalAVVLFIALFQAQAGSL----TAGdFTAFITAMIALIRP-----LKSLTNvnapMQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1306 LQLGAVKRIHGLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKS 1385
Cdd:TIGR02203 299 RGLAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1386 SFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPeRKCSDSTLWEALEIAQLKLV 1462
Cdd:TIGR02203 373 TLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDF 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1463 VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI 1542
Cdd:TIGR02203 452 VDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTI 531
|
490 500 510
....*....|....*....|....*....|...
gi 1189438338 1543 LSADLVIVLKRGAILEFDKPEKLLSRkDSVFAS 1575
Cdd:TIGR02203 532 EKADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
371-609 |
9.22e-52 |
|
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: 184.58 E-value: 9.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 371 FLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 450
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 451 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMT 530
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 531 SLRAFAIYTSISIFMNTAIPIAAVLITFVghVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 609
Cdd:cd18597 217 YVRKLQILRSILTAVAFSLPVLASMLSFI--TYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
310-607 |
3.77e-51 |
|
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: 183.46 E-value: 3.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 310 LLGFAGPLCIFGIVDHLgkENDVFQPKTQ---FLGVYFVSSqefLANAyvlavllflalllqrTFLQASYYVAIETGINL 386
Cdd:cd18596 11 VLSFAPPFFLNRLLRYL--EDPGEDATVRpwvWVLLLFLGP---LLSS---------------LLDQQYLWIGRRLSVRL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 387 RGAIQTKIYNKIMHL-----------------STSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 449
Cdd:cd18596 71 RAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 450 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEM 529
Cdd:cd18596 151 FLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEEL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 530 TSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEaDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 607
Cdd:cd18596 231 KWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQ-ELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLD 307
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1344-1554 |
7.42e-51 |
|
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: 177.19 E-value: 7.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPVLFSGTIRFNLdperkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFI 1503
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 1504 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRG 1554
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
444-920 |
2.22e-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: 179.57 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 444 IIVGVILLYYILGVSALigAAVIILL-AP--------VQYFvATKLSQAQRSTLEysneRLKQT-NEMLRGIKLLKLY-- 511
Cdd:COG4988 143 ALVPLLILVAVFPLDWL--SGLILLVtAPliplfmilVGKG-AAKASRRQWRALA----RLSGHfLDRLRGLTTLKLFgr 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 512 --AWENIFRTRVETTRRKEMTSLR-AFAIYTSISIFMNTAIPIAAVLITF---VGHVSFFkeadfspsVAFASLslfhIL 585
Cdd:COG4988 216 akAEAERIAEASEDFRKRTMKVLRvAFLSSAVLEFFASLSIALVAVYIGFrllGGSLTLF--------AALFVL----LL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 586 V----TPLFLLSSVVRSTVKALVSVQKLSEFLSSAEireeqcaPHEPTPQGPASKYQAVPLRVvnrkrparedcRGLTgp 661
Cdd:COG4988 284 ApeffLPLRDLGSFYHARANGIAAAEKIFALLDAPE-------PAAPAGTAPLPAAGPPSIEL-----------EDVS-- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 662 lqslvpsadgdadnccvqimggyFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSss 741
Cdd:COG4988 344 -----------------------FSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-- 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 742 lpdseiGEDPSPERETatdlDIRKRgpVAYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQT 820
Cdd:COG4988 398 ------GVDLSDLDPA----SWRRQ--IAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDT 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 821 QIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWII 900
Cdd:COG4988 466 PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRIL 542
|
490 500
....*....|....*....|
gi 1189438338 901 AMKDGTIQREGTLKDFQRSE 920
Cdd:COG4988 543 VLDDGRIVEQGTHEELLAKN 562
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1064-1569 |
3.96e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 179.53 E-value: 3.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1064 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1143
Cdd:PRK10790 68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1144 RSTLLCVSAL-AVISYVTPVFLVALL--PLAIVCYFIQKYF------RVASRdLQQLDDTtqlpllshFAETVEGLTTIR 1214
Cdd:PRK10790 148 RSAALIGAMLvAMFSLDWRMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEVINGMSVIQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1215 AFRYEARFQQKLLEYTDSNNIAslfltaanrwlevRMEYIGACVVLIAAVTSISNS--------LHRELSAGLVGLGLTY 1286
Cdd:PRK10790 219 QFRQQARFGERMGEASRSHYMA-------------RMQTLRLDGFLLRPLLSLFSAlilcgllmLFGFSASGTIEVGVLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1287 ALMvsNYLNWMVRNLADME-----LQLGAV--KRIHGLLKTEAESYegllAPSLIPKNwpdQGKIQIQNLSVRYDSSlKP 1359
Cdd:PRK10790 286 AFI--SYLGRLNEPLIELTtqqsmLQQAVVagERVFELMDGPRQQY----GNDDRPLQ---SGRIDIDNVSFAYRDD-NL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1360 VLKHVNALIAPGQKIGICGRTGSGKSSfsLAFFRM----VDTFEGHIIIDGIdiAKLPLHTLRSRLSIILQDPVLFSGTI 1435
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyypLTEGEIRLDGRPL--SSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1436 RFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1515
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 1516 ENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1569
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1344-1575 |
1.38e-46 |
|
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: 167.41 E-value: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPVLFSGTIRFNLDPER-KCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 1502
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1503 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKdSVFAS 1575
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG-GLYAE 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1342-1581 |
4.53e-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: 167.72 E-value: 4.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1342 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTfEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1501
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1502 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1581
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, ... |
371-609 |
1.55e-45 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 166.58 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 371 FLQASYYVAIETGINLRGAIQTKIYNKIMHLStsnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 450
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 451 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMT 530
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 531 SLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFfkEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 609
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAHVAL--GNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
304-609 |
1.62e-45 |
|
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: 166.57 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 304 FRILADLLGFAGPLCIFGIVDHLgkENDVFQPKTQFL--GVYFVSSqeFLAnayvlavllflalllqrTFLQASY-YVAI 380
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFL--EDSSEPLSDGYLyaLGLVLSS--LLG-----------------ALLSSHYnFQMN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 381 ETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFfflCPNL---WAMPVQIIVGVILLYYILGV 457
Cdd:cd18598 64 KVSLKVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 458 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAI 537
Cdd:cd18598 139 AFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKY 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 538 YTSISIFMNTAIPIAAVLITFVGHVsfFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 609
Cdd:cd18598 219 LDALCVYFWATTPVLISILTFATYV--LMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
691-917 |
1.30e-43 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 160.79 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAvfwssslpdseigedpsperetatdldIRKRGPVA 770
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK---------------------------IKHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 850
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 851 FLDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 917
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1012-1294 |
1.85e-43 |
|
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: 160.12 E-value: 1.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1012 LSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAArncslsqecTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLK 1091
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE---------TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1092 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLA 1171
Cdd:pfam00664 72 LSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1172 IVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRM 1251
Cdd:pfam00664 152 PLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGIT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1189438338 1252 EYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYL 1294
Cdd:pfam00664 232 QFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
444-912 |
2.14e-43 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 168.02 E-value: 2.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 444 IIVGVILLYYILGVSALI---GAAVIILLAPVqyFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTR 520
Cdd:COG4987 143 ILAAVAFLAFFSPALALVlalGLLLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALAR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 521 VETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPS----VAFASLSLFHILVTplflLSSVV 596
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPllalLVLAALALFEALAP----LPAAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 597 RSTVKALVSVQKLSEFLSSAeireeqcaPHEPTPQGPASKYQAVPLRVvnrkrparedcRGLTgplqslvpsadgdadnc 676
Cdd:COG4987 297 QHLGRVRAAARRLNELLDAP--------PAVTEPAEPAPAPGGPSLEL-----------EDVS----------------- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 677 cvqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERE 756
Cdd:COG4987 341 --------FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG--------GVDLRDLDE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 757 TatdlDIRKRgpVAYASQKPWLLNATVEENIIFESPfNKQRYKM--VIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 834
Cdd:COG4987 405 D----DLRRR--IAVVPQRPHLFDTTLRENLRLARP-DATDEELwaALERVGLGDWLAALPDGLDTWLGEGGRRLSGGER 477
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 835 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1092-1570 |
4.71e-43 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 169.52 E-value: 4.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1092 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP-VFLVALLPL 1170
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrLTMVTLINL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1171 AIVcYFIQK----YFRVASRDLQQ-LDDTTQLPLlshfaETVEGLTTIRAF---RYEA-RFQQKLLEYTDSN---NIASL 1238
Cdd:TIGR00958 312 PLV-FLAEKvfgkRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFaaeEGEAsRFKEALEETLQLNkrkALAYA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1239 FLTAANRWLE----VRMEYIGACVVLIAAVTSisnslhrelsAGLVGLgLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1314
Cdd:TIGR00958 386 GYLWTTSVLGmliqVLVLYYGGQLVLTGKVSS----------GNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKV 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1315 HGLL-KTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFF 1392
Cdd:TIGR00958 455 FEYLdRKPNIPLTGTLAPL------NLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1393 RMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPE-RKCSDSTLWEALEIAQLKLVVKALPGGLD 1471
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1472 AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILSADLVIVL 1551
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVL 686
|
490
....*....|....*....
gi 1189438338 1552 KRGAILEFDKPEKLLSRKD 1570
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1344-1579 |
7.87e-43 |
|
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: 156.93 E-value: 7.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1422
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1423 IILQDPVLFSGTIRFNL---DPERkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1499
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1500 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKdSVFASFVRA 1579
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1344-1569 |
2.76e-42 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 155.08 E-value: 2.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPG--ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1501 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1569
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1073-1578 |
3.76e-40 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 160.49 E-value: 3.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1073 LGIVLCLVTSVTVEWTGLKVAKRLHRSL--------LNRIILAPMRFFETTPLGSILNRFSSDcNTIDQHIPSTLECLSR 1144
Cdd:TIGR03796 198 LGMGLTALLQGVLTWLQLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTAL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1145 STLLCV-SALAVISYVTPVFLVALLPLAI---VCYFIQKYFRVASRDLQQldDTTQLpllshFAETVEGLTTIR------ 1214
Cdd:TIGR03796 277 DAVMLVfYALLMLLYDPVLTLIGIAFAAInvlALQLVSRRRVDANRRLQQ--DAGKL-----TGVAISGLQSIEtlkasg 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1215 ----AFRYEARFQQKLLEytdsnniaslfltaANRWLEVRMEYIGacvVLIAAVTSISNSLHRELSAGLV-------GLG 1283
Cdd:TIGR03796 350 lesdFFSRWAGYQAKLLN--------------AQQELGVLTQILG---VLPTLLTSLNSALILVVGGLRVmegqltiGML 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1284 LTY-ALMVS-----NYLNWMVRNLADMElqlGAVKRIHGLLKTEAESYEGLLAP--SLIPKNWPDQGKIQIQNLSVRYDS 1355
Cdd:TIGR03796 413 VAFqSLMSSflepvNNLVGFGGTLQELE---GDLNRLDDVLRNPVDPLLEEPEGsaATSEPPRRLSGYVELRNITFGYSP 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1356 SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTI 1435
Cdd:TIGR03796 490 LEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTV 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1436 RFNL---DPerKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID 1512
Cdd:TIGR03796 570 RDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1513 MATEnilqKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRkDSVFASFVR 1578
Cdd:TIGR03796 648 PETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAV-GGAYARLIR 710
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1342-1556 |
5.04e-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: 148.12 E-value: 5.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1342 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFR-------MVDTFEGhiiidgidiAKL 1412
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLklLAGLYkptsgsvLLDGTDI---------RQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1413 PLHTLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLF 1489
Cdd:cd03245 72 DPADLRRNIGYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 1490 CLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1556
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
685-911 |
5.55e-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: 148.12 E-value: 5.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGE-DPSperetatdlDI 763
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVL----LDGTDIRQlDPA---------DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKRgpVAYASQKPWLLNATVEENIIFESPF-NKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 842
Cdd:cd03245 77 RRN--IGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 843 LYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 911
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
685-905 |
1.15e-39 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 145.22 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssslpDSEIGEDPSPEretatdlDIR 764
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-----DGVDLRDLDLE-------SLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 KRgpVAYASQKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALY 844
Cdd:cd03228 76 KN--IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 845 QHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 905
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEA-LRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
685-912 |
5.78e-39 |
|
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: 145.45 E-value: 5.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAAlgemqkvsgavFWssslpdseigeDPSPERETATDLD 762
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPR-----------FY-----------DVDSGRILIDGHD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 763 IRK------RGPVAYASQKPWLLNATVEENIIFESPfNKQRyKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQ 833
Cdd:cd03251 66 VRDytlaslRRQIGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 834 RQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
317-609 |
1.28e-37 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 143.54 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 317 LCIFGIVDHLGKendVFQPktQFLG---VYFV-SSQEFLANAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQT 392
Cdd:cd18594 2 LGILLFLEESLK---IVQP--LLLGrlvAYFVpDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 393 KIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPV 472
Cdd:cd18594 77 LIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 473 QYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIA 552
Cdd:cd18594 155 QAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 553 AVLITFVGHVsFFKEAdFSPSVAFASLSLFHILVTPL-FLLSSVVRSTVKALVSVQKL 609
Cdd:cd18594 235 VSFATFVPYV-LTGNT-LTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1146-1551 |
1.54e-37 |
|
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: 149.74 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1146 TLLCVSALAVISYVTPVFLVALLPLAIVcYFIQKYFRVASRDLQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQK 1225
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPLIPI-FMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1226 LLEYTDSNNIASL------FLTAAnrwlevRMEYIGACVVLIAAVTsISNSL---HRELSAGLVGLGLTYALmvsnYLNw 1296
Cdd:TIGR02857 209 IRRSSEEYRERTMrvlriaFLSSA------VLELFATLSVALVAVY-IGFRLlagDLDLATGLFVLLLAPEF----YLP- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1297 mVRNL-----ADMELQlGAVKRIHGLLkteaeSYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPG 1371
Cdd:TIGR02857 277 -LRQLgaqyhARADGV-AAAEALFAVL-----DAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1372 QKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERK-CSDSTL 1450
Cdd:TIGR02857 349 ERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPdASDAEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1451 WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR 1530
Cdd:TIGR02857 429 REALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR 508
|
410 420
....*....|....*....|.
gi 1189438338 1531 TVVTIAHRVHTILSADLVIVL 1551
Cdd:TIGR02857 509 TVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1344-1568 |
2.21e-37 |
|
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: 141.08 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPVLFSGTIRFNLDPERKCSD-STLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 1502
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1503 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1568
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
375-616 |
4.30e-37 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 141.97 E-value: 4.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 375 SYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQL-MWFFFLcPNLWAMPVQIIVGVILLYY 453
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 454 ILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLR 533
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 534 AFAIYTSisifMNTAIP-IAAVLITFVGHVSFF-KEADFSPSVAFASLSLFHilvtplfllssVVRSTVKALV--SVQKL 609
Cdd:cd18593 217 RTSFLRA----LNMGLFfVSSKLILFLTFLAYIlLGNILTAERVFVTMALYN-----------AVRLTMTLFFpfAIQFG 281
|
....*..
gi 1189438338 610 SEFLSSA 616
Cdd:cd18593 282 SELSVSI 288
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1080-1569 |
4.62e-37 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 149.01 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1080 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV 1159
Cdd:PRK11176 84 ISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1160 T---PVFLVALLPL-AIVCYFIQKYFRVASRDLQ----QLDDTTQLPLLSHFAETVEGLTTIRAFRYEA---RFQQKLLE 1228
Cdd:PRK11176 164 SwqlSLILIVIAPIvSIAIRVVSKRFRNISKNMQntmgQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKvsnRMRQQGMK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1229 YTDSNN--------IASLFLtaanrwlevrmeyigACVVLIAAVTSISNslhrELSAGlvglglTYALMVSNYLNWM--V 1298
Cdd:PRK11176 244 MVSASSisdpiiqlIASLAL---------------AFVLYAASFPSVMD----TLTAG------TITVVFSSMIALMrpL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1299 RNLADMELQ----LGAVKRIHGLLKTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKI 1374
Cdd:PRK11176 299 KSLTNVNAQfqrgMAACQTLFAILDLEQEKDEGKRVIE------RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1375 GICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPERKCSDSTLWE 1452
Cdd:PRK11176 373 ALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1453 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 1532
Cdd:PRK11176 453 AARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS 532
|
490 500 510
....*....|....*....|....*....|....*..
gi 1189438338 1533 VTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1569
Cdd:PRK11176 533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1099-1569 |
7.37e-37 |
|
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: 150.28 E-value: 7.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1099 SLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLeclsRSTLLCVSALAVISYV-----TPVFLVALLPL--- 1170
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTI----LSLFLDMWILVIVGLFlvrqnMLLFLLSLLSIpvy 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1171 AIVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYEA-RFQQ----------KLLEYTDSNNIASLF 1239
Cdd:TIGR01193 309 AVIIILFKRTFNKLNHDAMQ----ANAVLNSSIIEDLNGIETIKSLTSEAeRYSKidsefgdylnKSFKYQKADQGQQAI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1240 LTAANRWLEVRMEYIGACVVLIAAVTsisnslhrelsaglVGLGLTYALMVSNYLNwMVRNLADMELQLGAVK----RIH 1315
Cdd:TIGR01193 385 KAVTKLILNVVILWTGAYLVMRGKLT--------------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvannRLN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1316 GLLKTEAESYEGLLAPSLIPKNwpdqGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV 1395
Cdd:TIGR01193 450 EVYLVDSEFINKKKRTELNNLN----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1396 DTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPERKCSDSTLWEALEIAQLKLVVKALPGGLDAI 1473
Cdd:TIGR01193 525 QARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1474 ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL 1551
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSDKIIVL 681
|
490
....*....|....*...
gi 1189438338 1552 KRGAILEFDKPEKLLSRK 1569
Cdd:TIGR01193 682 DHGKIIEQGSHDELLDRN 699
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1292-1558 |
6.66e-36 |
|
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: 145.73 E-value: 6.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1292 NYLNWMVR----NLADMElqlgavkRIHGLLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSlKPVLKHVNAL 1367
Cdd:COG5265 313 NFLGFVYReirqALADME-------RMFDLLDQPPEVADAPDAPPLVVG----GGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1368 IAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPErk 1444
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPD-- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1445 CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM 1524
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270
....*....|....*....|....*....|....
gi 1189438338 1525 TAFADRTVVTIAHRVHTILSADLVIVLKRGAILE 1558
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1071-1578 |
1.44e-35 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 145.87 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1071 CSLGIVLCLVTSVTVEWT-GLKVAK-------RLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECL 1142
Cdd:TIGR03797 178 IALALLAAAVGAAAFQLAqSLAVLRletrmdaSLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLTT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1143 SRSTLLCVSALAVISYVTP---VFLVALLPLAIVCYFIQKYFRVA-SRDLQQLDDTTQLPLLshfaETVEGLTTIR---- 1214
Cdd:TIGR03797 257 LLSGIFALLNLGLMFYYSWklaLVAVALALVAIAVTLVLGLLQVRkERRLLELSGKISGLTV----QLINGISKLRvaga 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1215 ---AF-RYEARF-QQKLLEYtDSNNIASlFLTAANRWLEVRmeyigACVVLIAAVTSISNSLHreLSAGLVgLGLTYAL- 1288
Cdd:TIGR03797 333 enrAFaRWAKLFsRQRKLEL-SAQRIEN-LLTVFNAVLPVL-----TSAALFAAAISLLGGAG--LSLGSF-LAFNTAFg 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1289 MVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALI 1368
Cdd:TIGR03797 403 SFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVSLQI 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1369 APGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGID----IAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdperk 1444
Cdd:TIGR03797 477 EPGEFVAIVGPSGSGKSTL----LRLLLGFETPESGSVFYdgqdLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI----- 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1445 CSDSTL-----WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNIL 1519
Cdd:TIGR03797 548 AGGAPLtldeaWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRT 623
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 1520 QKVVMTAFA--DRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRkDSVFASFVR 1578
Cdd:TIGR03797 624 QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR-EGLFAQLAR 683
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
448-912 |
1.93e-35 |
|
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: 144.09 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 448 VILLYYILGVSAligaaVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTN----EMLRGIKLLKLYAWENIFRTRVE- 522
Cdd:TIGR02203 147 IVLLYYSWQLTL-----IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaeETLQGYRVVKLFGGQAYETRRFDa 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 523 ---TTRRKEMTSLRAFAIYTSISIFmntaipIAAVLITFVGHVSFFKEADFSPSVA-FASLSLFHILV-TPLFLLSSVVR 597
Cdd:TIGR02203 222 vsnRNRRLAMKMTSAGSISSPITQL------IASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALiRPLKSLTNVNA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 598 STVKALVSVQKLSEFLSSaeireeqcaPHEPTPQGpaskyqavplRVVNRKRpAREDCRGLTgplqslvpsadgdadncc 677
Cdd:TIGR02203 296 PMQRGLAAAESLFTLLDS---------PPEKDTGT----------RAIERAR-GDVEFRNVT------------------ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 678 vqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEmqkvsgavfwssslPDS-EIGEDPSPE 754
Cdd:TIGR02203 338 -------FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYE--------------PDSgQILLDGHDL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 755 RE-TATDLdirkRGPVAYASQKPWLLNATVEENIIFESP--FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSG 831
Cdd:TIGR02203 397 ADyTLASL----RRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSG 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 832 GQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 911
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
.
gi 1189438338 912 T 912
Cdd:TIGR02203 550 T 550
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
691-912 |
2.52e-35 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 135.05 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssslpdseIGEDPSPERETATdldirKRGPVA 770
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL---------IDGIDIRDISRKS-----LRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLLNATVEENIIFESPFNKQryKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHA 847
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 848 NVVFLDDPFSALDIHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03254 159 KILILDEATSNIDTE-TEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
689-912 |
1.65e-33 |
|
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: 129.97 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKS---SLLLAalgemqkvsgavFWssslpdseigeDPSPERETATDLDIRK 765
Cdd:cd03249 14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKStvvSLLER------------FY-----------DPTSGEILLDGVDIRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 ------RGPVAYASQKPWLLNATVEENIIFESPFNKQryKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQR 836
Cdd:cd03249 70 lnlrwlRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
298-589 |
5.40e-33 |
|
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: 129.69 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 298 LVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDvfqPKTQFLGVYFVssqeFLANAYVLAVLlflalllqrtFLQASYY 377
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD---PETQALNVYSL----ALLLLGLAQFI----------LSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 378 VAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGV 457
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 458 S-ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFA 536
Cdd:pfam00664 142 KlTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 537 IYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPL 589
Cdd:pfam00664 222 VANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
445-902 |
7.97e-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: 135.49 E-value: 7.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 445 IVGVILLYYILGVSaLIGAAVIILLAP-VQYFVATKLSQAQRStleySNERLKQTN-------EMLRGIKLLKLYAWENI 516
Cdd:TIGR02857 130 IVPLAILAAVFPQD-WISGLILLLTAPlIPIFMILIGWAAQAA----ARKQWAALSrlsghflDRLRGLPTLKLFGRAKA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 517 FRTRVETT----RRKEMTSLR-AFAIYTSISIFMNTAIPIAAVLITF---VGHVSFFKeadfspsvafaslSLFHILVTP 588
Cdd:TIGR02857 205 QAAAIRRSseeyRERTMRVLRiAFLSSAVLELFATLSVALVAVYIGFrllAGDLDLAT-------------GLFVLLLAP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 589 LFL-----LSSVVRSTVKALVSVQKLSEFLSSAEIreeQCAPHEPTPQGPASkyqavPLRVVNrkrparedcrgltgplq 663
Cdd:TIGR02857 272 EFYlplrqLGAQYHARADGVAAAEALFAVLDAAPR---PLAGKAPVTAAPAS-----SLEFSG----------------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 664 slVPSADGDADnccvqimggyftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslp 743
Cdd:TIGR02857 327 --VSVAYPGRR------------------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI------- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 744 dsEIGEDPSPERETATdldirKRGPVAYASQKPWLLNATVEENIIFESPFNKQ-RYKMVIEACSLQPDIDILPHGDQTQI 822
Cdd:TIGR02857 380 --AVNGVPLADADADS-----WRDQIAWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 823 GERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAM 902
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
684-912 |
1.53e-32 |
|
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: 126.96 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvSGAVfwssslpdsEIGedpsperetatDL 761
Cdd:cd03253 7 TFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIlrLLFRFYDVS--SGSI---------LID-----------GQ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 DIRK------RGPVAYASQKPWLLNATVEENIIFESP--FNKQrykmVIEAC---SLQPDIDILPHGDQTQIGERGINLS 830
Cdd:cd03253 64 DIREvtldslRRAIGVVPQDTVLFNDTIGYNIRYGRPdaTDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 831 GGQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 910
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
..
gi 1189438338 911 GT 912
Cdd:cd03253 217 GT 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
693-912 |
2.18e-32 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 134.49 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIgedpsperetaTDLDIRKRGP-VAY 771
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR----LDGADL-----------SQWDREELGRhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQKPWLLNATVEENIifeSPFNKQRYKMVIEACSLqpdIDI------LPHGDQTQIGERGINLSGGQRQRISVARALYQ 845
Cdd:COG4618 411 LPQDVELFDGTIAENI---ARFGDADPEKVVAAAKL---AGVhemilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 846 HANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAA--IRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1095-1538 |
1.18e-31 |
|
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: 131.71 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1095 RLHRSLLnRIILAPMRFFETtplGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVC 1174
Cdd:TIGR02868 91 RVYERLA-RQALAGRRRLRR---GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1175 YFIQKYF-----RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEV 1249
Cdd:TIGR02868 167 GFVAPLVslraaRAAEQALARLRGE----LAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1250 RMEYIGACVVLIAAVTSISNSLHRELSAG------LVGLGLTYALMVsnylnwmvrnLADMELQLGAVK----RIHGLLK 1319
Cdd:TIGR02868 243 LTLLAAGLAVLGALWAGGPAVADGRLAPVtlavlvLLPLAAFEAFAA----------LPAAAQQLTRVRaaaeRIVEVLD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1320 TEAESYEGLL-APSLIPKNWPDqgkIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTF 1398
Cdd:TIGR02868 313 AAGPVAEGSApAAGAVGLGKPT---LELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1399 EGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEG 1477
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 1478 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1538
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1013-1313 |
1.52e-31 |
|
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: 126.18 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1013 SLLVFSQLLKHMVLVAIDYWLAKWTDSaltltpaarncslSQECTLDQT-VYAMVFTVLCSLGIVLCLVTSVTVEWTGLK 1091
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDD-------------PVNGPQEHGqVYLSVLGALAILQGITVFQYSMAVSIGGIF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1092 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVAlLPLA 1171
Cdd:cd18559 69 ASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1172 IVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDsNNIASLFLTAANRWLEVRM 1251
Cdd:cd18559 148 LLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 1252 EYIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKR 1313
Cdd:cd18559 227 WCVGPCIVLFASFFAY---VSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEV 285
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
378-912 |
2.90e-31 |
|
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: 130.93 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 378 VAIETGINLRGAIQTKIYNKIMhlsTSNLSMGEMTAGQICNlvaiDTNQLMWF--------FFLCPnlWaMPVQIIVgVI 449
Cdd:TIGR01842 69 VLVRIGEKLDGALNQPIFAASF---SATLRRGSGDGLQALR----DLDQLRQFltgpglfaFFDAP--W-MPIYLLV-CF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 450 LLYYILGVSALIGAAVIILLAPV-QYFVATKLSQAQrstlEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRK- 527
Cdd:TIGR01842 138 LLHPWIGILALGGAVVLVGLALLnNRATKKPLKEAT----EASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKy 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 528 ----EMTSLRAFAIYTSISIFMNtaipIAAVLITFVG-HVSFFKEAdfSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 602
Cdd:TIGR01842 214 lsaqSAASDRAGMLSNLSKYFRI----VLQSLVLGLGaYLAIDGEI--TPGMMIAGSILVGRALAPIDGAIGGWKQFSGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 603 LVSVQKLSEFLSSAEIREEQCAPhePTPQGPaskyqavpLRVVNrkrparedcrgltgplQSLVPsadgdadnccvqimg 682
Cdd:TIGR01842 288 RQAYKRLNELLANYPSRDPAMPL--PEPEGH--------LSVEN----------------VTIVP--------------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 683 gyftwtPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdseigedpspeRETATDL 761
Cdd:TIGR01842 327 ------PGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV------------------RLDGADL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 ---DIRKRGP-VAYASQKPWLLNATVEENII-FESPFNKQRykmVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQ 833
Cdd:TIGR01842 383 kqwDRETFGKhIGYLPQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILRLPDGYDTVIGPGGATLSGGQ 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 834 RQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1341-1579 |
1.20e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 129.70 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1341 QGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSR 1420
Cdd:PRK13657 332 KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1421 LSIILQDPVLFSGTIRFNLDPERK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1499
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1500 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE---FDKpeklLSRKDSVFASF 1576
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAAL 566
|
...
gi 1189438338 1577 VRA 1579
Cdd:PRK13657 567 LRA 569
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
690-920 |
4.87e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.19 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSperetatdldiRKRGPV 769
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF--------GKPPR-----------RARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQK---PWLLNATVEE--------NIIFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRIS 838
Cdd:COG1121 78 GYVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADR-PIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIqREGTLKDFQ 917
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVReYFDRVLLLNRGLV-AHGPPEEVL 226
|
...
gi 1189438338 918 RSE 920
Cdd:COG1121 227 TPE 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
685-910 |
7.68e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssslpDSEIGEDPSPERetatdldir 764
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV-----DGKPVTGPGPDR--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 krgpvAYASQK----PWLlnaTVEENIIF------ESPfnKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSG 831
Cdd:COG1116 83 -----GVVFQEpallPWL---TVLDNVALglelrgVPK--AERRERArelLELVGLAGFEDAYPH-----------QLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 832 GQRQRISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAMKD--GT 906
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSArpGR 218
|
....
gi 1189438338 907 IQRE 910
Cdd:COG1116 219 IVEE 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
685-906 |
1.01e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 118.34 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssslPDSEIGEDPSPERetatdldir 764
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV----DGKDLTKLSLKEL--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 kRGPVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 834
Cdd:cd03225 74 -RRKVGLVFQNPddQFFGPTVEEEVAF-GLENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 835 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 906
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1088-1314 |
1.95e-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: 120.68 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1088 TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVAL 1167
Cdd:cd18600 97 TLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLAT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1168 LPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFR----YEARFQQKLLEYTdsnniASLFL-TA 1242
Cdd:cd18600 177 VPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHT-----ANWFLyLS 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 1243 ANRWLEVRMEYIgaCVVLIAAVTSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1314
Cdd:cd18600 252 TLRWFQMRIEMI--FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1344-1554 |
1.98e-29 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 117.19 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDS---SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAffrmvdtfeghiiidgiDIAKLPLH----T 1416
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSA-----------------LLGELEKLsgsvS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1417 LRSRLSIILQDPVLFSGTIRFN------LDPERkcsdstLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFC 1490
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENilfgkpFDEER------YEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1491 LARAFVRKTSIFIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILSADLVIVLKRG 1554
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
684-920 |
4.38e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 117.20 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsssLPDseiGEDpspereTATDLDI 763
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-----LVD---GHD------LALADPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKRGPVAYASQKPWLLNATVEENIIFESPFNKQRykMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVA 840
Cdd:cd03252 73 WLRRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 841 RALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
689-916 |
5.05e-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: 116.66 E-value: 5.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETatdlDIRKRgp 768
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD--------GKDITKKNLR----ELRRK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKPW--LLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 838
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEEDVAF-GPENlglpreeiRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTIQREGTLKDF 916
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
686-912 |
9.11e-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: 116.68 E-value: 9.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 686 TWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPS--PERETAtdldi 763
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD--------GRDLAslSRRELA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKrgpVAYASQK---PWLLnaTVEENII--------FESPFNKQRYKMVIEACslqpdidilphgDQTQIG---ERGIN- 828
Cdd:COG1120 75 RR---IAYVPQEppaPFGL--TVRELVAlgryphlgLFGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDe 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 829 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHlsdHlmQAGILELLRD----DKRTVVLVTHKL-QYLPHADWIIAMK 903
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLK 212
|
....*....
gi 1189438338 904 DGTIQREGT 912
Cdd:COG1120 213 DGRIVAQGP 221
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
304-609 |
1.32e-28 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 117.32 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 304 FRILADLLGFAGPLCIFGIVdhlGKENDVFQPKTQ---FLGVYFVS--SQEFLANAYvlavllflalllqrtflqasYYV 378
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLL---WFDDPVNGPQEHgqvYLSVLGALaiLQGITVFQY--------------------SMA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 379 AIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVS 458
Cdd:cd18559 62 VSIGGIFASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 459 ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIY 538
Cdd:cd18559 140 AAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 539 TSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 609
Cdd:cd18559 220 RALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
380-934 |
2.22e-28 |
|
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: 123.14 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 380 IETGINlrGAIQTKIYNKIMHL--------STSNLSMGEMTAGQICNLVAIDT-NQLMWFFFLCPNLWampvqiivgviL 450
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLG-----------L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 451 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAWENIFRTRVE 522
Cdd:TIGR03797 270 MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 523 TTRRKEMtslrafaIYTSISIFmNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 602
Cdd:TIGR03797 350 LELSAQR-------IENLLTVF-NAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAV 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 603 LVSVQKLSEFLSS-AEIREEQCAPheptpqgpaskyqavplrvvnrkrparedcrgltGPLqslvpSADGDADNCCvqim 681
Cdd:TIGR03797 422 IPLWERAKPILEAlPEVDEAKTDP----------------------------------GKL-----SGAIEVDRVT---- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 682 ggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSperetatDL 761
Cdd:TIGR03797 459 ---FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYD--------GQDLA-------GL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 DI----RKRGPVAYASQkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRI 837
Cdd:TIGR03797 521 DVqavrRQLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 838 SVARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 917
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM 672
|
570
....*....|....*..
gi 1189438338 918 RSECQLFEhwktLMNRQ 934
Cdd:TIGR03797 673 AREGLFAQ----LARRQ 685
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
673-912 |
3.41e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 121.88 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 673 ADNCCVqimggyftWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQ-----KVSGAVFwssslpdsei 747
Cdd:PRK11174 352 AEDLEI--------LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIEL---------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 748 gedpsperetaTDLDIRK-RGPVAYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGER 825
Cdd:PRK11174 414 -----------RELDPESwRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 826 GINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKrTVVLVTHKLQYLPHADWIIAMKDG 905
Cdd:PRK11174 483 AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA--LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDG 559
|
....*..
gi 1189438338 906 TIQREGT 912
Cdd:PRK11174 560 QIVQQGD 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1327-1556 |
5.64e-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: 5.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1327 GLLAPSLIpknwpdQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVDTFEGHIIID 1405
Cdd:cd03248 1 GSLAPDHL------KGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVV----ALLENFYQPQGGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1406 GIDIAK-LPLHT---LRSRLSIILQDPVLFSGTIRFNLD-PERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGEN 1480
Cdd:cd03248 71 VLLDGKpISQYEhkyLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1481 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1556
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1164-1558 |
6.10e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.97 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1164 LVALLPLAIVCYFIQKY-------FRVASRDLQQLDDTTQlpllshfaetvEGLTTIR---AFRYE----ARFQQKLLEY 1229
Cdd:PRK10789 141 LLALLPMPVMAIMIKRYgdqlherFKLAQAAFSSLNDRTQ-----------ESLTSIRmikAFGLEdrqsALFAADAEDT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1230 TDSN------------------NIASLFLTAANRWLevrmeyigacvVLIAAVTSisnslhRELSAGLVGLGLTYALMVS 1291
Cdd:PRK10789 210 GKKNmrvaridarfdptiyiaiGMANLLAIGGGSWM-----------VVNGSLTL------GQLTSFVMYLGLMIWPMLA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1292 nyLNWMVrNLadMELQLGAVKRIHGLLKTEAESYEGLLApslIPknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPG 1371
Cdd:PRK10789 273 --LAWMF-NI--VERGSAAYSRIRAMLAEAPVVKDGSEP---VP---EGRGELDVNIRQFTYPQTDHPALENVNFTLKPG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1372 QKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpERKCSDSTLW 1451
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI--ALGRPDATQQ 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1452 EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAf 1527
Cdd:PRK10789 420 EIEHVARLASVhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHNLRQWG- 498
|
410 420 430
....*....|....*....|....*....|.
gi 1189438338 1528 ADRTVVTIAHRVHTILSADLVIVLKRGAILE 1558
Cdd:PRK10789 499 EGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
695-910 |
8.39e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 112.95 E-value: 8.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsssLPDSEIGEDPSPERetatdldirkrgpvAYASQ 774
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-----LVDGEPVTGPGPDR--------------GYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 K----PWLlnaTVEENIIFesPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 841
Cdd:cd03293 81 QdallPWL---TVLDNVAL--GLElqgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 842 ALYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM--KDGTIQRE 910
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALD-ALTREQLQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
689-912 |
3.04e-27 |
|
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: 111.43 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfWSSSLPDSEIGEDpsperetatdlDIRKRgp 768
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSI-LIDGVDISKIGLH-----------DLRSR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKPWLLNATVEENIifeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 845
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 846 HANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03244 157 KSKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
695-911 |
6.75e-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: 109.06 E-value: 6.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGEDPSPERetatdldiRKRgpVAYASQ 774
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL----LDGKDLASLSPKEL--------ARK--IAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 kpwllnatveeniifespfnkqrykmVIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQRISVARALYQHANVVFLD 853
Cdd:cd03214 81 --------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 854 DPFSALDIHlsdhlMQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 911
Cdd:cd03214 123 EPTSHLDIA-----HQIELLELLRRLARergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
692-907 |
7.81e-27 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 109.89 E-value: 7.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 692 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKV-SGAVFwssslpdseI-GEDPSPERETATDLDIRKRgpV 769
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVR---------VdGTDISKLSEKELAAFRRRH--I 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLLNA-TVEENI----IFESPFNKQRYKMVIEACslqpdidilphgDQTQIGERgIN-----LSGGQRQRISV 839
Cdd:cd03255 85 GFVFQSFNLLPDlTALENVelplLLAGVPKKERRERAEELL------------ERVGLGDR-LNhypseLSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
695-919 |
1.32e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.15 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPEREtatdlDIRKRgpVAYASQ 774
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL--------GEDVARDPA-----EVRRR--IGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWL-LNATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARALYQH 846
Cdd:COG1131 81 EPALyPDLTVRENLRFfarlyglPRKEARERIDELLELFGLTDAAD-------RKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKDFQRS 919
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
685-911 |
1.95e-26 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 108.76 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLDIR 764
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID--------GRD-------VTGVPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 KRGpVAYASQK----PWLlnaTVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQ 833
Cdd:cd03259 71 RRN-IGMVFQDyalfPHL---TVAENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 834 RQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 911
Cdd:cd03259 136 QQRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
685-907 |
1.98e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.75 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpDSEIGEDPSPEretatdldIR 764
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD----GKPLSAMPPPE--------WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 KRgpVAYASQKPWLLNATVEENIIF-----ESPFNKQRYKMVIEACSLQPDIdiLphgdQTQIGErginLSGGQRQRISV 839
Cdd:COG4619 74 RQ--VAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI--L----DKPVER----LSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEEL-LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
695-920 |
2.41e-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: 109.13 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETAtDLDIRKRgpVAYASQ 774
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID--------GEDISGLSEAE-LYRLRRR--MGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLLNA-TVEENIIFesPFN----------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARAL 843
Cdd:cd03261 85 SGALFDSlTVFENVAF--PLRehtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQR 918
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASG-----VIDDLIRSLKKelglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
..
gi 1189438338 919 SE 920
Cdd:cd03261 227 SD 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
693-912 |
2.54e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 115.97 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAV-FWSSSLPDSEIGEdpsperetatdldirKRGPVAY 771
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrFHDIPLTKLQLDS---------------WRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 850
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 851 FLDDPFSALDIHlSDHlmqaGILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK10789 474 ILDDALSAVDGR-TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
690-903 |
6.41e-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: 107.23 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSperetatdldiRKRGPV 769
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF--------GKPLE-----------KERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQK---PWLLNATVEE--------NIIFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRIS 838
Cdd:cd03235 71 GYVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALER---VGLSELADR-QIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHlsdhlMQAGILEL---LRDDKRTVVLVTHKL-QYLPHADWIIAMK 903
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPK-----TQEDIYELlreLRREGMTILVVTHDLgLVLEYFDRVLLLN 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
388-890 |
6.85e-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: 113.99 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 388 GAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVA--IDTNQLMWFFFLCPNLWAMPVQIIV--GVILLYYILGVSALIGA 463
Cdd:TIGR02868 86 GALRVRVYERLARQALA--GRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVGAAAvaAIAVLSVPAALILAAGL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 464 AVIILLAPvqyFVATKLSQAQRSTLEYS-NERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSIS 542
Cdd:TIGR02868 164 LLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 543 ifmnTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLF----LLSSVVRSTVKALVSVQKLSEFLSSAei 618
Cdd:TIGR02868 241 ----AALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeafaALPAAAQQLTRVRAAAERIVEVLDAA-- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 619 reeqcaPHEPTPQGPASKyqavplrvvnrkrparedcrgltgplqslvPSADGDADNCCVQIMGGYftwtPDGIPTLSNI 698
Cdd:TIGR02868 315 ------GPVAEGSAPAAG------------------------------AVGLGKPTLELRDLSAGY----PGAPPVLDGV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 699 TIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETatdlDIRKRgpVAYASQKPWL 778
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD--------GVPVSSLDQD----EVRRR--VSVCAQDAHL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 779 LNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFS 857
Cdd:TIGR02868 421 FDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
490 500 510
....*....|....*....|....*....|....*
gi 1189438338 858 ALDIHLSDHLmqagiLELLRD--DKRTVVLVTHKL 890
Cdd:TIGR02868 501 HLDAETADEL-----LEDLLAalSGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1344-1558 |
8.09e-26 |
|
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: 105.86 E-value: 8.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPlHTLRSRLSI 1423
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPVLFSGTIRFNLdperkcsdstlwealeiaqlklvvkalpggldaiitegGENFSQGQRQLFCLARAFVRKTSIFI 1503
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 1504 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE 1558
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
685-915 |
1.43e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.58 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKvsgavfwssslpdSEIGEDPSPERE-TATDL 761
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDIDE-------------GEILLDGHDLRDyTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 dirkRGPVAYASQKPWLLNATVEENIIFESpfnKQRY--KMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQR 836
Cdd:PRK11176 416 ----RNQVALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
444-912 |
1.67e-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: 113.26 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 444 IIVGVILLYYILGV--SALIGAAVIILLAPVqYFVATKLSQAQRStleySNERLKQTN----EMLRGIKLLKLYAWENIF 517
Cdd:TIGR02204 145 MCIGGLIMMFITSPklTSLVLLAVPLVLLPI-LLFGRRVRKLSRE----SQDRIADAGsyagETLGAIRTVQAFGHEDAE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 518 RTR----VETTRRKEMTSLRAFAIYTSISIFMNTAipiAAVLITFVGhVSFFKEADFSPSV--AFASLSLFhiLVTPLFL 591
Cdd:TIGR02204 220 RSRfggaVEKAYEAARQRIRTRALLTAIVIVLVFG---AIVGVLWVG-AHDVIAGKMSAGTlgQFVFYAVM--VAGSIGT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 592 LSSVVRSTVKALVSVQKLSEFLssaEIREEQCAPhePTPQGPASKYQA-VPLRVVNRKRPAREDcrgltgplqslvpsad 670
Cdd:TIGR02204 294 LSEVWGELQRAAGAAERLIELL---QAEPDIKAP--AHPKTLPVPLRGeIEFEQVNFAYPARPD---------------- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 671 gdadnccvqimggyftwtpdgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssslpdseigeD 750
Cdd:TIGR02204 353 ---------------------QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL-----------D 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 751 PSPERETATDlDIRKRgpVAYASQKPWLLNATVEENIIFESPfnKQRYKMVIEAC-SLQPD--IDILPHGDQTQIGERGI 827
Cdd:TIGR02204 401 GVDLRQLDPA-ELRAR--MALVPQDPVLFAASVMENIRYGRP--DATDEEVEAAArAAHAHefISALPEGYDTYLGERGV 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 828 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:TIGR02204 476 TLSGGQRQRIAIARAILKDAPILLLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRI 552
|
....*
gi 1189438338 908 QREGT 912
Cdd:TIGR02204 553 VAQGT 557
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1344-1579 |
2.71e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 113.02 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVR-YDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF------------SLaffrMVDTFEGhiiidgidiA 1410
Cdd:PRK11174 350 IEAEDLEILsPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSLlnallgflpyqgSL----KINGIEL---------R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1411 KLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQ 1487
Cdd:PRK11174 415 ELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1488 LFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE---FDKpek 1564
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE--- 569
|
250
....*....|....*
gi 1189438338 1565 lLSRKDSVFASFVRA 1579
Cdd:PRK11174 570 -LSQAGGLFATLLAH 583
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
685-920 |
4.56e-25 |
|
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: 112.91 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKvsGAVfwsssLPDS-EIGE-DPSPERetatd 760
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQH--GQV-----LVDGvDLAIaDPAWLR----- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 761 ldiRKRGPVAyasQKPWLLNATVEENIIFESPfnKQRYKMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRI 837
Cdd:TIGR01846 531 ---RQMGVVL---QENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRI 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 838 SVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 917
Cdd:TIGR01846 603 AIARALVGNPRILIFDEATSALDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELL 679
|
...
gi 1189438338 918 RSE 920
Cdd:TIGR01846 680 ALQ 682
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1344-1556 |
9.81e-25 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 102.68 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdtfeghiiidgidiAKLPLHTLRsrlsi 1423
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTL----------------------ARLILGLLR----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ilqdPVlfSGTIRfnLDperkCSDSTLWEALEIAQLklvVKALPGglDAIITEG--GEN-FSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03246 54 ----PT--SGRVR--LD----GADISQWDPNELGDH---VGYLPQ--DDELFSGsiAENiLSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 1501 IFIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1556
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1339-1570 |
1.77e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.30 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1339 PDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSS-FSLAffrmvdTFEGHIIIDGIDIAKLPLH-- 1415
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTlLQLL------TRAWDPQQGEILLNGQPIAdy 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1416 ---TLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQL-KLVvkALPGGLDAIITEGGENFSQGQRQL 1488
Cdd:PRK11160 408 seaALRQAISVVSQRVHLFSATLRDNLllaAPN--ASDEALIEVLQQVGLeKLL--EDDKGLNAWLGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1489 FCLARAFVRKTSIFIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
...
gi 1189438338 1568 RKD 1570
Cdd:PRK11160 563 QQG 565
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
692-911 |
5.62e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 102.20 E-value: 5.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 692 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETatDLDIRkRGPVAY 771
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD--------GKDLLKLSRR--LRKIR-RKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQKPWL-LNA--TVEENI-----IFESPFNKQRYKMVI--EACSLQPDIDIL---PHGdqtqigerginLSGGQRQRIS 838
Cdd:cd03257 87 VFQDPMSsLNPrmTIGEQIaeplrIHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKDGTIQREG 911
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKLQEelglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
684-912 |
7.66e-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: 107.68 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETATdLDI 763
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD--------GKDLTKLSRRSL-REL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKR-GPV---AYASqkpwlLNA--TVEEnIIFESPFN------KQRYKMV---IEACSLQPD-IDILPHGdqtqigergi 827
Cdd:COG1123 341 RRRvQMVfqdPYSS-----LNPrmTVGD-IIAEPLRLhgllsrAERRERVaelLERVGLPPDlADRYPHE---------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 828 nLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWII 900
Cdd:COG1123 405 -LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvRYI--ADRVA 476
|
250
....*....|..
gi 1189438338 901 AMKDGTIQREGT 912
Cdd:COG1123 477 VMYDGRIVEDGP 488
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
692-910 |
1.40e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 100.89 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 692 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKV-SGAVFWSsslpDSEIGEDPSPEREtatdlDIRKRgPVA 770
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVLID----GQDISSLSERELA-----RLRRR-HIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLL-NATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 842
Cdd:COG1136 90 FVFQFFNLLpELTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 843 LYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 910
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
691-906 |
2.22e-23 |
|
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: 98.09 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpDSEIGEDPSPERetatdldirkRGPVA 770
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID----GKDIAKLPLEEL----------RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVV 850
Cdd:cd00267 77 YVPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 851 FLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 906
Cdd:cd00267 103 LLDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
691-915 |
2.27e-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: 107.52 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwssslpdsEIGEDPSPeretATDLDIRK-RGPV 769
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSG-----------EILLNGFS----LKDIDRHTlRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLLNATVEENIIFESPFNKQRyKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 847 ANVVFLDDPFSALDIhlsdhLMQAGILE-LLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:TIGR01193 630 SKVLILDESTSNLDT-----ITEKKIVNnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1204-1568 |
4.33e-23 |
|
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: 105.60 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1204 AETVEGLTTIRAFRyeARFQQKLLEYTDSNNIASL---FLTAANRWLEVRMEYI----GACVVLiaavtsisnslHRELS 1276
Cdd:COG4618 204 AEVIEAMGMLPALR--RRWQRANARALALQARASDragGFSALSKFLRLLLQSAvlglGAYLVI-----------QGEIT 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1277 AGlvglgltyALMVSNYLnwMVRNLADMELQLG----------AVKRIHGLLKTEAESYEGLLAPslipknwPDQGKIQI 1346
Cdd:COG4618 271 PG--------AMIAASIL--MGRALAPIEQAIGgwkqfvsarqAYRRLNELLAAVPAEPERMPLP-------RPKGRLSV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1347 QNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdtfeghiiidgidiAKL-------------- 1412
Cdd:COG4618 334 ENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTL----------------------ARLlvgvwpptagsvrl 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1413 ---PLHTL-RSRLSIIL----QDPVLFSGTI-----RF-NLDPERkcsdstlweALEIAQL----KLVVKaLPGGLDAII 1474
Cdd:COG4618 392 dgaDLSQWdREELGRHIgylpQDVELFDGTIaeniaRFgDADPEK---------VVAAAKLagvhEMILR-LPDGYDTRI 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1475 TEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILSADLVIVLKR 1553
Cdd:COG4618 462 GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRD 541
|
410
....*....|....*
gi 1189438338 1554 GAILEFDKPEKLLSR 1568
Cdd:COG4618 542 GRVQAFGPRDEVLAR 556
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
685-919 |
5.90e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 99.88 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETATdldir 764
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD--------GRPVTRRRRKAF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 kRGPVAYASQKPWL-LNA--TVEENI-----IFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtQigerginLSGGQRQ 835
Cdd:COG1124 78 -RRRVQMVFQDPYAsLHPrhTVDRILaeplrIHGLPDREERIAELLEQVGLPPSFlDRYPH----Q-------LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 836 RISVARALYQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 910
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEE 220
|
....*....
gi 1189438338 911 GTLKDFQRS 919
Cdd:COG1124 221 LTVADLLAG 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
693-907 |
8.23e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 96.90 E-value: 8.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsssLPDseiGEDPSPERETAtdldirKRGPVAYA 772
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----RLD---GADISQWDPNE------LGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVVFL 852
Cdd:cd03246 82 PQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 853 DDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03246 121 DEPNSHLDVEGERALNQA--IAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
689-917 |
1.47e-22 |
|
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: 98.41 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpDSEIGEDPSPEretatdldIRK-RG 767
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID----GTDINKLKGKA--------LRQlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 PVAYASQKPWLLN-ATVEENI---------IFESPFN------KQRykmvieACSLQPDIDILPHGDQtqigeRGINLSG 831
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVlsgrlgrrsTWRSLFGlfpkeeKQR------ALAALERVGLLDKAYQ-----RADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 832 GQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQRE 910
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL-LKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFD 226
|
....*..
gi 1189438338 911 GTLKDFQ 917
Cdd:cd03256 227 GPPAELT 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
689-919 |
2.01e-22 |
|
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: 98.14 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLD-IRKRG 767
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID--------GED-------IREQDpVELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 PVAYASQKPWLL-NATVEENII-------FESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRI 837
Cdd:cd03295 76 KIGYVIQQIGLFpHMTVEENIAlvpkllkWPKEKIRERADELLALVGLDPAefADRYPH-----------ELSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 838 SVARALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDF 916
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEI 223
|
...
gi 1189438338 917 QRS 919
Cdd:cd03295 224 LRS 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
695-857 |
2.12e-22 |
|
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: 95.02 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETATdldirkRGPVAYASQ 774
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD--------GQDLTDDERKSL------RKEIGYVFQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLLNA-TVEENIIFESPFnKQRYKMVIEAcslQPDIDI----LPHGDQTQIGERGINLSGGQRQRISVARALYQHANV 849
Cdd:pfam00005 67 DPQLFPRlTVRENLRLGLLL-KGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKL 142
|
....*...
gi 1189438338 850 VFLDDPFS 857
Cdd:pfam00005 143 LLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
685-911 |
3.97e-22 |
|
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: 95.07 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETATDLdir 764
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD--------GVPVSDLEKALSSL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 krgpVAYASQKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALY 844
Cdd:cd03247 77 ----ISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 845 QHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 911
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSL-IFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1344-1568 |
8.38e-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: 101.13 E-value: 8.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD---TFEGHIIIDGIDIAKLPLHTLRSR 1420
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1421 LSIILQDP--VLFSGTIRFNLD--PERKCSDSTLWEALEIAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFV 1496
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1497 RKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1568
Cdd:COG1123 159 LDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
695-907 |
1.66e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 93.23 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPEREtatdlDIRKRgpVAYASQ 774
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL--------GKDIKKEPE-----EVKRR--IGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLL-NATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHANVVFLD 853
Cdd:cd03230 81 EPSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 854 DPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:cd03230 121 EPTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1344-1570 |
1.82e-21 |
|
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: 94.71 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAF------------FRMVDTfeghiiidgidiAK 1411
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsgevlVDGKDI------------TK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1412 LPLHTLRSRLSIILQDPV--LFSGTIR---------FNLDPErkcsdstlwEALEIAQ--LKLVvkalpgGLDAIITEGG 1478
Cdd:COG1122 68 KNLRELRRKVGLVFQNPDdqLFAPTVEedvafgpenLGLPRE---------EIRERVEeaLELV------GLEHLADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1556
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
250
....*....|....
gi 1189438338 1557 LEFDKPEKLLSRKD 1570
Cdd:COG1122 213 VADGTPREVFSDYE 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
690-912 |
2.67e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.45 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFWssslpDseiGEDpsperetATDLDIRKRG 767
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrmIAGLEDPT--SGEILI-----G---GRD-------VTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 pVAYASQKPWLL-NATVEENIIF------ESPfnKQRYKMVIEAcslqpdIDILphgdqtQIGE----RGINLSGGQRQR 836
Cdd:COG3839 77 -IAMVFQSYALYpHMTVYENIAFplklrkVPK--AEIDRRVREA------AELL------GLEDlldrKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQRE 910
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVE-MRAEIKRLHRRLGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQV 215
|
..
gi 1189438338 911 GT 912
Cdd:COG3839 216 GT 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
693-920 |
4.15e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.38 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIGEDPSpeRETATDLDIRKrgpvaya 772
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEV----LVDGLDVATTPS--RELAKRLAILR------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 sQKPWL-LNATVEENIIF-ESPFNKQR-----YKMVIEAcslqpdIDILphgDQTQIGERGIN-LSGGQRQRISVARALY 844
Cdd:COG4604 82 -QENHInSRLTVRELVAFgRFPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 845 QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDK-RTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
689-907 |
4.35e-21 |
|
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: 93.69 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvsgavfwssslpDSEIGEDPSPeretATDLDIRK- 765
Cdd:cd03248 25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQ-------------GGQVLLDGKP----ISQYEHKYl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 RGPVAYASQKPWLLNATVEENIIFESPfnKQRYKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 842
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 843 LYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03248 165 LIRNPQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1345-1554 |
5.86e-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: 91.15 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1345 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSII 1424
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1425 LQdpvlfsgtirfnldperkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFIM 1504
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 1505 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTI-LSADLVIVLKRG 1554
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
811-1581 |
7.26e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 100.10 E-value: 7.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 811 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKL 890
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 891 QYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVTERKATEPP----QGLSRA-MSSRDGL 965
Cdd:PTZ00265 641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSyiieQGTHDAlMKNKNGI 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 966 -----------------------------------------------LQDEEEEEEEAAESEEDDNLSS----------- 987
Cdd:PTZ00265 721 yytminnqkvsskkssnndndkdsdmkssaykdsergydpdemngnsKHENESASNKKSCKMSDENASEnnaggklpflr 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 988 -MLHQRAEIP------WRACAKYLSSAGILLLSLLVFSQLLKhmvLVAIDYwlAKWTDSALTLTPAARNCSlsqectlDQ 1060
Cdd:PTZ00265 801 nLFKRKPKAPnnlrivYREIFSYKKDVTIIALSILVAGGLYP---VFALLY--AKYVSTLFDFANLEANSN-------KY 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1061 TVYAMVftvlcslgIVLCLVTSVTVE-----WTGLKVAKRLHRSLLNRIILAPMRFFEttplgsilnrfsSDCNT---ID 1132
Cdd:PTZ00265 869 SLYILV--------IAIAMFISETLKnyynnVIGEKVEKTMKRRLFENILYQEISFFD------------QDKHApglLS 928
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1133 QHIPSTLECLSRSTllcVSALAVISYVTPVFLVALLplaivcyfIQKYFrvasrdlqqlddttqLPLLshfAETVEGLTT 1212
Cdd:PTZ00265 929 AHINRDVHLLKTGL---VNNIVIFTHFIVLFLVSMV--------MSFYF---------------CPIV---AAVLTGTYF 979
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1213 I--RAFRYEARF-QQKLLEYTDSNNIASLFL-----------------------TAANRWLEvrmEYIgaCVVLIAAVTS 1266
Cdd:PTZ00265 980 IfmRVFAIRARLtANKDVEKKEINQPGTVFAynsddeifkdpsfliqeafynmnTVIIYGLE---DYF--CNLIEKAIDY 1054
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1267 ISNSLHRE--LSAGLVGLGLTYALMVSNYLNW----MVRN----LADMELQL----------GAVKRIHGLLKTEAESYE 1326
Cdd:PTZ00265 1055 SNKGQKRKtlVNSMLWGFSQSAQLFINSFAYWfgsfLIRRgtilVDDFMKSLftflftgsyaGKLMSLKGDSENAKLSFE 1134
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1327 G----LLAPSLIP---------KNWPD-QGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAF 1391
Cdd:PTZ00265 1135 KyyplIIRKSNIDvrdnggiriKNKNDiKGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLL 1214
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1392 FRMVD-------------------------------------TFEGHIIIDGIDIAKL-----------------PLHTL 1417
Cdd:PTZ00265 1215 MRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnEFSLTKEGGSGEDSTVfknsgkilldgvdicdyNLKDL 1294
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1418 RSRLSIILQDPVLFSGTIRFNLDPERKcsDSTLWE---ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARA 1494
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENIKFGKE--DATREDvkrACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1495 FVRKTSIFIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL----KRGAILEFDKP-EKLLS 1567
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAHGThEELLS 1452
|
970
....*....|....
gi 1189438338 1568 RKDSVFASFVRADK 1581
Cdd:PTZ00265 1453 VQDGVYKKYVKLAK 1466
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
690-922 |
1.11e-20 |
|
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: 93.00 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETAtdldiRKRgpV 769
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID--------GEDVRKEPREA-----RRQ--I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWL-LNATVEENIIFESPFN-------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVAR 841
Cdd:COG4555 77 GVLPDERGLyDRLTVRENIRYFAELYglfdeelKKRIEELIELLGLEEFLDRRVGE-----------LSTGMKKKVALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 842 ALYQHANVVFLDDPFSALDIhLSDHLMQaGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDV-MARRLLR-EILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEI 223
|
..
gi 1189438338 921 CQ 922
Cdd:COG4555 224 GE 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
691-906 |
1.57e-20 |
|
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: 90.71 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPDSEIGEDPSPERetatdldirkrgPVA 770
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR------------RIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLL-NATVEENIIFespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHANV 849
Cdd:cd03229 80 MVFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 850 VFLDDPFSALDIhlsdhLMQAGILELLRD----DKRTVVLVTHKLQYLPH-ADWIIAMKDGT 906
Cdd:cd03229 122 LLLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
685-923 |
1.73e-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: 97.28 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALG---EMQKVSGAVFWSsslpdseiGEDPsperetaTDL 761
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLD--------GRDL-------LEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 DIRKRGP-VAYASQKPW--LLNATVEENIIfESPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLS 830
Cdd:COG1123 77 SEALRGRrIGMVFQDPMtqLNPVTVGDQIA-EALENlglsraeaRARVLELLEAVGLERRLDRYPH-----------QLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 831 GGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQY-LPHADWIIAMKDG 905
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDVTT-----QAEILDLLRELQRergtTVLLITHDLGVvAEIADRVVVMDDG 219
|
250
....*....|....*...
gi 1189438338 906 TIQREGTLKDFQRSECQL 923
Cdd:COG1123 220 RIVEDGPPEEILAAPQAL 237
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
695-926 |
2.97e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 94.06 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgEMQKvSGAVFWSsslpdseiGEDpspereTATDLDIRKRGpVAYA 772
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLriIAGL-ETPD-SGRIVLN--------GRD------LFTNLPPRERR-VGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKPWLL-NATVEENIIF----ESPFNKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 844
Cdd:COG1118 81 FQHYALFpHMTVAENIAFglrvRPPSKAEIRARVeelLELVQLEGLADRYPS-----------QLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 845 QHANVVFLDDPFSALDIHLSDHLMQaGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDfqrsecqL 923
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRR-WLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDE-------V 221
|
...
gi 1189438338 924 FEH 926
Cdd:COG1118 222 YDR 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1344-1568 |
3.11e-20 |
|
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: 91.84 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEG----HIIIDGIDIAKLPLHtLRS 1419
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMLAGLLKpdsgSILIDGEDVRKEPRE-ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1420 RLSIILQDPVLFSG-TIRFNLD---PERKCSDSTLWEALEIaqlklVVKALpgGLDAIITEGGENFSQGQRQLFCLARAF 1495
Cdd:COG4555 75 QIGVLPDERGLYDRlTVRENIRyfaELYGLFDEELKKRIEE-----LIELL--GLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 1496 VRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1568
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
687-907 |
3.32e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 90.55 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 687 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIGEDPsperetATDLdirkR 766
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI----EIDGIDISTIP------LEDL----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GPVAYASQKPWLLNATVEENIifeSPFNKQRYKMVIEACSlqpdidilphgdqtqIGERGINLSGGQRQRISVARALYQH 846
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 847 ANVVFLDDPFSALDIHlSDHLMQAGILELLRDDkrTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03369 144 PRVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
695-920 |
5.32e-20 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 90.81 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETATDlDIRKRgpVAYASQ 774
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD--------GQDITGLSEKELY-ELRRR--IGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLLNA-TVEENIIFesPFN----------KQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARAL 843
Cdd:COG1127 90 GGALFDSlTVFENVAF--PLRehtdlseaeiRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 844 YQHANVVFLDDPFSALDIHLS---DHLmqagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSaviDEL----IRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
.
gi 1189438338 920 E 920
Cdd:COG1127 233 D 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1344-1565 |
8.03e-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: 89.93 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHII--------IDGIDIAKLPLH 1415
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDegevlldgKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1416 tLRSRLSIILQDPVLFSGTIRFNLD--------PERKCSDSTLWEALEIAQLKLVVKALPGGLDaiiteggenFSQGQRQ 1487
Cdd:cd03260 79 -LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1488 LFCLARAFVRKTSIFIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKL 1565
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1345-1554 |
2.62e-19 |
|
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: 87.91 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1345 QIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSII 1424
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1425 LQDP--VLFSGTIR----FNLdPERKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRK 1498
Cdd:cd03225 81 FQNPddQFFGPTVEeevaFGL-ENLGLPEEEIEERVEEA-LELV------GLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1499 TSIFIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILS-ADLVIVLKRG 1554
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
695-891 |
5.10e-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: 87.62 E-value: 5.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFWSsslpdseiGEDPSPERETATDLdiRKRgpV 769
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLD--------GKDIYDLDVDVLEL--RRR--V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLLNATVEENI-----IFESPFNKQRYKMVIEACS---LQPDIDILPHGDQtqigerginLSGGQRQRISVAR 841
Cdd:cd03260 84 GMVFQKPNPFPGSIYDNVayglrLHGIKLKEELDERVEEALRkaaLWDEVKDRLHALG---------LSGGQQQRLCLAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189438338 842 ALYQHANVVFLDDPFSALDIHlSDHLMQAGILELlrDDKRTVVLVTHKLQ 891
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQ 201
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
690-890 |
9.37e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdseigedpspERETATdldirkrgPV 769
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------------RRAGGA--------RV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQK---PWLLNATVEENIIF-----ESPFNKQRY--KMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISV 839
Cdd:NF040873 58 AYVPQRsevPDSLPLTVRDLVAMgrwarRGLWRRLTRddRAAVDDALERVGLADLAG---RQLGE----LSGGQRQRALL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLSDHLmqAGILELLRDDKRTVVLVTHKL 890
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDL 179
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
685-925 |
9.61e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 9.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPDSEIGEdpsperetatdlDIR 764
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE------------KLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 KRGPVAYASQKPWLLNATVEENIIFESPFNKQRY-KMVIEACSLQPDIDILPHGD-QTQigergiNLSGGQRQRISVARA 842
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYdEMHRRVSEALKQVDMLERADyEPN------ALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 843 LYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQ 922
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
...
gi 1189438338 923 LFE 925
Cdd:PRK13648 236 LTR 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
689-914 |
1.72e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 91.71 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsssLPDSEigedPSPERETATdldIRKRgp 768
Cdd:TIGR00958 492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-----LLDGV----PLVQYDHHY---LHRQ-- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKPWLLNATVEENIIFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHA 847
Cdd:TIGR00958 557 VALVGQEPVLFSGSVRENIAYGLTDTPDEEIMaAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 848 NVVFLDDPFSALDIHlSDHLMQagilELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 914
Cdd:TIGR00958 637 RVLILDEATSALDAE-CEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
695-888 |
1.77e-18 |
|
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: 85.61 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETAtdldirkRGPVAYASQ 774
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN--------GEPIRDAREDY-------RRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLLNA-TVEENIIF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHAN 848
Cdd:COG4133 83 ADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438338 849 VVFLDDPFSALDIHLSDHLmqAGILELLRDDKRTVVLVTH 888
Cdd:COG4133 152 LWLLDEPFTALDAAGVALL--AELIAAHLARGGAVLLTTH 189
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
690-915 |
5.85e-18 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 84.60 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIgedpsperetaTDLDIRKRgPV 769
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL----LDGKDI-----------TNLPPHKR-PV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLL-NATVEENIIF-----ESPFNKQRYKmVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRISVARA 842
Cdd:cd03300 75 NTVFQNYALFpHLTVFENIAFglrlkKLPKAEIKER-VAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 843 LYQHANVVFLDDPFSALDIHLSDHlMQagiLELLRDDKR---TVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKD-MQ---LELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
690-911 |
5.92e-18 |
|
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: 84.23 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFwssslpdseIGEdpsperETATDLDIRKRG 767
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLrmIAGLEEPT--SGRIY---------IGG------RDVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 pVAYASQKPWLL-NATVEENIIFESPFNKQRyKMVIE------ACSLQpdIDILPHGDQTQigerginLSGGQRQRISVA 840
Cdd:cd03301 74 -IAMVFQNYALYpHMTVYDNIAFGLKLRKVP-KDEIDervrevAELLQ--IEHLLDRKPKQ-------LSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 841 RALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 911
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
690-912 |
7.05e-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: 87.08 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLDIRKRgPV 769
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD--------GRD-------VTGLPPEKR-NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQK----PWLlnaTVEENIIF------ESPfnKQRYKMVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRIS 838
Cdd:COG3842 80 GMVFQDyalfPHL---TVAENVAFglrmrgVPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 839 VARALyqhAN---VVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKlQY--LPHADWIIAMKDGTIQREGT 912
Cdd:COG3842 146 LARAL---APeprVLLLDEPLSALDAKLREE-MREELRRLQRELGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
684-912 |
1.09e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemQKVSGAvfWSsslPDS-EI---GEDPSPERETAT 759
Cdd:PRK11160 345 SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL-------QLLTRA--WD---PQQgEIllnGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 760 dldirkRGPVAYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDIlPHGDQTQIGERGINLSGGQRQRIS 838
Cdd:PRK11160 413 ------RQAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLSDHlmqagILELLRD---DKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQ-----ILELLAEhaqNK-TVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
690-912 |
1.36e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 83.93 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLDIRKRGpV 769
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG--------GED-------ATDVPVQERN-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLL-NATVEENIIF--------ESPFN---KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 837
Cdd:cd03296 77 GFVFQHYALFrHMTVFDNVAFglrvkprsERPPEaeiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 838 SVARALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKEL-RRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
693-912 |
1.44e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 88.34 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvSGAVFwssslpdseIGedpsperetatDLDIRKrgpVA 770
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRIL---------ID-----------GQDIRD---VT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YAS---------QKPWLLNATVEENIIFESPFNKQRykMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRIS 838
Cdd:COG5265 427 QASlraaigivpQDTVLFNDTIAYNIAYGRPDASEE--EVEAAaraAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSR-TERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
690-902 |
1.51e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDP---SPERetatdldirKR 766
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE--------GEDIstlKPEI---------YR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQ----PDidilphgdqtQIGERGIN-LSGGQRQRISVAR 841
Cdd:PRK10247 81 QQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLErfalPD----------TILTKNIAeLSGGEKQRISLIR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 842 ALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 902
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
695-946 |
1.87e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAV-FWSSSLPDSEIgeDPSperetatdlDIRKRgp 768
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVtFHGKNLYAPDV--DPV---------EVRRR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKPWLLNATVEENIIFESPFNKQRYKM--VIEACSLQPdidILPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIAYGARINGYKGDMdeLVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 847 ANVVFLDDPFSALdihlsDHLMQAGILELLRDDKR--TVVLVTHKLQYLPHADWIIAM----KDGTIQREGTLKDFQRSE 920
Cdd:PRK14243 170 PEVILMDEPCSAL-----DPISTLRIEELMHELKEqyTIIIVTHNMQQAARVSDMTAFfnveLTEGGGRYGYLVEFDRTE 244
|
250 260
....*....|....*....|....*.
gi 1189438338 921 cqlfehwkTLMNRQDQELEKETVTER 946
Cdd:PRK14243 245 --------KIFNSPQQQATRDYVSGR 262
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
689-888 |
2.03e-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: 82.84 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETATDLDIRKRGp 768
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN--------GQDVSDLRGRAIPYLRRKIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKpWLLNATVEENIIF------ESPFN-KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVAR 841
Cdd:cd03292 82 VVFQDFR-LLPDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189438338 842 ALYQHANVVFLDDPFSALDihlSDHlmQAGILELLRD-DKR--TVVLVTH 888
Cdd:cd03292 150 AIVNSPTILIADEPTGNLD---PDT--TWEIMNLLKKiNKAgtTVVVATH 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
705-911 |
2.28e-17 |
|
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: 82.73 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 705 GQLTMIVGQVGCGKSSLLLAALGeMQKVSGA--VFWSSSLPDSEIGEDPSPERetatdldiRKrgpVAYASQKPWLL-NA 781
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAG-LEKPDGGtiVLNGTVLFDSRKKINLPPQQ--------RK---IGLVFQQYALFpHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 782 TVEENIIFESPFNKQRYKMVIEAcslqpdiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHANVVFLDDPFSALD 860
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 861 IHLSDHLMQAgILELLRDDKRTVVLVTHKL---QYLphADWIIAMKDGTIQREG 911
Cdd:cd03297 164 RALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
678-912 |
2.42e-17 |
|
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: 88.08 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 678 VQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALgeMQKVSGAVFWssslpDSEIGEDPSPER 755
Cdd:TIGR03796 478 VELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIakLVAGL--YQPWSGEILF-----DGIPREEIPREV 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 756 ETATdldirkrgpVAYASQKPWLLNATVEENIIFESPFNKQryKMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGG 832
Cdd:TIGR03796 551 LANS---------VAMVDQDIFLFEGTVRDNLTLWDPTIPD--ADLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGG 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 833 QRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:TIGR03796 620 QRQRLEIARALVRNPSILILDEATSALDP-----ETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
695-920 |
3.28e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.92 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdsEIGEDPSPERETATDL-DIRKRgpVAYAS 773
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV---------TIGERVITAGKKNKKLkPLRKK--VGIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 QKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARAL 843
Cdd:PRK13634 92 QFPehQLFEETVEKDICF-GPMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLKD-FQR 918
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEM-FYKLHKEKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREiFAD 236
|
..
gi 1189438338 919 SE 920
Cdd:PRK13634 237 PD 238
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
695-912 |
3.56e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVF------WSSS----------LPDseigEDPSPEreta 758
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpiSMLSsrqlarrlalLPQ----HHLTPE---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 759 tdlDIRKRGPVAYAsQKPWL-----LnatveeniifeSPFNKQRYKMVIEacslqpdidilphgdQTQIGE----RGINL 829
Cdd:PRK11231 90 ---GITVRELVAYG-RSPWLslwgrL-----------SAEDNARVNQAME---------------QTRINHladrRLTDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 830 SGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQ 908
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVM 217
|
....
gi 1189438338 909 REGT 912
Cdd:PRK11231 218 AQGT 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
688-906 |
4.28e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.78 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAAL---GemqkvSGAVfwssSLPDSEigedpsperetatdld 762
Cdd:COG4178 372 TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLraIAGLwpyG-----SGRI----ARPAGA---------------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 763 irkrgPVAYASQKPWLLNATVEENIIF---ESPFNKQRYKMVIEACSLQpdiDILPHGDQTQIGERGinLSGGQRQRISV 839
Cdd:COG4178 427 -----RVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLG---HLAERLDEEADWDQV--LSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGT 906
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--TTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1361-1509 |
5.38e-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: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1361 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL 1439
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1440 DPERKC---SDSTLWEALEIAQLKLvvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1509
Cdd:pfam00005 81 RLGLLLkglSKREKDARAEEALEKL---GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1344-1555 |
5.62e-17 |
|
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: 81.61 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHI--IIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIIL--QDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1499
Cdd:cd03290 80 SVAYaaQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1500 SIFIMDEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVIVLKRGA 1555
Cdd:cd03290 160 NIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
694-920 |
9.35e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.34 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 694 TLSNITIR-----------IPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLD 762
Cdd:COG3840 3 RLDDLTYRygdfplrfdltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN--------GQD-------LTALP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 763 IRKRgPVAYASQK----PWLlnaTVEENIIFE-------SPFNKQRYKMVIEACSLQPDIDILPhgDQtqigerginLSG 831
Cdd:COG3840 68 PAER-PVSMLFQEnnlfPHL---TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 832 GQRQRISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQRE 910
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQE-MLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAAD 211
|
250
....*....|
gi 1189438338 911 GTLKDFQRSE 920
Cdd:COG3840 212 GPTAALLDGE 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1336-1551 |
9.91e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.62 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1336 KNWPDQGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAK-LP 1413
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1414 LHTLRSRLSIILQDPVLFSGTIRFN----------------------------LDPERKC--------------SDSTLW 1451
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdlealsnyynedgndsqenKNKRNSCrakcagdlndmsntTDSNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1452 -------------EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1515
Cdd:PTZ00265 535 iemrknyqtikdsEVVDVSKKVLIhdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270
....*....|....*....|....*....|....*...
gi 1189438338 1516 ENILQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL 1551
Cdd:PTZ00265 615 EYLVQKTInnLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
680-907 |
1.13e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.12 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 680 IMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGeMQKVSGAVFWssslpdseIGEDPSPERETAt 759
Cdd:COG4172 287 IKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRF--------DGQDLDGLSRRA- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 760 DLDIRKRGPVA----YASQKPWLlnaTVEEnIIFE---------SPfnKQRYKMVIEACS---LQPD-IDILPHgdqtqi 822
Cdd:COG4172 357 LRPLRRRMQVVfqdpFGSLSPRM---TVGQ-IIAEglrvhgpglSA--AERRARVAEALEevgLDPAaRHRYPH------ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 823 gErginLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRD--DKR--TVVLVTHKLQ---YLph 895
Cdd:COG4172 425 -E----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV-----QAQILDLLRDlqREHglAYLFISHDLAvvrAL-- 492
|
250
....*....|..
gi 1189438338 896 ADWIIAMKDGTI 907
Cdd:COG4172 493 AHRVMVMKDGKV 504
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
685-902 |
1.38e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.22 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQ---KVSGAVFwsssLPDSEIgedpsperetaTDL 761
Cdd:COG4136 7 LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVL----LNGRRL-----------TAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 DIRKRGpVAYASQKPWLL-NATVEENIIF---ESPFNKQRYKMVIEAcsLQpDIDiLPHgdqtqIGERGIN-LSGGQRQR 836
Cdd:COG4136 72 PAEQRR-IGILFQDDLLFpHLSVGENLAFalpPTIGRAQRRARVEQA--LE-EAG-LAG-----FADRDPAtLSGGQRAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 902
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLDAALRAQ-FREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
693-888 |
1.73e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsssLPDSEIGEDPSPERetatdldirkrGPVAya 772
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-----TLDGVPVTGPGADR-----------GVVF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 sQK----PWLlnaTVEENIIFESPFNK----QRYKMVIEACSLqpdIDiLPHGDQTQIGErginLSGGQRQRISVARALY 844
Cdd:COG4525 83 -QKdallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VG-LADFARRRIWQ----LSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438338 845 QHANVVFLDDPFSALDIhLSDHLMQAGILELLRDDKRTVVLVTH 888
Cdd:COG4525 151 ADPRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
695-909 |
2.15e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.78 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKVSGAVFWSSSLPDSEIGEDpsperetatDLDIRKRGPVAYASQ 774
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDKPTSGTYRVAGQDVATLDAD---------ALAQLRREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLL-NATVEENIifESPF---------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 844
Cdd:PRK10535 94 RYHLLsHLTAAQNV--EVPAvyaglerkqRLLRAQELLQRLGLEDRVEYQPS-----------QLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 845 QHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQR 909
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
688-888 |
3.10e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.96 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMqkvsgavfWSSSlpDSEIGedpSPERETatdldirkrg 767
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGL--------WPWG--SGRIG---MPEGED---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 pVAYASQKPWLLNATVEENIIFespfnkqrykmvieacslqpdidilPHGDqtqigergiNLSGGQRQRISVARALYQHA 847
Cdd:cd03223 66 -LLFLPQRPYLPLGTLREQLIY-------------------------PWDD---------VLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1189438338 848 NVVFLDDPFSALDIHLSDHLMQagileLLRDDKRTVVLVTH 888
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGH 146
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
702-911 |
3.35e-16 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 79.07 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 702 IPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIGEDPSPERetatdldirkrgPVAYASQKPWLL-N 780
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV----LINGVDVTAAPPADR------------PVSMLFQENNLFaH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 781 ATVEENI-------IFESPFNKQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALYQHANVVFLD 853
Cdd:cd03298 85 LTVEQNVglglspgLKLTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 854 DPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 911
Cdd:cd03298 154 EPFAALDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
693-912 |
3.41e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaALgeMQKVSgavfwssslpdseigeDPSPERETATDLDIRK------R 766
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI--NL--LQRVF----------------DPQSGRILIDGTDIRTvtraslR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GPVAYASQKPWLLNATVEENIIFESPfNKQRYKMVIEACSLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALY 844
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 845 QHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAA--LDELMKG-RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
684-915 |
4.20e-16 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 79.55 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGEDPSPERETAtdldi 763
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVL----VDGTDLTLLSGKELRKA----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKRgpVAYASQKPWLLNA-TVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 835
Cdd:cd03258 81 RRR--IGMIFQHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 836 RISVARALYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 910
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
....*
gi 1189438338 911 GTLKD 915
Cdd:cd03258 223 GTVEE 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
691-907 |
4.61e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.08 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEdpspERETATDLDIRKRGpVA 770
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD--------GK----EVSFASPRDARRAG-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVV 850
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 851 FLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:cd03216 105 ILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
689-915 |
4.72e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.12 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGEDPSperetaTDLDIRKRGP 768
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL----IKGEPIKYDKK------SLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVA 840
Cdd:PRK13639 82 IVFQNPDDQLFAPTVEEDVAF-GPLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 841 RALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKE 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1344-1559 |
4.93e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 79.09 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD------TFEGHIIIDGIDIAKLPLh 1415
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiIFDGKDLLKLSRRLRKIR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1416 tlRSRLSIILQDPvlFSgtirfNLDPERKCSDStLWEALEI--------AQLKLVVKALPG-GLDAII-----TEggenF 1481
Cdd:cd03257 81 --RKEIQMVFQDP--MS-----SLNPRMTIGEQ-IAEPLRIhgklskkeARKEAVLLLLVGvGLPEEVlnrypHE----L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1482 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVIVLKRGAI 1556
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
...
gi 1189438338 1557 LEF 1559
Cdd:cd03257 225 VEE 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
695-936 |
9.51e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.90 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemQKVSGAVFWSSSlPDSEI---GEdpSPERETATDLDIRK-RGPVA 770
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKS-AGSHIellGR--TVQREGRLARDIRKsRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLLNA-TVEENIIF----ESPFNKQRYKMVIEAcSLQPDIDILphgdqTQIG------ERGINLSGGQRQRISV 839
Cdd:PRK09984 90 YIFQQFNLVNRlSVLENVLIgalgSTPFWRTCFSWFTRE-QKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLK 914
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVM-----DTLRDinqnDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQ 238
|
250 260
....*....|....*....|..
gi 1189438338 915 DFQRSEcqlFEHWKTLMNRQDQ 936
Cdd:PRK09984 239 QFDNER---FDHLYRSINRVEE 257
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
695-907 |
9.82e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.95 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgemQKVSGAVFWSSSLPDSEIGEDpsperetaTDLDIRKrgpvayA 772
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLrlLAGL---ETPSAGELLAGTAPLAEARED--------TRLMFQD------A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKPWllnATVEENIIFESPFN-KQRYKMVIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQHANVVF 851
Cdd:PRK11247 91 RLLPW---KKVIDNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 852 LDDPFSALDIhLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 907
Cdd:PRK11247 157 LDEPLGALDA-LTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
689-915 |
9.91e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPD-SEIGEdpsperetatdLDIRKRG 767
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGL-----------MKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 PVAYASQKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISV 839
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVSF-GAVNlklpedevRKRVDNALKRTGIEHLKDKPTHC-----------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL-LVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
685-912 |
1.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.07 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllaalgemQKVSGAVFWSSSLPDSEIGEDpSPERETATDLDIR 764
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTI--------SKLINGLLLPDDNPNSKITVD-GITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 KRGPVAYASQKPWLLNATVEENIIFESPfNKQ--RYKMVIEACSLQPDIDILPHGDQTQIgergiNLSGGQRQRISVARA 842
Cdd:PRK13640 84 EKVGIVFQNPDNQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 843 LYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKL-IRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
710-912 |
1.42e-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: 79.85 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 710 IVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGEDPsPEREtatdldirkrgPVAYASQKPWLL-NATVEENII 788
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIM----LDGEDVTNVP-PHLR-----------HINMVFQSYALFpHMTVEENVA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 789 FESPFNK----QRYKMVIEACSLqpdidilphgdqTQIGERG----INLSGGQRQRISVARALYQHANVVFLDDPFSALD 860
Cdd:TIGR01187 65 FGLKMRKvpraEIKPRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 861 IHLSDhLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 912
Cdd:TIGR01187 133 KKLRD-QMQLELKTIQEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1340-1570 |
1.82e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.49 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1340 DQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRS 1419
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1420 RLSIILQDP-VLFSGT-----IRFNLdpERKCSDSTLWEALeIAQLKLVVkalpgGLDAIITEGGENFSQGQRQLFCLAR 1493
Cdd:PRK13632 84 KIGIIFQNPdNQFIGAtveddIAFGL--ENKKVPPKKMKDI-IDDLAKKV-----GMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1494 AFVRKTSIFIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1570
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
678-912 |
1.83e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.38 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 678 VQIMGGYFTW-TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKVSGAVFWSSSLPDSEIGEDP--- 751
Cdd:PTZ00265 1166 IEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVmsLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 752 -------------SPERETAT---------------------DLDIRK-RGPVAYASQKPWLLNATVEENIIF-ESPFNK 795
Cdd:PTZ00265 1246 eeqnvgmknvnefSLTKEGGSgedstvfknsgkilldgvdicDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFgKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 796 QRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILEL 875
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDI 1404
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1189438338 876 LRDDKRTVVLVTHKLQYLPHADWIIAM----KDGT-IQREGT 912
Cdd:PTZ00265 1405 KDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGT 1446
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
697-920 |
2.26e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGEDPSpeRETAtdldiRKRGPVAYasqkp 776
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW----LDGEHIQHYAS--KEVA-----RRIGLLAQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 777 wllNATVEENIIFESPFNKQRYKMvieacslQP--------DIDILPHGDQ----TQIGERGIN-LSGGQRQRISVARAL 843
Cdd:PRK10253 89 ---NATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 844 YQHANVVFLDDPFSALDIhlsDHlmQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQR 918
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT 233
|
..
gi 1189438338 919 SE 920
Cdd:PRK10253 234 AE 235
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
697-919 |
2.31e-15 |
|
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: 81.47 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLLlaalGEMQKVSGAVFWSSSLPDSEIGedpspereTATDLDIRKrgPVAYASQKP 776
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLI----NLLQRVYDPTVGQILIDGIDIN--------TVTRESLRK--SIATVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 777 WLLNATVEENIIF--ESPFNKQRYKMViEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDD 854
Cdd:TIGR01192 419 GLFNRSIRENIRLgrEGATDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 855 PFSALDIHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:TIGR01192 498 ATSALDVETEARVKNA--IDALRKN-RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
688-915 |
3.60e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVFWSssLPDSEIGEDPSPERETATDL---- 761
Cdd:PRK13651 16 LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNAL--LLPDTGTIEWI--FKDEKNKKKTKEKEKVLEKLviqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 ----------DIRKRGPVAYASQKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLqpDIDILPHGDqtqig 823
Cdd:PRK13651 92 trfkkikkikEIRRRVGVVFQFAEYQLFEQTIEKDIIF-GPVSmgvskeeaKKRAAKYIELVGL--DESYLQRSP----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 824 ergINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAM 902
Cdd:PRK13651 164 ---FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTIFF 238
|
250
....*....|....*..
gi 1189438338 903 KDGTIQREG----TLKD 915
Cdd:PRK13651 239 KDGKIIKDGdtydILSD 255
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
691-916 |
3.88e-15 |
|
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: 76.32 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGED----PSPEREtatdldirKR 766
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD--------GRDitglPPHERA--------RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GpVAYASQKPWLL-NATVEENIIF-ESPFNKQRYKMVIE-ACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVARAL 843
Cdd:cd03224 76 G-IGYVPEGRRIFpELTVEENLLLgAYARRRAKRKARLErVYELFPRL-------KERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 916
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEA--IRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
697-912 |
5.42e-15 |
|
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: 76.91 E-value: 5.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWS----SSLPDSEIgedpsperetatdLDIRKRgPVAYA 772
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiAAMSRKEL-------------RELRRK-KISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKPWLL-NATVEENIIF------ESPFNKQRYKM-VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 844
Cdd:cd03294 108 FQSFALLpHRTVLENVAFglevqgVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 845 QHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:cd03294 177 VDPDILLMDEAFSALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
689-911 |
5.81e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.86 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFW----SSSLPDSEIgedpsperetatdLDIR 764
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdLSRLKRREI-------------PYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 KR-GPVAyasQKPWLL-NATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 835
Cdd:COG2884 79 RRiGVVF---QDFRLLpDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 836 RISVARALyqhAN---VVFLDDPFSALDIHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPHADW-IIAMKDGTIQ 908
Cdd:COG2884 145 RVAIARAL---VNrpeLLLADEPTGNLDPETSW-----EIMELLEEINRrgtTVLIATHDLELVDRMPKrVLELEDGRLV 216
|
...
gi 1189438338 909 REG 911
Cdd:COG2884 217 RDE 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1344-1568 |
6.98e-15 |
|
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: 79.56 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLK---PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD------TFEGHIIIDGIDIAklpL 1414
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRptsgsiLFDGKDLTKLSRRS---L 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1415 HTLRSRLSIILQDPvlFSGtirfnLDPERKCSDStLWEALEIAQL-------KLVVKAL------PGGLDAIITEggenF 1481
Cdd:COG1123 338 RELRRRVQMVFQDP--YSS-----LNPRMTVGDI-IAEPLRLHGLlsraerrERVAELLervglpPDLADRYPHE----L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1482 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVIVLKRG 1554
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|....
gi 1189438338 1555 AILEFDKPEKLLSR 1568
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
695-915 |
1.23e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 75.06 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLDIRKRGpVAYASQ 774
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN--------GKD-------ITNLPPEKRD-ISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLL-NATVEENIIF----ESPFNKQRYKMVIE-ACSLqpDIDILPHGDQTqigergiNLSGGQRQRISVARALYQHAN 848
Cdd:cd03299 79 NYALFpHMTVYKNIAYglkkRKVDKKEIERKVLEiAEML--GIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 849 VVFLDDPFSALDIHLSDHLMqagilELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLR-----EELKKIRKefgvTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1082-1314 |
1.86e-14 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 75.92 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1082 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV-- 1159
Cdd:cd18552 60 TYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdw 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1160 --TPVFLVALLPLAIVCYFIQKYFRVASRDLQ-QLDDttqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSN--- 1233
Cdd:cd18552 140 klTLIALVVLPLAALPIRRIGKRLRKISRRSQeSMGD-----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLrrl 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1234 NIASLFLTAANRWLevrMEYIGACVVLIAAVTSISNSLHRELSAG-LVGLgLTYALMVSNYLnwmvRNLADM--ELQ--L 1308
Cdd:cd18552 215 SMKIARARALSSPL---MELLGAIAIALVLWYGGYQVISGELTPGeFISF-ITALLLLYQPI----KRLSNVnaNLQrgL 286
|
....*.
gi 1189438338 1309 GAVKRI 1314
Cdd:cd18552 287 AAAERI 292
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
685-916 |
2.13e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.07 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 685 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQ---KVSGAV-FWSSSLPDSEIGEDpspereta 758
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELEsevRVEGRVeFFNQNIYERRVNLN-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 759 tdldiRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKM----VIEACSLQPDI-DILPHgdqtQIGERGINLSGGQ 833
Cdd:PRK14258 85 -----RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLwDEIKH----KIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 834 RQRISVARALYQHANVVFLDDPFSALDIHLS---DHLMQAGILEllrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 910
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
....*.
gi 1189438338 911 GTLKDF 916
Cdd:PRK14258 232 GQLVEF 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
689-912 |
3.54e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.64 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSslpdSEIGeDPSPEREtatdldIRKRGP 768
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG----IDTG-DFSKLQG------IRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKPWLLNATVEENIIFeSPFNkqrykmvieACslQPDIDILPHGDQTqIGERGI---------NLSGGQRQRISV 839
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAF-GPEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1344-1567 |
3.61e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.64 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSL------------AFFRMVDTFEghiiidgidIAK 1411
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALhlngllrpqkgkVLVSGIDTGD---------FSK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1412 LPlhTLRSRLSIILQDP-VLFSG-TIRFNL--DPERKCSDSTlwealEIAqlKLVVKALPG-GLDAIITEGGENFSQGQR 1486
Cdd:PRK13644 72 LQ--GIRKLVGIVFQNPeTQFVGrTVEEDLafGPENLCLPPI-----EIR--KRVDRALAEiGLEKYRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1487 QLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKL 1565
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
..
gi 1189438338 1566 LS 1567
Cdd:PRK13644 223 LS 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
686-911 |
3.82e-14 |
|
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: 73.36 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 686 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIGEDPSPERetatdldirk 765
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI----KVNDQSHTGLAPYQR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 rgPVAYASQKPWLL-NATVEENIIFE-SPFNK----QRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRI 837
Cdd:TIGR01277 71 --PVSMLFQENNLFaHLTVRQNIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 838 SVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 911
Cdd:TIGR01277 138 ALARCLVRPNPILLLDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
683-910 |
4.75e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 74.07 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 683 GYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSlPDSEIgeDPSPERETATDLD 762
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQ-DLYQL--DRKQRRAFRRDVQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 763 -IRKRGPVAYASQKP--WLLNATVEENIIFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRIS 838
Cdd:TIGR02769 92 lVFQDSPSAVNPRMTvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 910
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
690-888 |
5.03e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.64 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGEDPSPERetatdldirkrgPV 769
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM----LDGVDLSHVPPYQR------------PI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLL-NATVEENIIFESPFNK-------QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 841
Cdd:PRK11607 94 NMMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1189438338 842 ALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH 888
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDR-MQLEVVDILERVGVTCVMVTH 208
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1063-1314 |
5.82e-14 |
|
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: 74.12 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1063 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1142
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1143 SRSTLLCVSALAVISYVTPV-FLVALLPLAIVCYFIQKYF---RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1218
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWKlTLVALLLLPLYVLILRYFRrriRKASREVRESLAE----LSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1219 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGlvglGLTYALMVSNYLNWMV 1298
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG----ELVAFLAYLGMLFGPI 272
|
250 260
....*....|....*....|
gi 1189438338 1299 RNLADMELQ----LGAVKRI 1314
Cdd:cd07346 273 QRLANLYNQlqqaLASLERI 292
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
687-892 |
7.36e-14 |
|
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: 71.81 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 687 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFwssslpdseIGEDPSPEREtatdldIR 764
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLnaLAGRRTGLGVSGEVL---------INGRPLDKRS------FR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 765 KRgpVAYASQKPWLL-NATVEENIIFespfnkqrykmvieACSLQpdidilphgdqtqigergiNLSGGQRQRISVARAL 843
Cdd:cd03213 82 KI--IGYVPQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALEL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY 892
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSS 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1344-1568 |
1.09e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 72.53 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSL--KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPvlfsgtiRFNLDPeRKCSDSTLWEALEIAQLKLVVKALPGGLDAIiteG-GENF--------SQGQRQLFCLA 1492
Cdd:COG1124 82 QMVFQDP-------YASLHP-RHTVDRILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1493 RAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
.
gi 1189438338 1568 R 1568
Cdd:COG1124 229 G 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
690-891 |
1.38e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIgEDPSPEREtatdldirkrgpV 769
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI----TLDGKPV-EGPGAERG------------V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQK--PWLlnaTVEENIIFespfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQH 846
Cdd:PRK11248 75 VFQNEGllPWR---NVQDNVAF-----GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 891
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
688-888 |
1.41e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 73.55 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALG---EMQKVSGAVFWSsslpdseiGEDPS--PEREtatdl 761
Cdd:COG0444 13 TRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFD--------GEDLLklSEKE----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 dIRK-RGP-VAYASQKPwlLNA-----TVEEniIFESPFN-------KQRYKMVIEA---CSLQPDIDIL---PHgdqtq 821
Cdd:COG0444 80 -LRKiRGReIQMIFQDP--MTSlnpvmTVGD--QIAEPLRihgglskAEARERAIELlerVGLPDPERRLdryPH----- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 822 igergiNLSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTH 888
Cdd:COG0444 150 ------ELSGGMRQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITH 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1344-1553 |
1.41e-13 |
|
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: 71.73 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSS--LKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKlPLHTLRSRL 1421
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLERPTSGEVLVDGE-PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLFS-GTIRFN--LDPERKCSDSTlwEALEIAQ--LKLVvkalpgGLdaiitEGGENF-----SQGQRQLFCL 1491
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGLELQGVPKA--EARERAEelLELV------GL-----SGFENAyphqlSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 1492 ARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILSADLVIVLKR 1553
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
698-919 |
1.57e-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: 73.99 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 698 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWS-SSLPDSEIGEDPSPERetatdldiRKrgpVAYASQKP 776
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgRTLFDSRKGIFLPPEK--------RR---IGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 777 WLL-NATVEENIIF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHANVV 850
Cdd:TIGR02142 85 RLFpHLSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 851 FLDDPFSALDIHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
698-902 |
2.41e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 698 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsssLPDSEIGEDPSPERETATDLDIRKRGPVAyaSQKPW 777
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW---LGKDLLGMKDDEWRAVRSDIQMIFQDPLA--SLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 778 LlnaTVEEnIIFEsPFN-----------KQRYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVARALYQ 845
Cdd:PRK15079 115 M---TIGE-IIAE-PLRtyhpklsrqevKDRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 846 HANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 902
Cdd:PRK15079 179 EPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
695-907 |
2.83e-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: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVfwssslpdsEIGEDPSPERETATDLdIRKRgpVAYA 772
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTI---------IIDGLKLTDDKKNINE-LRQK--VGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKPWLL-NATVEENIIfESP---FNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHAN 848
Cdd:cd03262 82 FQQFNLFpHLTVLENIT-LAPikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 849 VVFLDDPFSALDIHlsdhlMQAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:cd03262 156 VMLFDEPTSALDPE-----LVGEVLDVMKDlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
690-912 |
3.40e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllAALgemqkVSGAVFWSsslpDSEIGEDPSPeRETATDLDIRKRgpV 769
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTL--ASL-----LMGYYPLT----EGEIRLDGRP-LSSLSHSVLRQG--V 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANV 849
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 850 VFLDDPFSALDIHLSDHLMQAgiLELLRdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQA--LAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
684-915 |
3.65e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.56 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvSGAVFwsssLPDSEIgedpspERETATDL 761
Cdd:PRK13632 14 SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIskILTGLLKPQ--SGEIK----IDGITI------SKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 dirkRGPVAYASQKP--WLLNATVEENIIFeSPFNKQ--RYKM--VIEACSLQPDI-DILPHGDQtqigergiNLSGGQR 834
Cdd:PRK13632 82 ----RKKIGIIFQNPdnQFIGATVEDDIAF-GLENKKvpPKKMkdIIDDLAKKVGMeDYLDKEPQ--------NLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 835 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 914
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI-MVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPK 227
|
.
gi 1189438338 915 D 915
Cdd:PRK13632 228 E 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1344-1567 |
4.18e-13 |
|
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: 70.84 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKL----------- 1412
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTL----LRAL--------------AGLlkpssgevlld 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1413 --PLHTLRSR-----LSIILQDPVL-FSGTIR--------------FNLDPE-RKCSDSTLwEALEIAQLKlvvkalpgg 1469
Cdd:COG1120 62 grDLASLSRRelarrIAYVPQEPPApFGLTVRelvalgryphlglfGRPSAEdREAVEEAL-ERTGLEHLA--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1470 lDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILS 1544
Cdd:COG1120 132 -DRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARY 204
|
250 260
....*....|....*....|...
gi 1189438338 1545 ADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:COG1120 205 ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
686-890 |
4.23e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 686 TWTpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwssslpdsEIGEDPSPERETAtdldirK 765
Cdd:PRK15056 15 TWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-----------KISILGQPTRQAL------Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 RGPVAYASQKP---WLLNATVEENII---------FESPfnKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQ 833
Cdd:PRK15056 77 KNLVAYVPQSEevdWSFPVLVEDVVMmgryghmgwLRRA--KKRDRQIVTAALARVDMVEFRH---RQIGE----LSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 834 RQRISVARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKL 890
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNL 202
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
690-915 |
5.84e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.29 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLDIRKRgPV 769
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD--------GQD-------ITHVPAENR-HV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLL-NATVEENIIF-----ESPfNKQRYKMVIEA---CSLQPDIDILPHgdqtqigergiNLSGGQRQRISVA 840
Cdd:PRK09452 89 NTVFQSYALFpHMTVFENVAFglrmqKTP-AAEITPRVMEAlrmVQLEEFAQRKPH-----------QLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 841 RALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQ-MQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
688-923 |
5.88e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.35 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIgEDPSPERETATdldIRKRG 767
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV----TVDDITI-THKTKDKYIRP---VRKRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 PVAYASQKPWLLNATVEENIIFeSPFNkqrYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARALYQH 846
Cdd:PRK13646 88 GMVFQFPESQLFEDTVEREIIF-GPKN---FKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSECQL 923
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRL-LKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
691-920 |
6.11e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqKV-SGAVfwsssLPDS-EI---GEdpspERETATDLDIRK 765
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLM--------KIlSGVY-----QPDSgEIlldGE----PVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 RGpVAYASQKPWLL-NATVEENIIFESPFNK----QRYKMVIEACSL--QPDIDILPHgdqTQIGErginLSGGQRQRIS 838
Cdd:COG1129 79 AG-IAIIHQELNLVpNLSVAENIFLGREPRRggliDWRAMRRRARELlaRLGLDIDPD---TPVGD----LSVAQQQLVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQ 917
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAELT 228
|
...
gi 1189438338 918 RSE 920
Cdd:COG1129 229 EDE 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
818-911 |
6.22e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.77 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 818 DQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-A 896
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvS 219
|
90
....*....|....*
gi 1189438338 897 DWIIAMKDGTIQREG 911
Cdd:PRK10619 220 SHVIFLHQGKIEEEG 234
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1064-1314 |
6.37e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 71.05 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1064 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1143
Cdd:cd18557 39 ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1144 RSTLLCVSA---LAVISY-VTPVFLVALLPLAIVCYFIQKYFRVASRDLQQlddttQLPLLSHFA-ETVEGLTTIRAF-- 1216
Cdd:cd18557 119 RNILQVIGGliiLFILSWkLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQD-----ALAKAGQVAeESLSNIRTVRSFsa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1217 -RYE-ARFQQKLLEYTDSnNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSlhrELSAGLVGLGLTYALMVSNYL 1294
Cdd:cd18557 194 eEKEiRRYSEALDRSYRL-ARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSG---QLTVGELTSFILYTIMVASSV 269
|
250 260
....*....|....*....|
gi 1189438338 1295 NWMVRNLADMELQLGAVKRI 1314
Cdd:cd18557 270 GGLSSLLADIMKALGASERV 289
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
691-911 |
6.40e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssslpdseIGEDPSPERETATdldIRKRgpVA 770
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL---------VAGDDVEALSARA---ASRR--VA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWL-LNATVEENIIFESPFNKQRYKMVIEACSLQPDiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHAN 848
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 849 VVFLDDPFSALDIHlsdHLMQAgiLELLR---DDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 911
Cdd:PRK09536 160 VLLLDEPTASLDIN---HQVRT--LELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
684-926 |
6.45e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdsEIGEDPSPEretATDLDI 763
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI---------TVGGMVLSE---ETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKRgpVAYASQKP--WLLNATVEENIIF--EspfNKQ--RYKMV------IEACSLQPDIDILPHgdqtqigergiNLSG 831
Cdd:PRK13635 80 RRQ--VGMVFQNPdnQFVGATVQDDVAFglE---NIGvpREEMVervdqaLRQVGMEDFLNREPH-----------RLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 832 GQRQRISVARALYQHANVVFLDDPFSALDihlsdhlmQAG---ILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKD 904
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLD--------PRGrreVLETVRQLKEqkgiTVLSITHDLDEAAQADRVIVMNK 215
|
250 260
....*....|....*....|..
gi 1189438338 905 GTIQREGTLKdfqrsecQLFEH 926
Cdd:PRK13635 216 GEILEEGTPE-------EIFKS 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1339-1554 |
7.57e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.30 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1339 PDQGKIQIQNLSVRyDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKLPLH--- 1415
Cdd:COG4178 358 SEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAI--------------AGLWPYgsg 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1416 --TLRSRLSIIL--QDPVLFSGTIRFNL---DPERKCSDSTLWEALEIAQLKlvvkALPGGLDAIiTEGGENFSQGQRQL 1488
Cdd:COG4178 419 riARPAGARVLFlpQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLG----HLAERLDEE-ADWDQVLSLGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1489 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRG 1554
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1328-1563 |
7.94e-13 |
|
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: 73.18 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1328 LLA--PSLIPKNWPDQGK--IQIQNLSVRYD---SSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRM 1394
Cdd:COG4172 256 LLAaePRGDPRPVPPDAPplLEARDLKVWFPikrGLFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1395 VDT-----FEGHIIIDGIDIAKLPlhtLRSRLSIILQDPvlFSgtirfNLDPERKCSDsTLWEALEIAQLKL-------- 1461
Cdd:COG4172 336 IPSegeirFDGQDLDGLSRRALRP---LRRRMQVVFQDP--FG-----SLSPRMTVGQ-IIAEGLRVHGPGLsaaerrar 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1462 VVKAL------PGGLDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFA------- 1528
Cdd:COG4172 405 VAEALeevgldPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehg 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 1529 --------DRTVV-TIAHRvhtilsadlVIVLKRGAILE-------FDKPE 1563
Cdd:COG4172 477 laylfishDLAVVrALAHR---------VMVMKDGKVVEqgpteqvFDAPQ 518
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
695-918 |
8.33e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 71.65 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSpeRETATDldiRKRGPV--AYA 772
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH--------GTDVS--RLHARD---RKVGFVfqHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 sqkpWLLNATVEENIIF--------ESPFN---KQRYKMVIEACSLQPDIDILPhgdqTQigerginLSGGQRQRISVAR 841
Cdd:PRK10851 85 ----LFRHMTVFDNIAFgltvlprrERPNAaaiKAKVTQLLEMVQLAHLADRYP----AQ-------LSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 842 ALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQR 918
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKEL-RRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1344-1567 |
9.19e-13 |
|
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: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLrsrLSI 1423
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKS------------------------------TL---LKA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 IL--QDPVlfSGTIRFNLDPERKCSDStlwealeIA---QLKLVVKALP--------GGLD--------------AIITE 1476
Cdd:COG1121 52 ILglLPPT--SGTVRLFGKPPRRARRR-------IGyvpQRAEVDWDFPitvrdvvlMGRYgrrglfrrpsradrEAVDE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1477 -----GGENF--------SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI 1542
Cdd:COG1121 123 alervGLEDLadrpigelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAV 202
|
250 260
....*....|....*....|....*.
gi 1189438338 1543 LS-ADLVIVLKRGaILEFDKPEKLLS 1567
Cdd:COG1121 203 REyFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
695-929 |
1.07e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.94 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFwsssLPDSEIGEDPSPEretatdldIRKRGPV 769
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVY----LDGQDIFKMDVIE--------LRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPwLLNATVEENIIFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVA 840
Cdd:PRK14247 87 VFQIPNP-IPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 841 RALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDdkRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKD- 915
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD--MTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREv 232
|
250
....*....|....
gi 1189438338 916 FQRSECQLFEHWKT 929
Cdd:PRK14247 233 FTNPRHELTEKYVT 246
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
695-889 |
1.08e-12 |
|
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: 69.22 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQK---VSGAVFWSSSlpdseigedpspERETATDLDIrkrgpVAY 771
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ------------PRKPDQFQKC-----VAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQKPWLL-NATVEENIIFESPF-------NKQRYKMVieacslqpDIDILPHGDQTQIGERGI-NLSGGQRQRISVARA 842
Cdd:cd03234 86 VRQDDILLpGLTVRETLTYTAILrlprkssDAIRKKRV--------EDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1189438338 843 LYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHK 889
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
695-891 |
1.31e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.68 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFwsssLPDSEI---GEDPsperetatdLDIRKR 766
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLrclnrMNDLIPGARVEGEIL----LDGEDIydpDVDV---------VELRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 gpVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEA--------CSLQPDI-DILphgdqtqiGERGINLSGGQRQRI 837
Cdd:COG1117 94 --VGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVkDRL--------KKSALGLSGGQQQRL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 838 SVARALYQHANVVFLDDPFSALDIHLSdhlmqAGILELLRD--DKRTVVLVTHKLQ 891
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPIST-----AKIEELILElkKDYTIVIVTHNMQ 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1341-1569 |
1.41e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.56 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1341 QGKIQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTF-----EGHIIIDGIDIAKLPLH 1415
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1416 TLRSRLSIILQDP------VLFSGT---IRFN-LDPERKCSDSTLWEALEIAQLKLVVKalpGGLDAiiteGGENFSQGQ 1485
Cdd:PRK14247 79 ELRRRVQMVFQIPnpipnlSIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVK---DRLDA----PAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1486 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtilsADLVIVLKRGAILE- 1558
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEw 226
|
250
....*....|....*..
gi 1189438338 1559 ------FDKPEKLLSRK 1569
Cdd:PRK14247 227 gptrevFTNPRHELTEK 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
695-888 |
1.61e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVfwssSLPDSEIgEDPSPeretatdldirkRGPVAYA 772
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLrlIAGL--LPPAAGTI----KLDGGDI-DDPDV------------AEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQ----KPWLlnaTVEENIIFESPFNKQRYKMV---IEACSLQPDIDiLPHGdqtqigergiNLSGGQRQRISVARALYQ 845
Cdd:PRK13539 79 GHrnamKPAL---TVAENLEFWAAFLGGEELDIaaaLEAVGLAPLAH-LPFG----------YLSAGQKRRVALARLLVS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 846 HANVVFLDDPFSALDIH--------LSDHLMQAGIlellrddkrtVVLVTH 888
Cdd:PRK13539 145 NRPIWILDEPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1345-1557 |
1.85e-12 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 67.46 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1345 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLRSRLSII 1424
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKS------------------------------TLLKTLAGL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1425 LQdpvLFSGTIRFNLDPERKcsdstlWEALEIAQLKLVV----KALpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03214 49 LK---PSSGEILLDGKDLAS------LSPKELARKIAYVpqalELL--GLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1501 IFIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILSADLVIVLKRGAIL 1557
Cdd:cd03214 118 ILLLDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
694-891 |
2.04e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.03 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 694 TLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQ------KVSGAVFWSsslpdseiGEDP-SPERETatdLDIRKR 766
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLL-RSINRMNdlnpevTITGSIVYN--------GHNIySPRTDT---VDLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 gpVAYASQKPWLLNATVEENIIFESPFN----KQRYKMVIEACSLQPDI-----DILpHgdqtqigERGINLSGGQRQRI 837
Cdd:PRK14239 88 --IGMVFQQPNPFPMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdevkDRL-H-------DSALGLSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 838 SVARALYQHANVVFLDDPFSALDiHLSDHLMQAGILELlrDDKRTVVLVTHKLQ 891
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQ 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1344-1565 |
2.57e-12 |
|
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: 68.30 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLA----------FFRMVDTFEGHIIIdgidiak 1411
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLlrLIVgllrpdsgevLIDGEDISGLSEAE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1412 lpLHTLRSRLSIILQDPVLFSG-TIR----FNLDPERKCSDSTLweaLEIAQLKLVVKALPGGLDAIITEggenFSQGQR 1486
Cdd:cd03261 72 --LYRLRRRMGMLFQSGALFDSlTVFenvaFPLREHTRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE----LSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1487 QLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPE 1563
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
..
gi 1189438338 1564 KL 1565
Cdd:cd03261 223 EL 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
690-888 |
3.68e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 67.00 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssslpdseigedpsPERETATDLDIRKRGpV 769
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW--------------NGTPLAEQRDEPHEN-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLLNA-TVEENIIFESPFNKQRYKMVIEACslqpdidilphgdqTQIGERGIN------LSGGQRQRISVARA 842
Cdd:TIGR01189 76 LYLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 843 LYQHANVVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTH 888
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1345-1556 |
4.93e-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: 66.79 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1345 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRM-----------VDTFEGHIIIDGIDIAKLP 1413
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTL----LKAilgllkptsgsIRVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1414 LHTLRSRLS-IILQDPVLFSGTIRFNLDPERKCSDstlWEALEIAqLKLVvkalpgGLDAI----ITEggenFSQGQRQL 1488
Cdd:cd03235 75 QRRSIDRDFpISVRDVVLMGLYGHKGLFRRLSKAD---KAKVDEA-LERV------GLSELadrqIGE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1489 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-SADLVIVLKRGAI 1556
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLeYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1344-1568 |
5.34e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.29 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTL---RSR 1420
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVwdiREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1421 LSIILQDP-VLFSGT-----IRFNLDpERKCSDSTLwealeiaqLKLVVKALP--GGLDAIITEGgENFSQGQRQLFCLA 1492
Cdd:PRK13640 86 VGIVFQNPdNQFVGAtvgddVAFGLE-NRAVPRPEM--------IKIVRDVLAdvGMLDYIDSEP-ANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1493 RAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1568
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
672-912 |
5.51e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 672 DADNCCVQImggyftwtpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIGEDP 751
Cdd:PRK13548 4 EARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV----RLNGRPLADWS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 752 SPEREtatdldiRKRgpvAYASQK-----PWllnaTVEENI---IFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQig 823
Cdd:PRK13548 71 PAELA-------RRR---AVLPQHsslsfPF----TVEEVVamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQ-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 824 erginLSGGQRQRISVARALYQHAN------VVFLDDPFSALDIHlsdHlmQAGILELLRD----DKRTVVLVTHKL--- 890
Cdd:PRK13548 135 -----LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLA---H--QHHVLRLARQlaheRGLAVIVVLHDLnla 204
|
250 260
....*....|....*....|...
gi 1189438338 891 -QYlphADWIIAMKDGTIQREGT 912
Cdd:PRK13548 205 aRY---ADRIVLLHQGRLVADGT 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
693-907 |
6.19e-12 |
|
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: 67.63 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAalgemqkvsgaVFWSSSLPDSEIGEDpsperetatDLDIRK------R 766
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLA-----------FFRMVDIFDGKIVID---------GIDISKlplhtlR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 847 ANVVFLDDPFSALDIhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:cd03288 175 SSILIMDEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
693-915 |
6.82e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.81 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETatdLDIRKRGPVAYA 772
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD--------GLDTSDEENL---WDIRNKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 844
Cdd:PRK13633 93 NPDNQIVATIVEEDVAF-GPENlgippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 845 QHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1344-1560 |
7.41e-12 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 66.39 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEG----HIIIDGIDIAKLPLHtlRS 1419
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLERpdsgEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1420 RLSIILQDPVLFS-----GTIRFNLD----PERKCSDSTLwEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1490
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKlrgvPKAEIRARVR-ELLELVGLEGLLNRYPHEL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1491 LARAFVRKTSIFIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFD 1560
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
684-912 |
8.06e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIgedPSPERETATDLDI 763
Cdd:PRK13645 16 YAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI----VGDYAI---PANLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKRGPVAYASQKPWLLNATVEENIIFeSPFN-----KQRYKMVIEACSLQPdidiLPhgdQTQIGERGINLSGGQRQRIS 838
Cdd:PRK13645 89 RKEIGLVFQFPEYQLFQETIEKDIAF-GPVNlgenkQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1344-1562 |
9.07e-12 |
|
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: 66.82 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRSR 1420
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1421 LSIILQDpvlfsgtirFNLDPE----------RKCSDSTLW------------EALEIaqLKLVvkalpgGLDAIITEGG 1478
Cdd:cd03256 80 IGMIFQQ---------FNLIERlsvlenvlsgRLGRRSTWRslfglfpkeekqRALAA--LERV------GLLDKAYQRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILS-ADLVIVL 1551
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGL 218
|
250
....*....|.
gi 1189438338 1552 KRGAILeFDKP 1562
Cdd:cd03256 219 KDGRIV-FDGP 228
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1057-1226 |
9.13e-12 |
|
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: 67.92 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1057 TLDQTVYAM--VFTV--LCSLGIVLCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID 1132
Cdd:cd18573 39 SLKTFALALlgVFVVgaAANFGRVYLLRIA------GERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1133 QHIPSTLECLSRSTLLCVSALAVISYVTP-VFLVALL---PLAIVCYFIQKYFRVASRDLQQ-LDDTTQLPllshfAETV 1207
Cdd:cd18573 113 KSLTQNLSDGLRSLVSGVGGIGMMLYISPkLTLVMLLvvpPIAVGAVFYGRYVRKLSKQVQDaLADATKVA-----EERL 187
|
170 180
....*....|....*....|...
gi 1189438338 1208 EGLTTIRAF---RYE-ARFQQKL 1226
Cdd:cd18573 188 SNIRTVRAFaaeRKEvERYAKKV 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1359-1555 |
9.87e-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: 67.57 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1359 PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIidgidiaklplHTlrSRLSIILQDPVLFSGTIRFN 1438
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------HS--GRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1439 L------DPERKCSdstlweALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID 1512
Cdd:cd03291 118 IifgvsyDEYRYKS------VVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438338 1513 MATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGA 1555
Cdd:cd03291 192 VFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
689-911 |
9.87e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLL--AALGEMQKVSGAVFwssslpdseiGEDPSPERETatdlDIRKR 766
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLhlNGIYLPQRGRVKVM----------GREVNAENEK----WVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 gpVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQR 836
Cdd:PRK13647 81 --VGLVFQDPddQVFSSTVWDDVAF-GPVNmgldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 911
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
697-924 |
1.04e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLDIRKRGpVAYASQKP 776
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID--------GED-------VTHRSIQQRD-ICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 777 WLL-NATVEENIIF-------ESPFNKQRYKmviEACSLqpdIDILPHGDQ--TQIgerginlSGGQRQRISVARALYQH 846
Cdd:PRK11432 88 ALFpHMSLGENVGYglkmlgvPKEERKQRVK---EALEL---VDLAGFEDRyvDQI-------SGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLF 924
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
688-912 |
1.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.95 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIGEDPSPERETATDL------ 761
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI----QVGDIYIGDKKNNHELITNPYskkikn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 --DIRKRgpVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPD-IDILPHGdqtqigergin 828
Cdd:PRK13631 111 fkELRRR--VSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG----------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 829 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagileLLRDDK---RTVVLVTHKL-QYLPHADWIIAMKD 904
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-----LILDAKannKTVFVITHTMeHVLEVADEVIVMDK 251
|
....*...
gi 1189438338 905 GTIQREGT 912
Cdd:PRK13631 252 GKILKTGT 259
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1012-1314 |
1.16e-11 |
|
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: 67.18 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1012 LSLLVFSQLLKhmvlVAIDYWLAKWTDSALTltpaarncSLSQEcTLDQTVYAMV-FTVLCSL--GIVLCLVTSVTVewt 1088
Cdd:cd18572 2 FVFLVVAALSE----LAIPHYTGAVIDAVVA--------DGSRE-AFYRAVLLLLlLSVLSGLfsGLRGGCFSYAGT--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1089 glKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP----VFL 1164
Cdd:cd18572 66 --RLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWrltlLAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1165 VALLPLAIVCYFIQKYFRVASRDLQQ-LDDTTQLpllshfAETVEGL-TTIRAF---RYEA-RFQQKLLEYTDSN---NI 1235
Cdd:cd18572 144 ITVPVIALITKVYGRYYRKLSKEIQDaLAEANQV------AEEALSNiRTVRSFateEREArRYERALDKALKLSvrqAL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1236 ASLFLTAANRWLevrmEYIGACVVLIAAVTSIsnsLHRELSAG-LVGLGLtYALMVSNYLNWMVRNLADMELQLGAVKRI 1314
Cdd:cd18572 218 AYAGYVAVNTLL----QNGTQVLVLFYGGHLV---LSGRMSAGqLVTFML-YQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
695-934 |
1.48e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.31 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIGEDPSPERETATdldIRK-RGPVAYAS 773
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI----RVGDITIDTARSLSQQKGL---IRQlRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 QKPWLL-NATVEENIIfESPF---NKQRYKMVIEACSLQPDIDIlpHGDQTQIGERginLSGGQRQRISVARALYQHANV 849
Cdd:PRK11264 92 QNFNLFpHRTVLENII-EGPVivkGEPKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 850 VFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKdfqrsecQLFEHWK 928
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK-------ALFADPQ 236
|
....*.
gi 1189438338 929 TLMNRQ 934
Cdd:PRK11264 237 QPRTRQ 242
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1067-1314 |
1.51e-11 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 67.12 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1067 FTVLCSLGIVLCLVTSV---TVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1143
Cdd:cd18575 39 FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1144 RSTLLCVSALAVISYVTP---VFLVALLPLAIV-CYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAFRY 1218
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQdRLADLS-----AFAEETLSAIKTVQAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1219 EARFQQKLLEYTDSNniaslfLTAANRWLEVRMEYIGACVVLI-AAVTSI-----SNSLHRELSAGLVGLGLTYALMVSN 1292
Cdd:cd18575 194 EDAERQRFATAVEAA------FAAALRRIRARALLTALVIFLVfGAIVFVlwlgaHDVLAGRMSAGELSQFVFYAVLAAG 267
|
250 260
....*....|....*....|..
gi 1189438338 1293 YLNWMVRNLADMELQLGAVKRI 1314
Cdd:cd18575 268 SVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1344-1554 |
1.62e-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: 64.52 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLlrCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLFSG-TIRFNLdperkcsdstlwealeiaqlklvvkALPggldaiiteggenFSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------------------ALG-------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 1501 IFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVIVLKRG 1554
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
684-915 |
1.92e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.61 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETATDldI 763
Cdd:PRK13637 12 YMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID--------GVDITDKKVKLSD--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKRgpVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDI--DILPhgdqtqigergINLSG 831
Cdd:PRK13637 82 RKK--VGLVFQYPeyQLFEETIEKDIAF-GPINlglseeeiENRVKRAMNIVGLDYEDykDKSP-----------FELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 832 GQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 910
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQ 226
|
....*
gi 1189438338 911 GTLKD 915
Cdd:PRK13637 227 GTPRE 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1344-1554 |
2.25e-11 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 63.96 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdtfeghiiidgidiaklplhTLRSRLSI 1423
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTT-----------------------------LIKIILGL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDpvlfSGTIR-FNLDPERkcsdstlwealEIAQLKLVVKALPGGlDAIITE--GGEN--FSQGQRQLFCLARAFVRK 1498
Cdd:cd03230 50 LKPD----SGEIKvLGKDIKK-----------EPEEVKRRIGYLPEE-PSLYENltVRENlkLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1499 TSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILS-ADLVIVLKRG 1554
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
695-902 |
2.28e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 67.06 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperetATDLDIRKRGPVA---- 770
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD--------GQD-------ITGLSGRELRPLRrrmq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 ------YASqkpwlLNA--TVEEnIIFEsPF-------NKQRYKMV---IEACSLQPD-IDILPHgdqtqigErginLSG 831
Cdd:COG4608 99 mvfqdpYAS-----LNPrmTVGD-IIAE-PLrihglasKAERRERVaelLELVGLRPEhADRYPH-------E----FSG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 832 GQRQRISVARALYQHANVVFLDDPFSALDihLSdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 902
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALD--VS---IQAQVLNLLEDLQDelglTYLFISHDLSVVRHiSDRVAVM 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
688-917 |
2.43e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPDSEigedpSPERETATdldIRKRG 767
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSST-----SKQKEIKP---VRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 PVAYASQKPWLLnatvEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARALYQH 846
Cdd:PRK13643 87 GVVFQFPESQLF----EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQ 917
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDvFQ 233
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
377-609 |
2.79e-11 |
|
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: 66.42 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 377 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYIL 455
Cdd:cd07346 61 YLAARLGQRVVFDLRRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIGALVILFYLN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 456 GVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWE----NIFRTRVETTRRKEMTS 531
Cdd:cd07346 139 WKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 532 LRAFAIYTSISIFMNTaipIAAVLITFVGHVSFFKEaDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 609
Cdd:cd07346 219 ARLSALFSPLIGLLTA---LGTALVLLYGGYLVLQG-SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
695-929 |
3.03e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.63 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAV-FWSSSLPDSEIgeDPsperetatdLDIRKRGP 768
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVrLFGRNIYSPDV--DP---------IEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKPWLlNATVEENIIFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISV 839
Cdd:PRK14267 89 MVFQYPNPFP-HLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 840 ARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKR--TVVLVTHK-LQYLPHADWIIAMKDGTIQREG-TLKD 915
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANI-----DPVGTAKIEELLFELKKeyTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpTRKV 235
|
250
....*....|....
gi 1189438338 916 FQRSECQLFEHWKT 929
Cdd:PRK14267 236 FENPEHELTEKYVT 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1258-1558 |
3.62e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1258 VVLIAAVTSISNSLHRELSAGLvglgltyaLMVSNYLNwMVRNLAD--MELQLGAV---KRIHGLLKTEAESY-EGLLA- 1330
Cdd:PRK15134 189 VSVQAQILQLLRELQQELNMGL--------LFITHNLS-IVRKLADrvAVMQNGRCveqNRAATLFSAPTHPYtQKLLNs 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1331 -PSLIPKNWPDQGK--IQIQNLSV---------RYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDT- 1397
Cdd:PRK15134 260 ePSGDPVPLPEPASplLDVEQLQVafpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSq 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1398 ----FEGHIIIDGIDIAKLPlhtLRSRLSIILQDPvlfsgtiRFNLDPeRKCSDSTLWEALEIAQLKL--------VVKA 1465
Cdd:PRK15134 340 geiwFDGQPLHNLNRRQLLP---VRHRIQVVFQDP-------NSSLNP-RLNVLQIIEEGLRVHQPTLsaaqreqqVIAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1466 LPG-GLDAII-----TEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASID-------MATENILQKVVMTAFadrtv 1532
Cdd:PRK15134 409 MEEvGLDPETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY----- 479
|
330 340
....*....|....*....|....*..
gi 1189438338 1533 VTIAHRVHTILS-ADLVIVLKRGAILE 1558
Cdd:PRK15134 480 LFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1344-1568 |
4.15e-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: 64.52 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLK--PVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFE-------GHIIIDGIDIAKLPL 1414
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsgsvLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1415 HTLRSRLSIILQDPVLFS-----GTIRFNLD---PERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQR 1486
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1487 QLFCLARAFVRKTSIFIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKP 1562
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 1189438338 1563 EKLLSR 1568
Cdd:cd03258 226 EEVFAN 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1344-1538 |
6.26e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.56 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKL-PLHT------ 1416
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRAL--------------AGLwPWGSgrigmp 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1417 LRSRLSIILQDPVLFSGTIRfnldperkcsdstlwealeiaqlklvvkalpgglDAIITEGGENFSQGQRQLFCLARAFV 1496
Cdd:cd03223 62 EGEDLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438338 1497 RKTSIFIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1538
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1344-1512 |
6.31e-11 |
|
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: 63.65 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHII---IDGIDIAKLPLHTLRSR 1420
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILAGLLPPSAgevLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1421 LSIILQDPVLFSG-TIRFNLD-----PERKCSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLFCLARA 1494
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALARL 145
|
170
....*....|....*...
gi 1189438338 1495 FVRKTSIFIMDEATASID 1512
Cdd:COG4133 146 LLSPAPLWLLDEPFTALD 163
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
695-913 |
6.32e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSlpdseigedPSPERETATDLDIRKRgPVAYASQ 774
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ---------PMSKLSSAAKAELRNQ-KLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLL-NATVEENIIFESPFNKQRYKMVIEACSlqpdiDILPH-GDQTQIGERGINLSGGQRQRISVARALYQHANVVFL 852
Cdd:PRK11629 95 FHHLLpDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 853 DDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 913
Cdd:PRK11629 170 DEPTGNLDARNADSIFQL-LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
690-912 |
6.74e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.75 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFWSSSL--------PDSEIGEdPSPE----- 754
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvLRGMDQYEPTSGRIIYHVALcekcgyveRPSKVGE-PCPVcggtl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 755 RETATDL---------DIRKRgpVAYASQKPWLL--NATVEENIIfeSPFNKQRYKmviEACSLQPDIDILphgDQTQIG 823
Cdd:TIGR03269 90 EPEEVDFwnlsdklrrRIRKR--IAIMLQRTFALygDDTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 824 ER----GINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDhLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADW 898
Cdd:TIGR03269 160 HRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSDK 238
|
250
....*....|....
gi 1189438338 899 IIAMKDGTIQREGT 912
Cdd:TIGR03269 239 AIWLENGEIKEEGT 252
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
697-911 |
9.22e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.44 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMqkVSGAVFwssslpdseIGEdpsperETATDLDIRKRGpVAYASQ 774
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLrmIAGLEDI--TSGDLF---------IGE------KRMNDVPPAERG-VGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 K----PWLlnaTVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARAL 843
Cdd:PRK11000 83 SyalyPHL---SVAENMSFglklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 911
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
688-889 |
1.14e-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: 66.31 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLAALGEMQKVSGAVfwssslpdseigedpsperetatdLDIRKRG 767
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGR------------------------LTKPAKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 PVAYASQKPWLLNATVEENIIF-ESPFNKQRYKMvieacSLQPDIDILPHGDQTQIGERGIN----------LSGGQRQR 836
Cdd:TIGR00954 516 KLFYVPQRPYMTLGTLRDQIIYpDSSEDMKRRGL-----SDKDLEQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQR 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTHK 889
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDECTSAVSVD-----VEGYMYRLCREFGITLFSVSHR 638
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
695-916 |
1.33e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.09 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFwsssLPDSEIGEDPsperetaTDLD-IRKRgpVAY 771
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTIT----VDGEDLTDSK-------KDINkLRRK--VGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQK----PwllNATVEENIIfESP-----FNKQrykmviEACSLQpdIDILphgDQTQIGERG----INLSGGQRQRIS 838
Cdd:COG1126 82 VFQQfnlfP---HLTVLENVT-LAPikvkkMSKA------EAEERA--MELL---ERVGLADKAdaypAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLSdhlmqAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 914
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELV-----GEVLDVMRDlakEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPE 221
|
..
gi 1189438338 915 DF 916
Cdd:COG1126 222 EF 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
691-920 |
1.59e-10 |
|
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: 62.84 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGEDPSPEretatdldIRKRGpVA 770
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL----FDGEDITGLPPHE--------IARLG-IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLL-NATVEENII----------FESPFNKQRYKMVIEACSlqpdiDILphgDQTQIGERG----INLSGGQRQ 835
Cdd:cd03219 79 RTFQIPRLFpELTVLENVMvaaqartgsgLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 836 RISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLK 914
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPD 228
|
....*.
gi 1189438338 915 DFQRSE 920
Cdd:cd03219 229 EVRNNP 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1339-1578 |
1.95e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 63.18 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1339 PDQGKIQIQNLSVRYDSSLK--PVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKL---- 1412
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLI--------------AGLekpt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1413 ---------PLHTLRSRLSIILQDPVLF-----SGTIRFNLDPERKCSDstlwEALEIAQ--LKLV-----VKALPGGLd 1471
Cdd:COG1116 65 sgevlvdgkPVTGPGPDRGVVFQEPALLpwltvLDNVALGLELRGVPKA----ERRERARelLELVglagfEDAYPHQL- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1472 aiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILSADLV 1548
Cdd:COG1116 140 ----------SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDeAVFLADRV 209
|
250 260 270
....*....|....*....|....*....|....*..
gi 1189438338 1549 IVLKRG-----AILEFD--KPEKLLSRKDSVFASFVR 1578
Cdd:COG1116 210 VVLSARpgrivEEIDVDlpRPRDRELRTSPEFAALRA 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
695-902 |
2.01e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLllAALGEM--QKVSGAVFWSsslpdseiGED-PSPERETATDLdiRKR----- 766
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL--ARLLTMieTPTGGELYYQ--------GQDlLKADPEAQKLL--RQKiqivf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 -GPvaYASQKP-WLLNATVEENIIFESPFNKQRYKMVIEA----CSLQPD-IDILPHgdqtqigergiNLSGGQRQRISV 839
Cdd:PRK11308 99 qNP--YGSLNPrKKVGQILEEPLLINTSLSAAERREKALAmmakVGLRPEhYDRYPH-----------MFSGGQRQRIAI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 902
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQelglSYVFISHDLSVVEHiADEVMVM 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
690-888 |
2.42e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.74 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssslpdseigedpsPERETATDLDIRKRGpV 769
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL--------------NGGPLDFQRDSIARG-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQKPWLLNA-TVEENIIFESPFNKQrykmviEACslqpdIDILPHGDQTQIGERGIN-LSGGQRQRISVARALYQHA 847
Cdd:cd03231 76 LYLGHAPGIKTTlSVLENLRFWHADHSD------EQV-----EEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438338 848 NVVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTH 888
Cdd:cd03231 145 PLWILDEPTTALDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
695-915 |
3.03e-10 |
|
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: 62.41 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGA---VFwssslpdseiGEdpspERETATDLDIRKR-GPVA 770
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLF----------GE----RRGGEDVWELRKRiGLVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLLNATVEENII---FESPFNKQRY--KMVIEACSLQPDIDILPHGDQTqIGErginLSGGQRQRISVARALYQ 845
Cdd:COG1119 85 PALQLRFPRDETVLDVVLsgfFDSIGLYREPtdEQRERARELLELLGLAHLADRP-FGT----LSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 846 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP----HAdwiIAMKDGTIQREGTLKD 915
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLAL-LDKLAAEGAPTLVLVTHHVEEIPpgitHV---LLLKDGRVVAAGPKEE 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1344-1556 |
3.20e-10 |
|
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: 60.52 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLrsrLSI 1423
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKS------------------------------TL---MKI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 I--LQDPVlfSGTIRFNldpERKCSDSTLWEALE-----IAQLklvvkalpggldaiiteggenfSQGQRQLFCLARAFV 1496
Cdd:cd03216 46 LsgLYKPD--SGEILVD---GKEVSFASPRDARRagiamVYQL----------------------SVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 1497 RKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1556
Cdd:cd03216 99 RNARLLILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
686-890 |
3.94e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 686 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDpsperETATDLDIRk 765
Cdd:PRK10771 8 TWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN--------GQD-----HTTTPPSRR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 rgPVAYASQKPWLLN-ATVEENI-------IFESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 837
Cdd:PRK10771 72 --PVSMLFQENNLFShLTVAQNIglglnpgLKLNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 838 SVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRD--DKR--TVVLVTHKL 890
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPAL-----RQEMLTLVSQvcQERqlTLLMVSHSL 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1344-1537 |
4.31e-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: 59.38 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdtfeghiiidgidiaklplhtlrsrLSI 1423
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPVLFSGTIRFNldperkcsdstlwEALEIAQLklvvkalpggldaiiteggENFSQGQRQLFCLARAFVRKTSIFI 1503
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 1189438338 1504 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1537
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
695-888 |
4.41e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.17 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAAL-----GEMqKVSGAVFwsSSLPDSEIgedpspeREtatdldIRKRg 767
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLLerptsGSV-LVDGVDL--TALSEREL-------RA------ARRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 pVAYASQKPWLLNA-TVEENIIFesPF------NKQRYKMVIEACSLqpdIDILPHGDQ--TQigerginLSGGQRQRIS 838
Cdd:COG1135 84 -IGMIFQHFNLLSSrTVAENVAL--PLeiagvpKAEIRKRVAELLEL---VGLSDKADAypSQ-------LSGGQKQRVG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 839 VARALyqhAN---VVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTH 888
Cdd:COG1135 151 IARAL---ANnpkVLLCDEATSALDPETTR-----SILDLLKDINRelglTIVLITH 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1344-1556 |
5.51e-10 |
|
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: 60.88 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRSR 1420
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1421 LSIILQDpvlfsgtirFNLDPERKCSDSTLWeALEIAQL--KLVVKALPGGLDAIITEGGEN-----FSQGQRQLFCLAR 1493
Cdd:cd03292 80 IGVVFQD---------FRLLPDRNVYENVAF-ALEVTGVppREIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 1494 AFVRKTSIFIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRvhtilsadlVIVLKRGAI 1556
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHR---------VIALERGKL 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
696-897 |
5.59e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 696 SNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVFWSsslpdseiGEDpsperetatdldIRKRGPvAYAS 773
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLriLAGL--ARPDAGEVLWQ--------GEP------------IRRQRD-EYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 QKPWL--LNA-----TVEENIIFespfnkqrykmvieACSLQPDIDilphGDQT-----QIGERGI------NLSGGQRQ 835
Cdd:PRK13538 75 DLLYLghQPGiktelTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 836 RISVARALYQHANVVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTHklQYLPHAD 897
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH--QDLPVAS 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
697-915 |
5.65e-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: 62.81 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLL--LAAL-----GEMQkVSGAVfwsssLPDSEIGEDPSPERetatdldirkRgPV 769
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLraIAGLerpdsGRIR-LGGEV-----LQDSARGIFLPPHR----------R-RI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQK----PWLlnaTVEENIIF---ESPFNKQRYKM--VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVA 840
Cdd:COG4148 80 GYVFQEarlfPHL---SVRGNLLYgrkRAPRAERRISFdeVVELLGIGHLLDRRPA-----------TLSGGERQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 841 RALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRT-VVLVTHKL---QYLphADWIIAMKDGTIQREGTLKD 915
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILP--YLERLRDELDIpILYVSHSLdevARL--ADHVVLLEQGRVVASGPLAE 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
695-927 |
5.73e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.57 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL-------LAALGEMQkVSGAVFWSSSLPDseigedpsperetatDLDIRK-R 766
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLrvlnlleMPRSGTLN-IAGNHFDFSKTPS---------------DKAIRElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GPVAYASQK----PWLlnaTVEENIIfESPFN---------KQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQ 833
Cdd:PRK11124 82 RNVGMVFQQynlwPHL---TVQQNLI-EAPCRvlglskdqaLARAEKLLERLRLKPYADRFP-----------LHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 834 RQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 912
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
250
....*....|....*
gi 1189438338 913 LKDFQRSECQLFEHW 927
Cdd:PRK11124 225 ASCFTQPQTEAFKNY 239
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1063-1225 |
8.16e-10 |
|
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: 61.63 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1063 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1142
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1143 SRSTLLCVSALAVISYV----TPVFLVALLPLAIVCYFIQKYFRVASRDL-QQLDDttqlpLLSHFAETVEGLTTIRAFR 1217
Cdd:cd18544 123 IGDLLLLIGILIAMFLLnwrlALISLLVLPLLLLATYLFRKKSRKAYREVrEKLSR-----LNAFLQESISGMSVIQLFN 197
|
....*...
gi 1189438338 1218 YEARFQQK 1225
Cdd:cd18544 198 REKREFEE 205
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
695-913 |
9.00e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 59.64 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEmqkvSGAVFWSSSLPdseigedpsperetatdldirkrgpvAYASQ 774
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLP--------------------------KFSRN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KpwllnatveenIIFESpfnkqrykmvieacSLQPDIDI----LPHGDQTQigergiNLSGGQRQRISVARALYQHA-NV 849
Cdd:cd03238 61 K-----------LIFID--------------QLQFLIDVglgyLTLGQKLS------TLSGGELQRVKLASELFSEPpGT 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 850 VF-LDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 913
Cdd:cd03238 110 LFiLDEPSTGLHQQDINQLL--EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKV 172
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1344-1542 |
2.32e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM------------VDTFEGHIIIDgidiaK 1411
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesevrvegrVEFFNQNIYER-----R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1412 LPLHTLRSRLSIILQDPVLFSGTI---------------RFNLDP--ERKCSDSTLWEalEIAQlKLVVKALpggldaii 1474
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVydnvaygvkivgwrpKLEIDDivESALKDADLWD--EIKH-KIHKSAL-------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 1475 teggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1542
Cdd:PRK14258 150 -----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1082-1229 |
2.46e-09 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 60.19 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1082 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP 1161
Cdd:cd18576 57 IYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 1162 ---VFLVALLP-LAIVCYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAF---RYEA-RFQQKLLEY 1229
Cdd:cd18576 137 kltLLMLATVPvVVLVAVLFGRRIRKLSKKVQdELAEAN-----TIVEETLQGIRVVKAFtreDYEIeRYRKALERV 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1343-1568 |
2.55e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.03 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1343 KIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1422
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1423 IILQDP-VLFSGT-----IRFNLDpERKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFV 1496
Cdd:PRK13635 85 MVFQNPdNQFVGAtvqddVAFGLE-NIGVPREEMVERVDQA-LRQV------GMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 1497 RKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1568
Cdd:PRK13635 157 LQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1344-1557 |
2.66e-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: 58.92 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFeghiiidgidiaklplhtLRSRL 1421
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGL------------------LEPDA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIIL-------QDPVLFSGTIRFNLDPERKCSDSTLWEALEI---------AQLKLVVKALPGGLD--AIITEGGENFSQ 1483
Cdd:cd03266 60 GFATvdgfdvvKEPAEARRRLGFVSDSTGLYDRLTARENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFST 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1484 GQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAIL 1557
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
690-920 |
3.03e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 59.23 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGED---PSPERetatdldIRKR 766
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD--------GEDitgLPPHR-------IARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GpVAYASQK----PWLlnaTVEENII--FESPFNKQRYKMVIEACslqpdIDILPhgdqtQIGER----GINLSGGQRQR 836
Cdd:COG0410 79 G-IGYVPEGrrifPSL---TVEENLLlgAYARRDRAEVRADLERV-----YELFP-----RLKERrrqrAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKD 915
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFE--IIRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAE 222
|
....*
gi 1189438338 916 FQRSE 920
Cdd:COG0410 223 LLADP 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
695-911 |
3.07e-09 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 58.74 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGqLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETatdldIRKRgpVAYASQ 774
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRID--------GQDVLKQPQK-----LRRR--IGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KP-WLLNATVEENIIF-------ESPFNKQRYKMVIEAcslqpdIDILPHGDQtQIGErginLSGGQRQRISVARALYQH 846
Cdd:cd03264 80 EFgVYPNFTVREFLDYiawlkgiPSKEVKARVDEVLEL------VNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 847 ANVVFLDDPFSALD----IHLSDHLMQAGilellrdDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 911
Cdd:cd03264 149 PSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1090-1226 |
3.42e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 59.77 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1090 LKVAKRLHRSLL----NRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPST-LECLSRSTLLCVSALAVISYVTPVFL 1164
Cdd:cd18570 67 LKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 1165 VALLPL---AIVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFRYEARFQQKL 1226
Cdd:cd18570 146 ITLLIIplyILIILLFNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKKI 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1344-1569 |
3.72e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRY---DSSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP- 1413
Cdd:PRK10261 314 LQVRNLVTRFplrSGLLNRVTREVHAVekvsfdLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1414 --LHTLRSRLSIILQDPVLfsgtirfNLDPERKCSDSTLwEALEIAQLkLVVKALPGGLDAIITEGG----------ENF 1481
Cdd:PRK10261 394 gkLQALRRDIQFIFQDPYA-------SLDPRQTVGDSIM-EPLRVHGL-LPGKAAAARVAWLLERVGllpehawrypHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1482 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NI---LQKVVMTAFA----DRTVVT-IAHRVHTILSADLVI 1549
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLlldLQRDFGIAYLfishDMAVVErISHRVAVMYLGQIVE 544
|
250 260
....*....|....*....|
gi 1189438338 1550 VLKRGAIleFDKPEKLLSRK 1569
Cdd:PRK10261 545 IGPRRAV--FENPQHPYTRK 562
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
695-912 |
4.06e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQ----KVSGAVFWssslpdseIGEDpsperetATDLD-IRKRG 767
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYdskiKVDGKVLY--------FGKD-------IFQIDaIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 PVAYASQKP-WLLNATVEENIIFesPF------NKQRYKMVIEACSLQPDIDILPHgdqTQIGERGINLSGGQRQRISVA 840
Cdd:PRK14246 91 EVGMVFQQPnPFPHLSIYDNIAY--PLkshgikEKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 841 RALYQHANVVFLDDPFSALDIhLSDHLMQAGILELlrDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 912
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDI-VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
684-920 |
4.23e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.37 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 684 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIgedpspeRETATDLDI 763
Cdd:PRK13649 12 YQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV----RVDDTLI-------TSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RK-RGPVAYASQKPWllNATVEENIIFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 841
Cdd:PRK13649 81 KQiRKKVGLVFQFPE--SQLFEETVLKDVAFGPQNFGVsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 842 ALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRS 919
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDiFQDV 236
|
.
gi 1189438338 920 E 920
Cdd:PRK13649 237 D 237
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
695-902 |
4.37e-09 |
|
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: 58.42 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSL---LLAALGEMQKVSGAvfwsSSLPDSEIGEDPSPERETATDLdirkrGPVAY 771
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdTIYAEGQRRYVESL----SAYARQFLGQMDKPDVDSIEGL-----SPAIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQKPWLLN-----ATVEE-----NIIFESPFNKQRYKMVIEacslqpdidilphgdqtqIG------ERGIN-LSGGQR 834
Cdd:cd03270 82 IDQKTTSRNprstvGTVTEiydylRLLFARVGIRERLGFLVD------------------VGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 835 QRISVARALyqHANVV----FLDDPFSALdiHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 902
Cdd:cd03270 144 QRIRLATQI--GSGLTgvlyVLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
695-915 |
5.09e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.05 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSslpdseigedpsperETATDLDIRK-RGPVAYAS 773
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG---------------EPITKENIREvRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 QKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARAL 843
Cdd:PRK13652 85 QNPddQIFSPTVEQDIAF-GPINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEE 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1344-1556 |
5.70e-09 |
|
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: 57.92 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDpvlfsgtirFNLDPE--------------RKCSDStlwEALEIAQ--LKLVvkalpgGLDAIITEGGENFSQGQ 1485
Cdd:cd03262 79 GMVFQQ---------FNLFPHltvlenitlapikvKGMSKA---EAEERALelLEKV------GLADKADAYPAQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1486 RQLFCLARAFVRKTSIFIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1556
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
695-920 |
6.33e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.95 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdseigeDPSPERETATDL-DIRKRGPVAYAS 773
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV-------------KIDGELLTAENVwNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 QKPWLLNATVEENIIF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHANV 849
Cdd:PRK13642 90 PDNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDF-----KTREPAR---LSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 850 VFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 920
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRV-IHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSElFATSE 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1363-1556 |
6.37e-09 |
|
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: 57.89 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1363 HVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKLPLHTLRSR--LSIILQDPVLFSG-TIRFNL 1439
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL----LNLIAGFETPQSGRVLINGVDVTAAPPADrpVSMLFQENNLFAHlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1440 DPERkcsdSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIL 1519
Cdd:cd03298 92 GLGL----SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438338 1520 QKVVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1556
Cdd:cd03298 168 LDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
693-920 |
6.49e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.97 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPEretaTDLDIRKRGPVAYA 772
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID--------GDLLTEE----NVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKPWLLNATVEENIIF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHAN 848
Cdd:PRK13650 89 NPDNQFVGATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDF-----KEREPAR---LSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 849 VVFLDDPFSALDihlsdhlmQAGILELLRDDKR-------TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 920
Cdd:PRK13650 161 IIILDEATSMLD--------PEGRLELIKTIKGirddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSRGN 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
687-907 |
6.60e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 58.21 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 687 WTPDGIPT-LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGemQKVSGAVFWSsslpdseiGEDPSP--ERETATdl 761
Cdd:COG4181 19 GTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLglLAGLD--RPTSGTVRLA--------GQDLFAldEDARAR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 dIRKRGpVAYASQKPWLLNA-TVEENI-----IFESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQ 835
Cdd:COG4181 87 -LRARH-VGFVFQSFQLLPTlTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 836 RISVARALYQHANVVFLDDPFSALDIHLSDHlmqagILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDGTI 907
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQ-----IIDLLFELNRergtTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
691-911 |
6.66e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssslpdseIGEDPSPERETATDLDirkrGPVA 770
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---------IDGQEMRFASTTAALA----AGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLL-NATVEENII---FESPFNKQRYKMVIEACSLQPD---IDILPhgdQTQIGErginLSGGQRQRISVARAL 843
Cdd:PRK11288 83 IIYQELHLVpEMTVAENLYlgqLPHKGGIVNRRLLNYEAREQLEhlgVDIDP---DTPLKY----LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLqylphaDWIIAMKDG-TIQREG 911
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
690-912 |
6.79e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 57.76 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKVSGAVFwssslpdseiGEDPSpeRETAtdlDIRKRg 767
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTikMLTTLLKPTSGRATVA----------GHDVV--REPR---EVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 768 pVAYASQKPWLLNA-TVEENI-IFESPFN------KQRYKMVIEAcslqpdIDILPHGDqtqigERGINLSGGQRQRISV 839
Cdd:cd03265 75 -IGIVFQDLSVDDElTGWENLyIHARLYGvpgaerRERIDELLDF------VGLLEAAD-----RLVKTYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 840 ARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGT 912
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGT 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
690-918 |
7.31e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.08 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLpdsEIGEDPSpERETatdLDirkrgpv 769
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV---KIGYFDQ-HQEE---LD------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 ayasqkpwlLNATVEENIifeSPFNKQRYKMVIEACsLQpdiDILPHGDQ--TQIGergiNLSGGQRQRISVARALYQHA 847
Cdd:COG0488 392 ---------PDKTVLDEL---RDGAPGGTEQEVRGY-LG---RFLFSGDDafKPVG----VLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 848 NVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ-REGTLKDFQR 918
Cdd:COG0488 452 NVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHdryfldRV-----ATRILEFEDGGVReYPGGYDDYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
690-906 |
7.54e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 55.92 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPdseigedpsperetatdldirkrgpV 769
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-------------------------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 770 AYASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANV 849
Cdd:cd03221 66 GYFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 850 VFLDDPFSALDIHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGT 906
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEA-----LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
695-912 |
7.56e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 58.39 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSL----LLAAL-----------GEMQKVSGAVF--WSSSLPDSEIGEDPSPERET 757
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtLYPALarrlhlkkeqpGNHDRIEGLEHidKVIVIDQSPIGRTPRSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 758 ATDL--DIR---------KRgpvaYASQKpwL------------LNATVEENIIFESPFNKQRYKmvieacsLQPDIDIl 814
Cdd:cd03271 91 YTGVfdEIRelfcevckgKR----YNRET--LevrykgksiadvLDMTVEEALEFFENIPKIARK-------LQTLCDV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 815 phG-DQTQIGERGINLSGGQRQRISVARALYQHAN---VVFLDDPFSALdiHLSD--HLMQagILELLRDDKRTVVLVTH 888
Cdd:cd03271 157 --GlGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL--HFHDvkKLLE--VLQRLVDKGNTVVVIEH 230
|
250 260 270
....*....|....*....|....*....|
gi 1189438338 889 KLQYLPHADWIIAM------KDGTIQREGT 912
Cdd:cd03271 231 NLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
829-905 |
8.46e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 58.31 E-value: 8.46e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 829 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINL-MLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1344-1566 |
9.14e-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: 58.17 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF-SLAFFRM-----------------VDTFEghiiid 1405
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLpptygndvrlfgerrggEDVWE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1406 gidiaklplhtLRSRLSII---LQDPVLFSGTIR-------FnldperkcsDST-LWEALEIAQLKLVVKALPG-GLDAI 1473
Cdd:COG1119 76 -----------LRKRIGLVspaLQLRFPRDETVLdvvlsgfF---------DSIgLYREPTDEQRERARELLELlGLAHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1474 ItegGENF---SQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILSA- 1545
Cdd:COG1119 136 A---DRPFgtlSQGEQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGi 210
|
250 260
....*....|....*....|.
gi 1189438338 1546 DLVIVLKRGAILEFDKPEKLL 1566
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1344-1569 |
1.05e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHT------- 1416
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpdvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1417 LRSRLSIILQDPVLFSG-TIRFNLDPERKCSD--STLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLAR 1493
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1494 AFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILSADLVIVLKRGAILE-------FDKPEKL 1565
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgptrkvFENPEHE 242
|
....
gi 1189438338 1566 LSRK 1569
Cdd:PRK14267 243 LTEK 246
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1344-1556 |
1.42e-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: 56.73 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLrsrL 1421
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS------------------------------TL---L 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SII--LQDPVlfSGTIRFNLDPERKCSDSTLWE--------------------ALEIAQLKLVVKALPG----------- 1468
Cdd:cd03255 48 NILggLDRPT--SGEVRVDGTDISKLSEKELAAfrrrhigfvfqsfnllpdltALENVELPLLLAGVPKkerreraeell 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1469 ---GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRvHT 1541
Cdd:cd03255 126 ervGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTHD-PE 202
|
250
....*....|....*.
gi 1189438338 1542 ILS-ADLVIVLKRGAI 1556
Cdd:cd03255 203 LAEyADRIIELRDGKI 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1348-1554 |
1.87e-08 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 56.02 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1348 NLSVRYDSSL----KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVdtfEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:cd03213 8 NLTVTVKSSPsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTG---LGVSGEVLINGRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLFsgtirfnldperkcSDSTLWEALEI-AQLKlvvkalpgGLdaiiteggenfSQGQRQLFCLARAFVRKTS 1500
Cdd:cd03213 85 GYVPQDDILH--------------PTLTVRETLMFaAKLR--------GL-----------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1501 IFIMDEATASIDMATENILQKVVMtAFAD--RTVVTIAHRVHTIL--SADLVIVLKRG 1554
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
695-926 |
2.15e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.00 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSP-ERETATDLdirkRGPVAYAS 773
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR--------GEPLAKlNRAQRKAF----RRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 Q-KPWLLNA--TVEEnIIFE--------SPFNKQ-RYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVA 840
Cdd:PRK10419 96 QdSISAVNPrkTVRE-IIREplrhllslDKAERLaRASEMLRAVDLDDSVlDKRPP-----------QLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 841 RALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLkd 915
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQqfgtACLFITHDLRLVERfCQRVMVMDNGQIVETQPV-- 236
|
250
....*....|.
gi 1189438338 916 fqrSECQLFEH 926
Cdd:PRK10419 237 ---GDKLTFSS 244
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1344-1581 |
2.22e-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: 56.93 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPVLFSG-TIRFN--LDPerkcsdsTL--WEALEIAQ-----LKLVvkalpgGLDaiITEGGENF----SQGQRQLF 1489
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVP-------KLlkWPKEKIREradelLALV------GLD--PAEFADRYphelSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1490 CLARAFVRKTSIFIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILSADLVIVLKRGAILEFDKP 1562
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTP 220
|
250 260
....*....|....*....|
gi 1189438338 1563 EKLLSRKDSVF-ASFVRADK 1581
Cdd:cd03295 221 DEILRSPANDFvAEFVGADR 240
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
830-907 |
2.43e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.86 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 830 SGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKRT----VVLVTHKL---QYLPHAdwIIAM 902
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225
|
....*
gi 1189438338 903 KDGTI 907
Cdd:PRK11701 226 KQGRV 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1572 |
3.25e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.68 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPV-LFSGTI-----RFNLDPErkcsdstlweALEIAQLKLVVKALPGGLDAIITEGGE--NFSQGQRQLFCLARAF 1495
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENH----------AVPYDEMHRRVSEALKQVDMLERADYEpnALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1496 VRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSV 1572
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
695-941 |
3.43e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.15 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslPDSEIG----EDPSPERETATD---------L 761
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---KGLRIGylpqEPPLDDDLTVLDtvldgdaelR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 DIRKRgpVAYASQKPwllnATVEENII--------FESpfnkqrykmvIEACSLQPDIDI------LPHGDQTQ-IGErg 826
Cdd:COG0488 91 ALEAE--LEELEAKL----AEPDEDLErlaelqeeFEA----------LGGWEAEARAEEilsglgFPEEDLDRpVSE-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 827 inLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlsdhlmqaGIL---ELLRDDKRTVVLVTH------KLqylphAD 897
Cdd:COG0488 153 --LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE--------SIEwleEFLKNYPGTVLVVSHdryfldRV-----AT 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1189438338 898 WIIAMKDGTIQR-EGTLKDFQRSECQLFEHWKTLMNRQDQELEKE 941
Cdd:COG0488 218 RILELDRGKLTLyPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKE 262
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
695-888 |
3.44e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssslpdsEIGEDPSPERETATDlDIRKRGPVAYASQ 774
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-------DVPDNQFGREASLID-AIGRKGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 kpwLLNAT-VEENIIFESPFNkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHANVVFLD 853
Cdd:COG2401 118 ---LLNAVgLSDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1189438338 854 DPFSALDIHLSdHLMQAGILELLRDDKRTVVLVTH 888
Cdd:COG2401 162 EFCSHLDRQTA-KRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
695-920 |
4.18e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKVSGAvfwssslpdsEIGEDPSPERETATDLDIRKrgpVAYASQ 774
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPPSEG----------EILLDAQPLESWSSKAFARK---VAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 K-PWLLNATVEENI-IFESP-------FNKQRYKMVIEACSLqpdIDILPhgdqtqIGERGIN-LSGGQRQRISVARALY 844
Cdd:PRK10575 93 QlPAAEGMTVRELVaIGRYPwhgalgrFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 845 QHANVVFLDDPFSALDI-HLSDHLmqAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSE 920
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
693-911 |
4.36e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVfwsssLPDSEIGEDPSperetATDLDIRKRGPVA 770
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcINKLEEIT--SGDL-----IVDGLKVNDPK-----VDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YasQKPWLL-NATVEENIIFeSPFnkqRYKMVIEACSLQPDIDILphgDQTQIGERG----INLSGGQRQRISVARALYQ 845
Cdd:PRK09493 83 F--QQFYLFpHLTALENVMF-GPL---RVRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 846 HANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 911
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
692-891 |
4.86e-08 |
|
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: 55.80 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 692 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdSEIGEDPSPEREtatdlDIRKRGPVAY 771
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV--------RVAGLVPWKRRK-----KFLRRIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 A--SQKPWLLNATVEENI---IFESPfnKQRYKMVIEACSlqpdiDILPHGDQTQIGERgiNLSGGQRQRISVARALYQH 846
Cdd:cd03267 101 GqkTQLWWDLPVIDSFYLlaaIYDLP--PARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1189438338 847 ANVVFLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQ 891
Cdd:cd03267 172 PEILFLDEPTIGLDVV-AQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
829-916 |
5.70e-08 |
|
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: 57.39 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 829 LSGGQRQRISVARALyqhAN---VVFLDDPFSALDIHLsdhlmQAGILELLRDDKRT----VVLVTHKL----QYlphAD 897
Cdd:COG4172 157 LSGGQRQRVMIAMAL---ANepdLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLgvvrRF---AD 225
|
90
....*....|....*....
gi 1189438338 898 WIIAMKDGTIQREGTLKDF 916
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAEL 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
695-915 |
5.82e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.99 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLllaalgeMQKVSGAVFWSSSLPDSeIGEDPSPERETATDLDIRKRGPVAYASQ 774
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTL-------MQHFNALLKPSSGTITI-AGYHITPETGNKNLKKLRKKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALYQH 846
Cdd:PRK13641 95 EAQLFENTVLKDVEF-GPKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHLMQagileLLRDDKR---TVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 915
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQ-----LFKDYQKaghTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKE 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1344-1568 |
7.13e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.12 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFsLAFFRMVDTFEGHIIIDGIDIAKLP---------- 1413
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEPTSGRIIYHVALCEkcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1414 --------------------------LHTLRSRLSIILQDPvlfsgtirFNLDPERKCSDSTLwEALEIAQLKlVVKALP 1467
Cdd:TIGR03269 78 vgepcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRT--------FALYGDDTVLDNVL-EALEEIGYE-GKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1468 GGLDAI--------ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH 1537
Cdd:TIGR03269 148 RAVDLIemvqlshrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSH 227
|
250 260 270
....*....|....*....|....*....|..
gi 1189438338 1538 RVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1568
Cdd:TIGR03269 228 WPEVIEDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
691-920 |
7.99e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllaalgeMQKVSGAVfwsssLPDS---EIGEDP----SPERetATDLDI 763
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTL-------MKIIAGIV-----PPDSgtlEIGGNPcarlTPAK--AHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 rkrgpvaY-ASQKPWLL-NATVEENIIFESPFNKQRYKMVIE-----ACSLQPDIdilphgdqtQIGergiNLSGGQRQR 836
Cdd:PRK15439 89 -------YlVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDS---------SAG----SLEVADRQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 915
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTAD 226
|
....*
gi 1189438338 916 FQRSE 920
Cdd:PRK15439 227 LSTDD 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
695-912 |
9.45e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.20 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWS----SSLPDSEIgedpspeRETatdldirKRGPVA 770
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAEL-------REV-------RRKKIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLL-NATVEENIIFESPFN----KQRYKMVIEACSlQPDIDILPHGDQTQigerginLSGGQRQRISVARALYQ 845
Cdd:PRK10070 110 MVFQSFALMpHMTVLDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 846 HANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK10070 182 NPDILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1091-1225 |
9.77e-08 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 55.49 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1091 KVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVF-LVALL- 1168
Cdd:cd18547 75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtLIVLVt 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1169 -PLAIVC-YFI----QKYFRVASRDLQQLDdttqlpllSHFAETVEGLTTIRAFRYEARFQQK 1225
Cdd:cd18547 155 vPLSLLVtKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEE 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1344-1559 |
1.10e-07 |
|
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: 54.12 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQkIGICGRTGSGKSSFslafFRMVDTF----EGHIIIDGIDIAKLPlHTLRS 1419
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTL----MRILATLtppsSGTIRIDGQDVLKQP-QKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1420 RLSIILQDPVLFSG-TIRFNLD--------PERKCsDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1490
Cdd:cd03264 73 RIGYLPQEFGVYPNfTVREFLDyiawlkgiPSKEV-KARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 1491 LARAFVRKTSIFIMDEATASID----MATENILQKVVmtafADRTVVTIAHRVHTILS-ADLVIVLKRGAILEF 1559
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG----EDRIVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
695-920 |
1.11e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.22 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMqkvSGAVFWSSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQ 774
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLLnaTVEENIIFespfnkQRYKMVIEACSL-QPDIDILPH-----GDQTQIGERGINLSGGQRQRISVARALYQ--- 845
Cdd:PRK13547 94 PAFAF--SAREIVLL------GRYPHARRAGALtHRDGEIAWQalalaGATALVGRDVTTLSGGELARVQFARVLAQlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 846 -HANVV-----FLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQR 918
Cdd:PRK13547 166 pHDAAQpprylLLDEPTAALDLA-HQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVLT 244
|
..
gi 1189438338 919 SE 920
Cdd:PRK13547 245 PA 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
690-905 |
1.19e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFWS------SSLPDSEigedpsperetatdl 761
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMkvLSGVYPHGTYEGEIIFEgeelqaSNIRDTE--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 762 dirkRGPVAYASQKPWLL-NATVEENIIFES---PFNKQRY-KMVIEACSL--QPDIDILPHgdqTQIGergiNLSGGQR 834
Cdd:PRK13549 81 ----RAGIAIIHQELALVkELSVLENIFLGNeitPGGIMDYdAMYLRAQKLlaQLKLDINPA---TPVG----NLGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 835 QRISVARALYQHANVVFLDDPFSALDIHLSDHLmqagiLELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVL-----LDIIRDLKAhgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
690-860 |
1.24e-07 |
|
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: 53.81 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLA---ALGEMQKVSGAVFWSsslpdseiGEDPSPERETAtdldirkR 766
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYN--------GIPYKEFAEKY-------P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GPVAYASQK----PWLlnaTVEENIIFespfnkqrykmvieACSLQpdidilphGDQTQigeRGInlSGGQRQRISVARA 842
Cdd:cd03233 83 GEIIYVSEEdvhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEA 132
|
170
....*....|....*...
gi 1189438338 843 LYQHANVVFLDDPFSALD 860
Cdd:cd03233 133 LVSRASVLCWDNSTRGLD 150
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
678-917 |
1.25e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 678 VQIMGGYFTWTPDGIptLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGED-PSPERE 756
Cdd:PRK11831 8 VDMRGVSFTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD--------GENiPAMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 757 TAtdLDIRKRGPVAYASqKPWLLNATVEENIIF--------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiN 828
Cdd:PRK11831 78 RL--YTVRKRMSMLFQS-GALFTDMNVFDNVAYplrehtqlPAPLLHSTVMMKLEAVGLRGAAKLMPS-----------E 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 829 LSGGQRQRISVARALYQHANVVFLDDPFSALD-------IHLSDHLMQA-GIlellrddkrTVVLVTHKL-QYLPHAD-- 897
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDpitmgvlVKLISELNSAlGV---------TCVVVSHDVpEVLSIADha 214
|
250 260
....*....|....*....|
gi 1189438338 898 WIIAmkDGTIQREGTLKDFQ 917
Cdd:PRK11831 215 YIVA--DKKIVAHGSAQALQ 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1344-1570 |
1.29e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVD-TFEGHIIIDGIDIAKLPLHT---LR 1418
Cdd:PRK13650 5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDgLLEAESGQIIIDGDLLTEENvwdIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1419 SRLSIILQDP-VLFSGT-----IRFNLDP---ERKCSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLF 1489
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGAtveddVAFGLENkgiPHEEMKERVNEALELV-----------GMQDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1490 CLARAFVRKTSIFIMDEATASID--------MATENILQKVVMTafadrtVVTIAHRVHTILSADLVIVLKRGAILEFDK 1561
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQMT------VISITHDLDEVALSDRVLVMKNGQVESTST 223
|
....*....
gi 1189438338 1562 PEKLLSRKD 1570
Cdd:PRK13650 224 PRELFSRGN 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
829-910 |
1.35e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 829 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQ 908
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL-LFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
..
gi 1189438338 909 RE 910
Cdd:PRK10584 226 EE 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
828-890 |
1.43e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 1.43e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 828 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKL 890
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKL 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
690-905 |
1.46e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.99 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 690 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFWSSS-LPDSEIgedpspeRETatdldirKR 766
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWSGSpLKASNI-------RDT-------ER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 767 GPVAYASQKPWLL-NATVEENIIFES----PFNKQRYKMVIEACS---LQPDIDILPhgDQTQIGERGinlsGGQRQRIS 838
Cdd:TIGR02633 78 AGIVIIHQELTLVpELSVAENIFLGNeitlPGGRMAYNAMYLRAKnllRELQLDADN--VTRPVGDYG----GGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETE-----ILLDIIRDLKAhgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1344-1558 |
1.68e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.90 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM---------VDTFEghiiIDGIDIAKLPL 1414
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEerptsgqvlVNGQD----LSRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1415 htLRSRLSIILQDpvlfsgtirFNLDPERkcsdsTLWE----ALEIAQ-------------LKLV-----VKALPGGLda 1472
Cdd:COG2884 77 --LRRRIGVVFQD---------FRLLPDR-----TVYEnvalPLRVTGksrkeirrrvrevLDLVglsdkAKALPHEL-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1473 iiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTILSADL- 1547
Cdd:COG2884 139 ---------SGGEQQRVAIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELVDRMPKr 206
|
250
....*....|.
gi 1189438338 1548 VIVLKRGAILE 1558
Cdd:COG2884 207 VLELEDGRLVR 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
828-957 |
1.69e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 828 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 902
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVI 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438338 903 KDGTIQREGTLKDfqrsecqLFEHWKTLMNRQ------DQELEkETVTERKATEPPQGLSR 957
Cdd:PRK11153 215 DAGRLVEQGTVSE-------VFSHPKHPLTREfiqstlHLDLP-EDYLARLQAEPTTGSGP 267
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
691-915 |
2.60e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllaalgeMQKVSGAVFWSSSLPDSEIGEDPSPERETATDLDIrkrgPVA 770
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTL-------MKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI----GII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YasQKPWLLNA-TVEENI--------------IFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQ 835
Cdd:PRK09700 86 Y--QELSVIDElTVLENLyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 836 RISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 914
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVS 230
|
.
gi 1189438338 915 D 915
Cdd:PRK09700 231 D 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1579 |
2.89e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.97 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDP--VLFSGTI-------RFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARA 1494
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1495 FVRKTSIFIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEkLLSR 1568
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTD 227
|
250
....*....|.
gi 1189438338 1569 KDSVFASFVRA 1579
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1057-1245 |
2.92e-07 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 53.96 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1057 TLDQTVYAMVFTVLCSLGIVLCL------VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNT 1130
Cdd:cd18554 36 TLDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1131 IDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVA---LLPLAIVC-YFIQKYFRVASRDLQQLDDTTQlpllSHFAET 1206
Cdd:cd18554 116 TKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFYILAvKYFFGRLRKLTKERSQALAEVQ----GFLHER 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 1189438338 1207 VEGLTTIRAFRYEARFQQkllEYTDSNNiasLFLTAANR 1245
Cdd:cd18554 192 IQGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
689-912 |
3.33e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.46 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgemQKVSGAvfwssslpDSEIGEDPSPERETAtDLDIRK- 765
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLrmVAGL---ERITSG--------EIWIGGRVVNELEPA-DRDIAMv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 ------------RGPVAYAsqkpwLLNATVEENIIfespfnKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQ 833
Cdd:PRK11650 82 fqnyalyphmsvRENMAYG-----LKIRGMPKAEI------EERVAEAARILELEPLLDRKPR-----------ELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 834 RQRISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
698-911 |
3.58e-07 |
|
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: 52.76 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 698 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdsEI-GEDPSPERetatdLDIRKRGPVAYASQK- 775
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA---------TVdGFDVVKEP-----AEARRRLGFVSDSTGl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 776 -PWLlnaTVEENIIFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARALYQHA 847
Cdd:cd03266 90 yDRL---TARENLEYFAGLYglkgdelTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 848 NVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 911
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
689-890 |
3.61e-07 |
|
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: 55.40 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssslpdseIGEdpspeRETATDLDIRKRGP 768
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL---------VGG-----KDIETNLDAVRQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 769 VAYASQKPWLLNATVEENIIFESPFNKQRYkmviEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 848
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438338 849 VVFLDDPFSALDIHlsdhlMQAGILELLRDDK--RTVVLVTHKL 890
Cdd:TIGR01257 1082 VVVLDEPTSGVDPY-----SRRSIWDLLLKYRsgRTIIMSTHHM 1120
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1361-1567 |
3.91e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.27 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1361 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRS----RLSIILQDpvlfsgtir 1436
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1437 FNLDPERKCSDSTLWeALEIAQLKLVVKAlPGGLDAIITEGGENF--------SQGQRQLFCLARAFVRKTSIFIMDEAT 1508
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 1509 ASID--MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
695-907 |
4.00e-07 |
|
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: 52.05 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPERETatdlDIRKRGpVAYAS- 773
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD--------GKPVTRRSPR----DAIRAG-IAYVPe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 ---QKPWLLNATVEENIIFespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQHANVV 850
Cdd:cd03215 83 drkREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 851 FLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 907
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1007-1572 |
4.03e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1007 AGILLLSLLvfSQLLKHMVLVAIDYWLAKWTDSALTLTPAarncslsqectldqtvyamvFTVLCSLGIVLCLVTSVTVE 1086
Cdd:PRK10522 16 ISVMALSLA--SAALGIGLIAFINQRLIETADTSLLVLPE--------------------FLGLLLLLMAVTLGSQLALT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1087 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID---QHIPStlecLSRSTLLCVSALAVISYVTP-V 1162
Cdd:PRK10522 74 TLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITiafVRLPE----LVQGIILTLGSAAYLAWLSPkM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1163 FLVALLPLAIVcyFIQKYFRVAS-----RDLQQLDDTtqlpLLSHFAETVEG-----LTTIRA-FRYEARFQQKLLEYTD 1231
Cdd:PRK10522 150 LLVTAIWMAVT--IWGGFVLVARvykhmATLRETEDK----LYNDYQTVLEGrkeltLNRERAeYVFENEYEPDAQEYRH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1232 SNNIASLFLTAANRWLEVRMeyIGAcvvlIAAVTSISNSLhrelsaGLVGLGL--TYALMVSNYLNWMVRNLADMELQLG 1309
Cdd:PRK10522 224 HIIRADTFHLSAVNWSNIMM--LGA----IGLVFYMANSL------GWADTNVaaTYSLTLLFLRTPLLSAVGALPTLLS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1310 AVKRIHGLLKTEAESYEGLLAPSLIPKNWPdqgKIQIQNLSVRYDS---SLKPVlkhvNALIAPGQKIGICGRTGSGKSS 1386
Cdd:PRK10522 292 AQVAFNKLNKLALAPYKAEFPRPQAFPDWQ---TLELRNVTFAYQDngfSVGPI----NLTIKRGELLFLIGGNGSGKST 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1387 FSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTirfnLDPERKCSDSTLWEA-LEIAQLKlvvka 1465
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMA----- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1466 lpgglDAIITEGGE----NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRV 1539
Cdd:PRK10522 436 -----HKLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDD 510
|
570 580 590
....*....|....*....|....*....|...
gi 1189438338 1540 HTILSADLVIVLKRGAILEFDKPEKLLSRKDSV 1572
Cdd:PRK10522 511 HYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
695-905 |
4.30e-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: 52.28 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPDSEIGEDPS--PEretatdldirKRGpvAYA 772
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylPE----------ERG--LYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKpwllnatVEENIIFESpfnkQRYKMVIEACSLQPD-----IDILPHGDQtQIGErginLSGGQRQRISVARALYQHA 847
Cdd:cd03269 84 KMK-------VIDQLVYLA----QLKGLKKEEARRRIDewlerLELSEYANK-RVEE----LSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 848 NVVFLDDPFSALDIHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 905
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDV-IRE-LARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
825-911 |
4.63e-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: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 825 RGIN--LSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADWI 899
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRV 175
|
90
....*....|..
gi 1189438338 900 IAMKDGTIQREG 911
Cdd:cd03217 176 HVLYDGRIVKSG 187
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
688-907 |
5.77e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.78 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 688 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAalgemqkVSGAVfwsssLPDS-EI---GEDPSPEREtatdldi 763
Cdd:COG1101 15 TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA-------IAGSL-----PPDSgSIlidGKDVTKLPE------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKRGpvAYAS---QKPwLL----NATVEENII----------FESPFNKQRYKMVIEACSlqpDIDI-LPHGDQTQIGer 825
Cdd:COG1101 76 YKRA--KYIGrvfQDP-MMgtapSMTIEENLAlayrrgkrrgLRRGLTKKRRELFRELLA---TLGLgLENRLDTKVG-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 826 giNLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagiL--ELLRDDKRTVVLVTHKLQY-LPHADWIIAM 902
Cdd:COG1101 148 --LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRLIMM 222
|
....*
gi 1189438338 903 KDGTI 907
Cdd:COG1101 223 HEGRI 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1358-1569 |
7.80e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1358 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIA------KLPLHTLRSRLSIILQDPVLF 1431
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1432 SG-TIRFNLD-PERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1509
Cdd:PRK14246 103 PHlSIYDNIAyPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1510 SIDMATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILE-------FDKPEKLLSRK 1569
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKNELTEK 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
830-893 |
9.38e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 9.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 830 SGGQRQRISVARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKRtvvlvTHKLQYL 893
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSL-----DKTVQAQILALLKSLQQ-----KHQLAYL 480
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1343-1565 |
9.72e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1343 KIQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIdgidiAKLPLH------- 1415
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVE-----GKVTFHgknlyap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1416 -----TLRSRLSIILQDPVLFSGTI-------------RFNLDP--ERKCSDSTLWEALEiAQLKlvvkalpggldaiit 1475
Cdd:PRK14243 83 dvdpvEVRRRIGMVFQKPNPFPKSIydniaygaringyKGDMDElvERSLRQAALWDEVK-DKLK--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1476 EGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVHTI---LSAD 1546
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMtafFNVE 226
|
250 260
....*....|....*....|
gi 1189438338 1547 LVIVLKR-GAILEFDKPEKL 1565
Cdd:PRK14243 227 LTEGGGRyGYLVEFDRTEKI 246
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1479-1577 |
1.09e-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: 51.57 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVIVLKRG 1554
Cdd:cd03299 128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNG 206
|
90 100
....*....|....*....|....
gi 1189438338 1555 AILEFDKPEKLLSRKDSVF-ASFV 1577
Cdd:cd03299 207 KLIQVGKPEEVFKKPKNEFvAEFL 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1344-1572 |
1.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYD-SSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1422
Cdd:PRK13642 5 LEVENLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1423 IILQDP------VLFSGTIRFNLDPE---RKCSDSTLWEALeiaqlkLVVKALPggldaIITEGGENFSQGQRQLFCLAR 1493
Cdd:PRK13642 85 MVFQNPdnqfvgATVEDDVAFGMENQgipREEMIKRVDEAL------LAVNMLD-----FKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1494 AFVRKTSIFIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1570
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
..
gi 1189438338 1571 SV 1572
Cdd:PRK13642 233 DM 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
820-899 |
1.39e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.60 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 820 TQIGERGI-NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPH-AD 897
Cdd:cd03236 130 RHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSD 207
|
..
gi 1189438338 898 WI 899
Cdd:cd03236 208 YI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1342-1577 |
1.60e-06 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 52.00 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1342 GKIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdtfeghiiidgidiaklplhTLRsrl 1421
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKST-----------------------------LLR--- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 sII--LQDPVlfSGTIRFN------LDP-ERKCS----DSTLW----------------------------EALEIAQLK 1460
Cdd:COG3839 48 -MIagLEDPT--SGEILIGgrdvtdLPPkDRNIAmvfqSYALYphmtvyeniafplklrkvpkaeidrrvrEAAELLGLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1461 LVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVVMTafadrTV 1532
Cdd:COG3839 125 DLLDRKPKQL-----------SGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TI 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1533 -VTiahrvH------TIlsADLVIVLKRGAILEFDKPEKLLSRKDSVF-ASFV 1577
Cdd:COG3839 189 yVT-----HdqveamTL--ADRIAVMNDGRIQQVGTPEELYDRPANLFvAGFI 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
692-912 |
1.62e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.03 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 692 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpDSEIGEDPSpERETATDLDIRKRGPVAY 771
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFD----GKDITDWQT-AKIMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQkpwllnaTVEENIIFESPF-NKQRYKMVIEACslqpdIDILPHGDQTQIgERGINLSGGQRQRISVARALYQHANVV 850
Cdd:PRK11614 93 SRM-------TVEENLAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 851 FLDDPfsalDIHLSDHLMQA--GILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 912
Cdd:PRK11614 160 LLDEP----SLGLAPIIIQQifDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
693-918 |
1.68e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.24 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 693 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMqkvsgavfwssslpdseigedPSPERETATDLDIRKRgPVAyA 772
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIL---------------------PAGVRQTAGRVLLDGK-PVA-P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 773 SQKPWLLNATVEENIifESPFNKQRyKM---VIEAC---SLQPDIDILPH-------GDQTQIGER-GINLSGGQRQRIS 838
Cdd:PRK10418 74 CALRGRKIATIMQNP--RSAFNPLH-TMhthARETClalGKPADDATLTAaleavglENAARVLKLyPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 839 VARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKRT----VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTL 913
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDV-----VAQARILDLLESIVQKralgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDV 225
|
....*.
gi 1189438338 914 KD-FQR 918
Cdd:PRK10418 226 ETlFNA 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
692-919 |
1.71e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 692 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPDSEIGEDPSPERETATDLDIRKRGPVAY 771
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQKPWL-LNA--TVEENIIfESPFNKQ---RYKMVIEACSLQPDIDIlPHGdQTQIGERGINLSGGQRQRISVARALYQ 845
Cdd:PRK10261 109 IFQEPMTsLNPvfTVGEQIA-ESIRLHQgasREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 846 HANVVFLDDPFSALDIhlsdhLMQAGILELLR----DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 919
Cdd:PRK10261 186 RPAVLIADEPTTALDV-----TIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1061-1302 |
1.89e-06 |
|
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: 51.31 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1061 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLE 1140
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1141 CLSRSTLLCVSALAVISYVTPVF-LVAL--LP-LAIVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAF 1216
Cdd:cd18545 120 NLIPDLLTLVGIVIIMFSLNVRLaLVTLavLPlLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1217 RYE----ARFQQKLLEYTDSNNIASLFLTAANRWLEVrMEYIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYA----- 1287
Cdd:cd18545 196 AREdeneEIFDELNRENRKANMRAVRLNALFWPLVEL-ISALGTALVYWYGGKLV---LGGAITVGVLVAFIGYVgrfwq 271
|
250
....*....|....*..
gi 1189438338 1288 --LMVSNYLNWMVRNLA 1302
Cdd:cd18545 272 piRNLSNFYNQLQSAMA 288
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1358-1567 |
1.89e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1358 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHT------LRSRLSIILQDPVLF 1431
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyrdvleFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1432 SGTIRFN-LDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATAS 1510
Cdd:PRK14271 114 PMSIMDNvLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1511 IDMATENILQKVVMTaFADR-TVVTIAHRV-HTILSADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:PRK14271 194 LDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
695-872 |
1.91e-06 |
|
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: 50.62 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsssLPDSEIGEDPsperetatdLDIRKRGPVAYASQ 774
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL----LDGQDITKLP---------MHKRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLL-NATVEENI--IFESpFNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHANVVF 851
Cdd:cd03218 83 EASIFrKLTVEENIlaVLEI-RGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLL 156
|
170 180
....*....|....*....|....*...
gi 1189438338 852 LDDPFSALD-IHLSD------HLMQAGI 872
Cdd:cd03218 157 LDEPFAGVDpIAVQDiqkiikILKDRGI 184
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
697-919 |
2.01e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGemqkvsgavfwsssLPDSeigedpsPERETATDLDIRKRGPVAYAS-QK 775
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMG--------------LIDY-------PGRVMAEKLEFNGQDLQRISEkER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 776 PWLLNATVEenIIFESPFN------------------------KQRYKMVIEACSLQ--PD----IDILPHgdqtqiger 825
Cdd:PRK11022 84 RNLVGAEVA--MIFQDPMTslnpcytvgfqimeaikvhqggnkKTRRQRAIDLLNQVgiPDpasrLDVYPH--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 826 giNLSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELL----RDDKRTVVLVTHKLQYLPH-ADWII 900
Cdd:PRK11022 153 --QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-----TIQAQIIELLlelqQKENMALVLITHDLALVAEaAHKII 225
|
250
....*....|....*....
gi 1189438338 901 AMKDGTIQREGTLKDFQRS 919
Cdd:PRK11022 226 VMYAGQVVETGKAHDIFRA 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1346-1387 |
2.33e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.99 E-value: 2.33e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1189438338 1346 IQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1387
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL 40
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1344-1567 |
2.45e-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: 50.13 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTlRSRLSI 1423
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 IL--QDPVLFSG-TIRFNLD-PERKCSDSTLWEALEIaqlklVVKALPgGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1499
Cdd:cd03224 78 GYvpEGRRIFPElTVEENLLlGAYARRRAKRKARLER-----VYELFP-RLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1500 SIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:cd03224 152 KLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1344-1571 |
2.90e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.14 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslkpVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVDT---FEGHIIIDGIDIAKLPLhtlr 1418
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLnlIAGFLPPDSgriLWNGQDLTALPPAERPV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1419 srlSIILQDPVLFSG-TIRFN----LDPERKCSD---STLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1490
Cdd:COG3840 74 ---SMLFQENNLFPHlTVAQNiglgLRPGLKLTAeqrAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1491 LARAFVRKTSIFIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
....
gi 1189438338 1568 RKDS 1571
Cdd:COG3840 220 GEPP 223
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
697-888 |
2.95e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.96 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdSEIGEdPSPERETatdldiRKRGPVAYASQKP 776
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI--------SLCGE-PVPSRAR------HARQRVGVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 777 WL-LNATVEENI-IFESPFN------KQRYKMVIEACSLQPDIDilphgdqTQIGErginLSGGQRQRISVARALYQHAN 848
Cdd:PRK13537 90 NLdPDFTVRENLlVFGRYFGlsaaaaRALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVNDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438338 849 VVFLDDPFSALDIHlSDHLMQAGILELLRDDKrTVVLVTH 888
Cdd:PRK13537 159 VLVLDEPTTGLDPQ-ARHLMWERLRSLLARGK-TILLTTH 196
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
695-957 |
3.44e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVF----WSSSLPDSEIGEDPSPERETATDLDIRKRgpva 770
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnWQLAWVNQETPALPQPALEYVIDGDREYR---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 yasQKPWLLNATVEENiifespfNKQRYKMV------IEACSLQPDIDILPHG---DQTQIGERGINLSGGQRQRISVAR 841
Cdd:PRK10636 93 ---QLEAQLHDANERN-------DGHAIATIhgkldaIDAWTIRSRAASLLHGlgfSNEQLERPVSDFSGGWRMRLNLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 842 ALYQHANVVFLDDPFSALDihlsdhlMQAGI-LE-LLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTI-QREGTLKDFQ 917
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLD-------LDAVIwLEkWLKSYQGTLILISHDRDFLdPIVDKIIHIEQQSLfEYTGNYSSFE 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1189438338 918 RSECQLFEHWKTLMNRQDQELEK-ETVTER---KATEPPQGLSR 957
Cdd:PRK10636 236 VQRATRLAQQQAMYESQQERVAHlQSYIDRfraKATKAKQAQSR 279
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
821-912 |
4.01e-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: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 821 QIGERGINLSGGQRQRISVARALYQHAN---VVFLDDPFSALdiHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPH 895
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKT 897
|
90 100
....*....|....*....|...
gi 1189438338 896 ADWII------AMKDGTIQREGT 912
Cdd:TIGR00630 898 ADYIIdlgpegGDGGGTVVASGT 920
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1344-1567 |
5.03e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 50.61 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDPVL---FSG--TIRFNLDPERK---CSDSTLWEALEIAQLKLVVKALpggLDAIITEggenFSQGQRQLFCLARAF 1495
Cdd:PRK09536 82 VPQDTSLsfeFDVrqVVEMGRTPHRSrfdTWTETDRAAVERAMERTGVAQF---ADRPVTS----LSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1496 VRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLSA---DLVIVLKRGAILEFDKPEKLLS 1567
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPPADVLT 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1344-1558 |
5.59e-06 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 49.27 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDS--SLKPVLKHVNALIAPGQKIGICGRTGSGKSSF----------------------------SLAFFR 1393
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnilggldrptsgevlidgqdisslserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1394 mvdtfeghiiidgidiaklplhtlRSRLSIILQDpvlfsgtirFNLDPE-----------------RKCSDSTLWEALEI 1456
Cdd:COG1136 85 ------------------------RRHIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLER 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1457 AQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFAD---RTV 1532
Cdd:COG1136 132 VGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTI 198
|
250 260
....*....|....*....|....*.
gi 1189438338 1533 VTIAHRVHTILSADLVIVLKRGAILE 1558
Cdd:COG1136 199 VMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1057-1239 |
5.81e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 50.10 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1057 TLDQTVYAMVFTVLCSLGIVLCLVTS-VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHI 1135
Cdd:cd18541 35 TASQLLRYALLILLLALLIGIFRFLWrYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1136 PSTLECLSRSTLLCVSALAVISYVTPVF-LVALLPL---AIVCYFIQKYFRVASRDLQQ----LDDTTQlpllshfaETV 1207
Cdd:cd18541 115 GPGILYLVDALFLGVLVLVMMFTISPKLtLIALLPLpllALLVYRLGKKIHKRFRKVQEafsdLSDRVQ--------ESF 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438338 1208 EGLTTIRAF----RYEARFQQKLLEYTDSNN----IASLF 1239
Cdd:cd18541 187 SGIRVIKAFvqeeAEIERFDKLNEEYVEKNLrlarVDALF 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
691-911 |
5.83e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.71 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLPDseiGEDPSPERETatdLDIRKRgpVA 770
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG---GRSIFNYRDV---LEFRRR--VG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLLNATVEENIIFESPFNK----QRYKMVIEACSLQPDidiLPHGDQTQIGERGINLSGGQRQRISVARALYQH 846
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVG---LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHlmqagILELLRD--DKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREG 911
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEK-----IEEFIRSlaDRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1060-1232 |
6.04e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 49.74 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1060 QTVYAMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1139
Cdd:cd18551 37 GLLALLVALFL--LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1140 -ECLSRSTLLCVS--ALAVISYVTPVFLVALLPLAIVC-YFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1214
Cdd:cd18551 115 pQLVTGVLTVVGAvvLMFLLDWVLTLVTLAVVPLAFLIiLPLGRRIRKASKRAQD-----ALGELSAALErALSAIRTVK 189
|
170
....*....|....*...
gi 1189438338 1215 AFRYEARFQQKLLEYTDS 1232
Cdd:cd18551 190 ASNAEERETKRGGEAAER 207
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1069-1242 |
6.96e-06 |
|
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: 49.80 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1069 VLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILA--------PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLE 1140
Cdd:cd18546 39 LLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRvfahlqrlSLDFHERETSGRIMTRMTSDIDALSELLQTGLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1141 CLSRSTLLCVSALAVISYVTP----VFLVALLPLAIVCYFiqkyFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF 1216
Cdd:cd18546 119 QLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRW----FRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAF 194
|
170 180
....*....|....*....|....*....
gi 1189438338 1217 RYEARFQQKLLEYTDSN---NIASLFLTA 1242
Cdd:cd18546 195 RRERRNAERFAELSDDYrdaRLRAQRLVA 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
697-881 |
7.60e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWS----SSLPDSE----------IGEDPSperetaTDLD 762
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqriDTLSPGKlqalrrdiqfIFQDPY------ASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 763 IRKrgPVAYASQKPWLLNAtveeniIFESPFNKQRYKMVIEACSLQPDIDI-LPHgdqtqigergiNLSGGQRQRISVAR 841
Cdd:PRK10261 416 PRQ--TVGDSIMEPLRVHG------LLPGKAAAARVAWLLERVGLLPEHAWrYPH-----------EFSGGQRQRICIAR 476
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438338 842 ALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR 881
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVSI-----RGQIINLLLDLQR 511
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
829-905 |
7.86e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 829 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 903
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 1189438338 904 DG 905
Cdd:PRK15134 232 NG 233
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
704-888 |
9.13e-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: 47.37 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 704 RGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssslpdseigedpsperetatdldirkrgpvayasqkpwLLNATV 783
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------------------------------YIDGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 784 EENIIFESPFNkqrykmvieacslqpdidilphgdqTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHL 863
Cdd:smart00382 41 ILEEVLDQLLL-------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQ 95
|
170 180
....*....|....*....|....*....
gi 1189438338 864 SDHLMQAGILELL----RDDKRTVVLVTH 888
Cdd:smart00382 96 EALLLLLEELRLLlllkSEKNLTVILTTN 124
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
691-888 |
9.17e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWS----SSLPDSEIgedPSPERETAT---DLDI 763
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdiTRLKNREV---PFLRRQIGMifqDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 764 RKRGPVAYASQKPWLLNATVEENIifespfnKQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQRQRISVARAL 843
Cdd:PRK10908 91 LMDRTVYDNVAIPLIIAGASGDDI-------RRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR---TVVLVTH 888
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSE-----GILRLFEEFNRvgvTVLMATH 195
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1344-1522 |
1.02e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.32 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYD------------SSLKPVlKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAK 1411
Cdd:PRK15079 9 LEVADLKVHFDikdgkqwfwqppKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1412 L---PLHTLRSRLSIILQDPvLFSgtirfnLDPERKCSD------STLWEALEIAQLKLVVKAL---PGGLDAIITEGGE 1479
Cdd:PRK15079 88 MkddEWRAVRSDIQMIFQDP-LAS------LNPRMTIGEiiaeplRTYHPKLSRQEVKDRVKAMmlkVGLLPNLINRYPH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1189438338 1480 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKV 1522
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNLLQQL 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
695-888 |
1.15e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqkvsgAVFWSSSLPDSEIGEDPSPERETATDLDIRKRGpvAYASQ 774
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLM------------NALAFRSPKGVKGSGSVLLNGMPIDAKEMRAIS--AYVQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLLNA-TVEENIIFESPF----------NKQRYKMVIEACSLQPDIDILphgdqTQIGERGINLSGGQRQRISVARAL 843
Cdd:TIGR00955 107 DDLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCANTR-----IGVPGRVKGLSGGERKRLAFASEL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1189438338 844 YQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTH 888
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1344-1387 |
1.26e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.68 E-value: 1.26e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1387
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1064-1314 |
1.43e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 48.66 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1064 AMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1143
Cdd:cd18563 48 GLAGAYV--LSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1144 RSTLLCVSALAVISYVTPVF-LVALLPLAIVCYFIQKYFRVASRDLQQL----DDTTqlpllSHFAETVEGLTTIRAF-- 1216
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLaLLVLIPVPLVVWGSYFFWKKIRRLFHRQwrrwSRLN-----SVLNDTLPGIRVVKAFgq 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1217 -RYE-ARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEyIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYALMVSNYL 1294
Cdd:cd18563 201 eKREiKRFDEANQELLDANIRAEKLWATFFPLLTFLTS-LGTLIVWYFGGRQV---LSGTMTLGTLVAFLSYLGMFYGPL 276
|
250 260
....*....|....*....|
gi 1189438338 1295 NWMVRNLADMELQLGAVKRI 1314
Cdd:cd18563 277 QWLSRLNNWITRALTSAERI 296
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
695-892 |
1.58e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdseigedpsperETATDLDirkrgpVAYASQ 774
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------------------HCGTKLE------VAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLLNA--TVEENIifesPFNKQ------RYKMVIEacSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQH 846
Cdd:PRK11147 390 HRAELDPekTVMDNL----AEGKQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHLMqagilELLRDDKRTVVLVTHKLQY 892
Cdd:PRK11147 459 SNLLILDEPTNDLDVETLELLE-----ELLDSYQGTVLLVSHDRQF 499
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1061-1271 |
1.59e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 48.61 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1061 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLE 1140
Cdd:cd18567 42 TVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1141 CLSRSTLLCVSALAVI-SYVTPVFLVALLPLAIVC---YFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAF 1216
Cdd:cd18567 121 EALLDGLMAILTLVMMfLYSPKLALIVLAAVALYAllrLALYPPLRRATEEQIVASAKEQ----SHFLETIRGIQTIKLF 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 1217 RYEARFQQKLLE-YTDSNN------IASLFLTAANRWLeVRMEYIGacVVLIAAVTSISNSL 1271
Cdd:cd18567 197 GREAEREARWLNlLVDAINadirlqRLQILFSAANGLL-FGLENIL--VIYLGALLVLDGEF 255
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1344-1537 |
1.96e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.85 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD-------TFEGHIIIDGIDIAKLPLHT 1416
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevtiTGSIVYNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1417 LRSRLSIILQDPVLFSGTI--------RFNLDPERKCSDSTLWEALEIAQLKLVVKAlpggldaIITEGGENFSQGQRQL 1488
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438338 1489 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1537
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
695-860 |
2.24e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpDSEIGEDP-SPEretatDLDIRKRGPVAYAS 773
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGV-------EGVITYDGiTPE-----EIKKHYRGDVVYNA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 QK----PWLlnaTVEENIIF----ESPFNkqRYKMVIEACSLQPDIDI------LPHGDQTQIGE---RGInlSGGQRQR 836
Cdd:TIGR00956 145 ETdvhfPHL---TVGETLDFaarcKTPQN--RPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRGV--SGGERKR 217
|
170 180
....*....|....*....|....
gi 1189438338 837 ISVARALYQHANVVFLDDPFSALD 860
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
705-915 |
2.63e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.86 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 705 GQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSS-----------SLPDSEIGEDPSperetaTDLDIRKRgpvayAS 773
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrSQRIRMIFQDPS------TSLNPRQR-----IS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 774 QkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQRQRISVARALYQHANVVFL 852
Cdd:PRK15112 108 Q---ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 853 DDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 915
Cdd:PRK15112 174 DEALASLDMSMRSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1361-1570 |
2.66e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.90 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1361 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV----DTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGT 1434
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpssGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1435 IRFNLDPERKCSDSTLWEALEIAqLKLVVKAlpGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-M 1513
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKA-LKWLKKV--GLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1514 ATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKD 1570
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1348-1572 |
2.68e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.69 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1348 NLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIIL 1425
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLfmNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1426 QDP---VLFS---GTIRFNLD----PE----RKCSDS-TLWEALEIAQLKLvvkalpggldaiiteggENFSQGQRQLFC 1490
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRnlgvPEaeitRRVDEAlTLVDAQHFRHQPI-----------------QCLSHGQKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1491 LARAFVRKTSIFIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKL 1565
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEV 223
|
....*..
gi 1189438338 1566 LSRKDSV 1572
Cdd:PRK13638 224 FACTEAM 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
691-891 |
2.73e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.58 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssSLPDSEIGEDPsperetatdLDIRKRGPVA 770
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI----IIDDEDISLLP---------LHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLLNA-TVEENI-----IFESPFNKQRYKMVIEacsLQPDIDILPHGDQTqigerGINLSGGQRQRISVARALY 844
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLmavlqIRDDLSAEQREDRANE---LMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438338 845 QHANVVFLDDPFSALD-IHLSDhlmQAGILELLRDDKRTVVLVTHKLQ 891
Cdd:PRK10895 154 ANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
782-872 |
2.79e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 47.33 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 782 TVEENI--IFE-SPFNKQRYKMVIEacSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHANVVFLDDPFSA 858
Cdd:COG1137 94 TVEDNIlaVLElRKLSKKEREERLE--ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
90 100
....*....|....*....|.
gi 1189438338 859 LD-IHLSD------HLMQAGI 872
Cdd:COG1137 167 VDpIAVADiqkiirHLKERGI 187
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
827-890 |
2.79e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 2.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 827 INLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL 890
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA-IRRLSEEGKKTALVVEHDL 132
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1452-1577 |
3.21e-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: 47.87 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1452 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVV 1523
Cdd:TIGR01187 83 EALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkTIQEQLG 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1524 MtafadrTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKDSVF-ASFV 1577
Cdd:TIGR01187 152 I------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1344-1556 |
3.22e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVDTFEGHIIIDGIDIAKlPLHTLRSRL 1421
Cdd:PRK15439 12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLFSG-TIRFNL--------DPERKCSDstLWEALEiAQLKLVVKAlpGGLDAiiteggenfsqGQRQLFCLA 1492
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENIlfglpkrqASMQKMKQ--LLAALG-CQLDLDSSA--GSLEV-----------ADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 1493 RAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1556
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1062-1225 |
3.36e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 47.63 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1062 VYAMVFTVLC--SLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1139
Cdd:cd18780 41 LNQAVLILLGvvLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1140 ECLSRSTLLCVSALAVISYV----TPVFLVALLPLAIVCYFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1214
Cdd:cd18780 121 SMLLRYLVQIIGGLVFMFTTswklTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQD-----ALAAASTVAEeSISNIRTVR 195
|
170
....*....|.
gi 1189438338 1215 AFRYEARFQQK 1225
Cdd:cd18780 196 SFAKETKEVSR 206
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
830-890 |
4.90e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.41 E-value: 4.90e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 830 SGGQRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTHKL 890
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
697-913 |
5.56e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQK----VSGAVfwsssLPDSEIGEDPSPERetatdldiRKRGpva 770
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLinAISGLTRPQKgrivLNGRV-----LFDAEKGICLPPEK--------RRIG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLL-NATVEENIIFE-SPFNKQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQRQRISVARALYQHAN 848
Cdd:PRK11144 80 YVFQDARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 849 VVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVL-VTHKLQYLPH-ADWIIAMKDGTIQREGTL 913
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPL 213
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1075-1289 |
7.38e-05 |
|
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: 46.54 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1075 IVLCLVTSVTVEWTGLK------VAKRLH---RSLLNR-IILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSR 1144
Cdd:cd18784 40 IIMGLLAIASSVAAGIRgglftlAMARLNiriRNLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1145 STLLCVSALAVI---SYVTPVFLVALLPL-AIVCYFIQKYFRVASRDLQqlddtTQLPLLSHFA-ETVEGLTTIRAF--- 1216
Cdd:cd18784 120 SLVKAIGVIVFMfklSWQLSLVTLIGLPLiAIVSKVYGDYYKKLSKAVQ-----DSLAKANEVAeETISSIRTVRSFane 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1217 -----RYEARFQQ-------KLLEYTDSNNIASLFLTAanrwLEVRMEYIGACVVLIAAVTS---ISNSLHR-ELSAGLV 1280
Cdd:cd18784 195 dgeanRYSEKLKDtyklkikEALAYGGYVWSNELTELA----LTVSTLYYGGHLVITGQISGgnlISFILYQlELGSCLE 270
|
250
....*....|
gi 1189438338 1281 GLGLTYA-LM 1289
Cdd:cd18784 271 SVGSVYTgLM 280
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
390-607 |
7.39e-05 |
|
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: 46.65 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 390 IQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYI---LGVSALIGAAV 465
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTsALTVLVRDPLTVIGLLGVLFYLdwkLTLIALVVLPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 466 IILlaPVQYFvATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FRTRVETTRRKEMTSLRAFAIYTSI 541
Cdd:cd18552 152 AAL--PIRRI-GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438338 542 SIFMnTAIPIAAVLItFVGHVSFfkEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 607
Cdd:cd18552 229 MELL-GAIAIALVLW-YGGYQVI--SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
691-905 |
7.93e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSlpdseigedpsperetatdldirkrgPVA 770
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK--------------------------EID 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWLLNA--------------TVEENIIF-----ESPFNKQRyKMVIEACSL--QPDIDILPHgdqtqigERGINL 829
Cdd:PRK10982 64 FKSSKEALENGismvhqelnlvlqrSVMDNMWLgryptKGMFVDQD-KMYRDTKAIfdELDIDIDPR-------AKVATL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 830 SGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDG 905
Cdd:PRK10982 136 SVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1354-1578 |
9.06e-05 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 46.10 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1354 DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRS-RLSIILQDpv 1429
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQS-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1430 lfsgtirFNLDPERKCSDSTLWeALEIA-------------QLKLVvkALPGGLDAIITEggenFSQGQRQLFCLARAFV 1496
Cdd:cd03294 111 -------FALLPHRTVLENVAF-GLEVQgvpraereeraaeALELV--GLEGWEHKYPDE----LSGGMQQRVGLARALA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1497 RKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLL-SRKDSV 1572
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILtNPANDY 256
|
....*.
gi 1189438338 1573 FASFVR 1578
Cdd:cd03294 257 VREFFR 262
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
695-889 |
9.12e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQkvsgavfwSSSLPDSEIGEDPSPERETatdldIRKRGpvaYASQ 774
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ--------GNNFTGTILANNRKPTKQI-----LKRTG---FVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLL-NATVEENIIFES----PFNKQRYKMVIEACSLQPDIDiLPHGDQTQIGE---RGInlSGGQRQRISVARALYQH 846
Cdd:PLN03211 148 DDILYpHLTVRETLVFCSllrlPKSLTKQEKILVAESVISELG-LTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLIN 224
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1189438338 847 ANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHK 889
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLT--LGSLAQKGKTIVTSMHQ 265
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1344-1577 |
1.19e-04 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 45.31 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAK----LPLHtlRS 1419
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFETPTSGEILLDGKditnLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1420 RLSIILQDPVLF-----SGTIRFNLDpERKCSDSTLWEALEiAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARA 1494
Cdd:cd03300 73 PVNTVFQNYALFphltvFENIAFGLR-LKKLPKAEIKERVA-EALDLV------QLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1495 FVRKTSIFIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILSADLVIVLKRGAILEFDKPEKLLSRKD 1570
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
....*...
gi 1189438338 1571 SVF-ASFV 1577
Cdd:cd03300 224 NRFvADFI 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
828-890 |
1.25e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 1.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 828 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIhlSDHLMQAGILELLRDDKRTVVLVTHKL 890
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
824-920 |
1.28e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 824 ERGIN-LSGGQRQRISVARAL-YQHANVVF-LDDPfsALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWII 900
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEP--SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|....*.
gi 1189438338 901 AM------KDGTIQREGTLKDFQRSE 920
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILANP 586
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1344-1567 |
1.45e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.46 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRY----DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM---------VDTFEGHIIIDgidia 1410
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlipsegkvyVDGLDTSDEEN----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1411 klpLHTLRSRLSIILQDP------------VLFsGTIRFNLDPE--RKCSDstlwEALEIAQLKLVVKALPGGLdaiite 1476
Cdd:PRK13633 80 ---LWDIRNKAGMVFQNPdnqivativeedVAF-GPENLGIPPEeiRERVD----ESLKKVGMYEYRRHAPHLL------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1477 ggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILSADLVIV 1550
Cdd:PRK13633 146 -----SGGQKQRVAIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIV 216
|
250
....*....|....*..
gi 1189438338 1551 LKRGAILEFDKPEKLLS 1567
Cdd:PRK13633 217 MDSGKVVMEGTPKEIFK 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1343-1567 |
1.72e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.00 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1343 KIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1422
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1423 IILQDPVLFSG-TIRfNLDPERKCSDSTLWEALEIAQLKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1500
Cdd:PRK11231 80 LLPQHHLTPEGiTVR-ELVAYGRSPWLSLWGRLSAEDNARVNQAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1501 IFIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
691-888 |
1.80e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 45.59 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 691 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdSEIGEdPSPERETATdldiRKRgpVA 770
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI--------TVLGV-PVPARARLA----RAR--IG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 771 YASQKPWL-LNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVARALYQHANV 849
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQL 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 1189438338 850 VFLDDPFSALDIHlSDHLMQAGILELLRDDKrTVVLVTH 888
Cdd:PRK13536 194 LILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1344-1567 |
1.82e-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: 45.95 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPVLKHVNAL---IAPGQKIGICGRTGSGKSSFS--LA----------FFRM----VDTFEghiii 1404
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSkiIAgvleptsgevNVRVgdewVDMTK----- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1405 dgidiaklPLHTLRSR----LSIILQDPVLFsgtirfnldPERKCSDStLWEAL------EIAQLKLVVKALPGGLD--- 1471
Cdd:TIGR03269 355 --------PGPDGRGRakryIGILHQEYDLY---------PHRTVLDN-LTEAIglelpdELARMKAVITLKMVGFDeek 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1472 --AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-AD 1546
Cdd:TIGR03269 417 aeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCD 496
|
250 260
....*....|....*....|.
gi 1189438338 1547 LVIVLKRGAILEFDKPEKLLS 1567
Cdd:TIGR03269 497 RAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
697-915 |
2.14e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 697 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGEDPSPEREtatdLDIRKRGpVAYASQKP 776
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN--------GKDISPRSP----LDAVKKG-MAYITESR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 777 ----WLLNATVEENIIFESPFNKQRYKMVI----------EACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVARA 842
Cdd:PRK09700 348 rdngFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 843 LYQHANVVFLDDPFSALDIHlsdhlMQAGILELLR---DDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVG-----AKAEIYKVMRqlaDDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1334-1577 |
2.76e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.21 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1334 IPKNWPDQGK-----IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGID 1408
Cdd:PRK11607 5 IPRPQAKTRKaltplLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1409 IAKLPLHT--LRSRLSIILQDPVLF-----SGTIRFNLDPERKCSD---STLWEALEIAQLKLVVKALPGGLdaiitegg 1478
Cdd:PRK11607 79 DGVDLSHVppYQRPINMMFQSYALFphmtvEQNIAFGLKQDKLPKAeiaSRVNEMLGLVHMQEFAKRKPHQL-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1479 enfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKV----VMTAFADRTVVTIAHRvhtilsad 1546
Cdd:PRK11607 151 ---SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrMQLEvvDILERVgvtcVMVTHDQEEAMTMAGR-------- 219
|
250 260 270
....*....|....*....|....*....|..
gi 1189438338 1547 lVIVLKRGAILEFDKPEKLLSRKDSVF-ASFV 1577
Cdd:PRK11607 220 -IAIMNRGKFVQIGEPEEIYEHPTTRYsAEFI 250
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1086-1233 |
3.12e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 44.73 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1086 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVF-L 1164
Cdd:cd18542 64 EKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLtL 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 1165 VALLPLAIVCYFIQKYFRVASRDLQQLDDttQLPLLSHFA-ETVEGLTTIRAF---RYE-ARFQQKLLEYTDSN 1233
Cdd:cd18542 144 ISLAIIPFIALFSYVFFKKVRPAFEEIRE--QEGELNTVLqENLTGVRVVKAFareDYEiEKFDKENEEYRDLN 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
692-911 |
3.14e-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: 45.18 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 692 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssslpdsEIGEDPsperetatdLDIRKRGPVAY 771
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV-------RVGDEW---------VDMTKPGPDGR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 772 ASQKPWL----------LNATVEEN----IIFESPFNKQRYKMVI----------EACSLqpdIDILPHgdqtqigergi 827
Cdd:TIGR03269 361 GRAKRYIgilhqeydlyPHRTVLDNlteaIGLELPDELARMKAVItlkmvgfdeeKAEEI---LDKYPD----------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 828 NLSGGQRQRISVARALYQHANVVFLDDPFSALD----IHLSDHLMQAGIlELlrddKRTVVLVTHKLQY-LPHADWIIAM 902
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKARE-EM----EQTFIIVSHDMDFvLDVCDRAALM 501
|
....*....
gi 1189438338 903 KDGTIQREG 911
Cdd:TIGR03269 502 RDGKIVKIG 510
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
710-899 |
3.17e-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: 45.31 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 710 IVGQVGCGKSSLLlaalgemqKVSGAVfwssslpDSEI-GED-PSPeretatdlDIRkrgpVAYASQKPWL-LNATVEEN 786
Cdd:TIGR03719 36 VLGLNGAGKSTLL--------RIMAGV-------DKDFnGEArPQP--------GIK----VGYLPQEPQLdPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 787 II-------------------FESP---FNKQRYKM-----VIEAC---SLQPDIDI------LPHGDQtQIGergiNLS 830
Cdd:TIGR03719 89 VEegvaeikdaldrfneisakYAEPdadFDKLAAEQaelqeIIDAAdawDLDSQLEIamdalrCPPWDA-DVT----KLS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 831 GGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWI 899
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPGTVVAVTHDRYFLDNvAGWI 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1344-1556 |
3.21e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 44.65 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSL---KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFR---------MVDTFEGHIIidgidiaK 1411
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkptsgkiIIDGVDITDK-------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1412 LPLHTLRSRLSIILQDP--VLFSGT----IRF---NLDPERKCSDSTLWEALEIAQLKlvvkalpggLDAIITEGGENFS 1482
Cdd:PRK13637 76 VKLSDIRKKVGLVFQYPeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 1483 QGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1556
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1061-1180 |
3.59e-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: 44.39 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1061 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID----QHIP 1136
Cdd:cd18577 47 NKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQdgigEKLG 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1189438338 1137 STLECLSrstlLCVSALaVISYV---------TPVFLVALLPLAIVCYFIQKY 1180
Cdd:cd18577 127 LLIQSLS----TFIAGF-IIAFIyswkltlvlLATLPLIAIVGGIMGKLLSKY 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
695-862 |
3.66e-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: 44.93 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssslpdsEIGE--------------DPSPE--RETA 758
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI---------EIGEtvklayvdqsrdalDPNKTvwEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 759 TDLDIRKRGPV-----AYASQkpwllnatveeniifespFNkqrYKmvieacslqpdidilpHGDQTQ-IGErginLSGG 832
Cdd:TIGR03719 409 GGLDIIKLGKReipsrAYVGR------------------FN---FK----------------GSDQQKkVGQ----LSGG 447
|
170 180 190
....*....|....*....|....*....|
gi 1189438338 833 QRQRISVARALYQHANVVFLDDPFSALDIH 862
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
829-903 |
3.92e-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: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 829 LSGGQRQRISVARALyQHANV-----VFLDDPFSALDIHLSDHLMQAgILELLrDDKRTVVLVTHKLQYLPHADWIIAMK 903
Cdd:cd03227 78 LSGGEKELSALALIL-ALASLkprplYILDEIDRGLDPRDGQALAEA-ILEHL-VKGAQVIVITHLPELAELADKLIHIK 154
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1570 |
4.24e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1423
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1424 ILQDP--VLFS---------GTIRFNLDPErkcsdsTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1492
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEE------TVAHRVSSA-LHML------GLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1493 RAFVRKTSIFIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 1189438338 1568 RKD 1570
Cdd:PRK13652 228 QPD 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1370-1563 |
4.56e-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: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1370 PGQKIGICGRTGSGKSSFSLAFFRMVDtfeghiiidgidiaklplhtlrsrlsiilqdpVLFSGTIRFNLDPERKCSDST 1449
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG--------------------------------PPGGGVIYIDGEDILEEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1450 LWEAleiaqlklvvkalpggldaIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAF-- 1527
Cdd:smart00382 49 LLLI-------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1189438338 1528 -----ADRTVVTIAHRVHTILSADLVIVLKRgaILEFDKPE 1563
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRRRFDR--RIVLLLIL 148
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1368-1550 |
4.93e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.42 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1368 IAPGQKIGICGRTGSGKSSF-SL-AFFRMVDTfeghiiidgidiAKLPL----HTL----RSRLSIILQDPVLFSG-TIR 1436
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLlNLiAGFLTPAS------------GSLTLngqdHTTtppsRRPVSMLFQENNLFSHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1437 FN----LDPERKCSDSTLWEALEIAQ---LKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATA 1509
Cdd:PRK10771 90 QNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438338 1510 SIDMATENILQKVVMTAFADR--TVVTIAHRV---HTILSADLVIV 1550
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERqlTLLMVSHSLedaARIAPRSLVVA 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1344-1560 |
5.06e-04 |
|
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: 43.01 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKL-----PLHtlR 1418
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEPTSGRIYIGGRDvtdlpPKD--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1419 SrLSIILQDPVLFS-----GTIRFNLD----PERKCSDSTLWEAlEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLF 1489
Cdd:cd03301 73 D-IAMVFQNYALYPhmtvyDNIAFGLKlrkvPKDEIDERVREVA-ELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438338 1490 CLARAFVRKTSIFIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILSADLVIVLKRGAILEFD 1560
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1344-1557 |
5.28e-04 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 43.58 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSsLKpVLKHVNALIAPGQKIGICGRTGSGKSS-FSL-----------AFFRMVDTfeghiiidgidiAK 1411
Cdd:cd03219 1 LEVRGLTKRFGG-LV-ALDDVSFSVRPGEIHGLIGPNGAGKTTlFNLisgflrptsgsVLFDGEDI------------TG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1412 LPLHtLRSRLSII--LQDPVLFSG-TIRFNL-------------DPERKCSDSTLWE-ALEIaqLKLVvkalpgGLDAII 1474
Cdd:cd03219 67 LPPH-EIARLGIGrtFQIPRLFPElTVLENVmvaaqartgsgllLARARREEREARErAEEL--LERV------GLADLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1475 TEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLK 1552
Cdd:cd03219 138 DRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLD 217
|
....*
gi 1189438338 1553 RGAIL 1557
Cdd:cd03219 218 QGRVI 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
695-890 |
6.66e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.18 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 695 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSSLpdsEIGedpsperetatdldirkrgpvaYASQ 774
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---RIG----------------------YVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 775 KPWLlNATVeeniifesPFNKQRYKMvieacsLQPDI---DILPHGDQTQIGERgIN-----LSGGQRQRISVARALYQH 846
Cdd:PRK09544 75 KLYL-DTTL--------PLTVNRFLR------LRPGTkkeDILPALKRVQAGHL-IDapmqkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438338 847 ANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRT----VVLVTHKL 890
Cdd:PRK09544 139 PQLLVLDEPTQGVDVN-----GQVALYDLIDQLRREldcaVLMVSHDL 181
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
444-560 |
6.91e-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: 43.65 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 444 IIVGVILLYY--ILGVSALIGAAVIILLApvqYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAW 513
Cdd:cd18555 130 VIYLIYMLYYspLLTLIVLLLGLLIVLLL---LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKslgsekniYKKW 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1189438338 514 ENIFRTRVETTRRKEMTSlrafAIYTSISIFMNTAIPIaavLITFVG 560
Cdd:cd18555 207 ENLFKKQLKAFKKKERLS----NILNSISSSIQFIAPL---LILWIG 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1344-1385 |
9.69e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.76 E-value: 9.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438338 1344 IQIQNLSVRY------DSSLK--------------PVLKHVNALIAPGQKIGICGRTGSGKS 1385
Cdd:COG1134 5 IEVENVSKSYrlyhepSRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKS 66
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
689-907 |
1.01e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.48 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 689 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSsslpdseiGED---PSPERetatdldIRK 765
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD--------GEDitgLSPRE-------RRR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 766 RGpVAYASQKPW----LLNATVEENIIFES----PFNK----QRYKMVIEACSLQPDIDILPHGDQTQIGergiNLSGGQ 833
Cdd:COG3845 333 LG-VAYIPEDRLgrglVPDMSVAENLILGRyrrpPFSRggflDRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438338 834 RQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILElLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTI 907
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQR-LLE-LRDAGAAVLLISEDLDeILALSDRIAVMYEGRI 480
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1344-1570 |
1.18e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 42.91 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD--TFEGHIIIDGIDIAKLPLHTLRSRL 1421
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpsSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDP--VLFSGTIRFNLdperkcsdstlweALEIAQLKLVVKALPGGLDAIITEGG---------ENFSQGQRQLFC 1490
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDV-------------SFGAVNLKLPEDEVRKRVDNALKRTGiehlkdkptHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1491 LARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LSADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFA 231
|
...
gi 1189438338 1568 RKD 1570
Cdd:PRK13636 232 EKE 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
824-890 |
1.28e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 824 ERGI-NLSGGQRQRISVARALYQHANVVFLDDPFSALDIH--LSdhlMQAGILELLRDdkRTVVLVTHKL 890
Cdd:PRK13409 207 DRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrLN---VARLIRELAEG--KYVLVVEHDL 271
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1479-1556 |
1.28e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1479 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRG 1554
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDG 216
|
..
gi 1189438338 1555 AI 1556
Cdd:COG1129 217 RL 218
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1095-1226 |
1.34e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 42.47 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1095 RLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIdQHIPSTLECLSRSTLLCVSALAVISYVTP----VFLVALLPL 1170
Cdd:cd18543 73 DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPplalVALASLPPL 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 1171 AIVCYFIQKYFRVASRDLQQL--DDTTqlpllsHFAETVEGLTTIRAFRYEARFQQKL 1226
Cdd:cd18543 152 VLVARRFRRRYFPASRRAQDQagDLAT------VVEESVTGIRVVKAFGRERRELDRF 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1344-1387 |
1.38e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 42.45 E-value: 1.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1387
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTL 44
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1344-1577 |
1.61e-03 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 41.94 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAK-LPLHTLRSR-L 1421
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAGLERPDSGTILFGGEdATDVPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1422 SIILQDPVLF-----SGTIRFNLDPERKcsdSTLWEALEIAQ-----LKLVvkalpgGLDAIITEGGENFSQGQRQLFCL 1491
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRVKPR---SERPPEAEIRAkvhelLKLV------QLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1492 ARAFVRKTSIFIMDEATASIDMATENILQKVVmTAFADRTVVT---IAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1567
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 1189438338 1568 RKDSVF-ASFV 1577
Cdd:cd03296 227 HPASPFvYSFL 237
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1061-1232 |
1.68e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 42.19 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1061 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPSTLE 1140
Cdd:cd18782 42 YVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1141 CLSRSTLLCVSALAV-ISYVTPVFLVAL--LPLAIVCYF---------IQKYFRVASRdlqqlddtTQlpllSHFAETVE 1208
Cdd:cd18782 121 TTLLDVLFSVIYIAVlFSYSPLLTLVVLatVPLQLLLTFlfgpilrrqIRRRAEASAK--------TQ----SYLVESLT 188
|
170 180
....*....|....*....|....*
gi 1189438338 1209 GLTTIRAFRYEARFQQKLLE-YTDS 1232
Cdd:cd18782 189 GIQTVKAQNAELKARWRWQNrYARS 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1344-1578 |
1.68e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 42.37 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSsfSLAffRM-------------VDTFEghiiidgid 1408
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLI--RCinllerptsgsvlVDGVD--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1409 IAKLP---LHTLRSRLSIILQDpvlfsgtirFNLDPERkcsdsTLWE----ALEIAQ-------------LKLV-----V 1463
Cdd:COG1135 69 LTALSereLRAARRKIGMIFQH---------FNLLSSR-----TVAEnvalPLEIAGvpkaeirkrvaelLELVglsdkA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1464 KALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENIL---QKVvmtafADR---TVVTIA 1536
Cdd:COG1135 135 DAYPSQL-----------SGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIVLIT 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1189438338 1537 HRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKDSVFA-SFVR 1578
Cdd:COG1135 199 HEMDVVRRiCDRVAVLENGRIVEQGPVLDVFANPQSELTrRFLP 242
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1358-1572 |
1.82e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.94 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1358 KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKlplHTLRsRLSIILQDPVLFSG-T 1434
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYPHlT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1435 IRFNLdpeRKCSDSTLWEALEiAQLKLVVKalpgglDAIITEGG----EN----------FSQGQRQLFCLARAFVRKTS 1500
Cdd:PLN03211 157 VRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 1501 IFIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILsaDLVIVLKRGAILEFDKPEKLLSRKDSV 1572
Cdd:PLN03211 227 LLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
816-935 |
2.17e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 816 HGDQ-TQIGERginLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTHKLQYL- 893
Cdd:PRK10636 420 QGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVSHDRHLLr 491
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1189438338 894 PHADWIIAMKDGTIQR-EGTLKDFQRsecqlfehWKTLMNRQD 935
Cdd:PRK10636 492 STTDDLYLVHDGKVEPfDGDLEDYQQ--------WLSDVQKQE 526
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
707-888 |
2.23e-03 |
|
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: 41.10 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 707 LTMIVGQVGCGKSSLLLAalgemqkVSGAVFwssslpdseiGEDPSPERETATDLDIrkrgpvayasqkpwllnATVEE- 785
Cdd:cd03279 30 LFLICGPTGAGKSTILDA-------ITYALY----------GKTPRYGRQENLRSVF-----------------APGEDt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 786 -NIIFESPFNKQRYKmVIEACSLQPD----IDILPHGDQTQIGERGI-NLSGGQRQRISVARAL------YQHANVV--- 850
Cdd:cd03279 76 aEVSFTFQLGGKKYR-VERSRGLDYDqftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevlQNRGGARlea 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1189438338 851 -FLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTH 888
Cdd:cd03279 155 lFIDEGFGTLDPEALEAVATA--LELIRTENRMVGVISH 191
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
829-912 |
2.28e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 829 LSGGQRQRISVARALYQHAN---VVFLDDPFSAL---DIHlsdHLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAM 902
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIR---KLLE--VLHRLVDKGNTVVVIEHNLDVIKTADWIIDL 905
|
90
....*....|....*.
gi 1189438338 903 ------KDGTIQREGT 912
Cdd:PRK00349 906 gpeggdGGGEIVATGT 921
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1344-1558 |
2.35e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 41.66 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKlPL------- 1414
Cdd:PRK11264 4 IEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTIRVGDITIDTAR-SLsqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1415 HTLRSRLSIILQDpvlfsgtirFNLDPERKcsdstlweALE-IAQLKLVVKALPGG---------LDAIITEGGEN---- 1480
Cdd:PRK11264 81 RQLRQHVGFVFQN---------FNLFPHRT--------VLEnIIEGPVIVKGEPKEeatararelLAKVGLAGKETsypr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1481 -FSQGQRQLFCLARAFVRKTSIFIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1556
Cdd:PRK11264 144 rLSGGQQQRVAIARALAMRPEVILFDEPTSALDpeLVGE-VLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
..
gi 1189438338 1557 LE 1558
Cdd:PRK11264 223 VE 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
822-913 |
2.36e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 822 IGERGINLSGGQRQRISVARALY---QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADW 898
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLV--QLRTLVSLGHSVIYIDHDPALLKQADY 1770
|
90
....*....|....*
gi 1189438338 899 IIAMKDGTIQREGTL 913
Cdd:PRK00635 1771 LIEMGPGSGKTGGKI 1785
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1063-1225 |
2.59e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 41.67 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1063 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFF---ETTPlGSILNRFSSDCNTI----DQHI 1135
Cdd:cd18578 54 WALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddpENST-GALTSRLSTDASDVrglvGDRL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1136 PSTLECLsrSTLLCVSALAVISY--VTPVfLVALLPLAIVCYFIQKYF--RVASRDLQQLDDTTQLpllshFAETVEGLT 1211
Cdd:cd18578 133 GLILQAI--VTLVAGLIIAFVYGwkLALV-GLATVPLLLLAGYLRMRLlsGFEEKNKKAYEESSKI-----ASEAVSNIR 204
|
170
....*....|....
gi 1189438338 1212 TIRAFRYEARFQQK 1225
Cdd:cd18578 205 TVASLTLEDYFLEK 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
830-893 |
2.73e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438338 830 SGGQRQRISVARALYQHANVVFLDDPFSALDIH----LSDHLMQAgilellrddKRTVVLVTHKLQYL 893
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKW---------PKTFIVVSHAREFL 404
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1351-1551 |
2.74e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 41.24 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1351 VRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVL 1430
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1431 FSGTIRFNL-----------DPERKCSDstlwealeiaqlkLVVKALPgglDAIITEGGENFSQGQRQLFCLARAFVRKT 1499
Cdd:PRK10247 93 FGDTVYDNLifpwqirnqqpDPAIFLDD-------------LERFALP---DTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438338 1500 SIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVL 1551
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
827-908 |
2.74e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.27 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 827 INLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 906
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
..
gi 1189438338 907 IQ 908
Cdd:PRK10522 527 LS 528
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1089-1233 |
3.31e-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: 41.38 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1089 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCntidQHIPSTLE-CLS---RSTLL---CVSALAVISYVTP 1161
Cdd:cd18574 70 GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV----QEFKSSFKqCVSqglRSVTQtvgCVVSLYLISPKLT 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438338 1162 VFLVALLPLAIVC-YFIQKYFRVASRDLQQLDDTTqlplLSHFAETVEGLTTIRAFRYEAR----FQQKLLEYTDSN 1233
Cdd:cd18574 146 LLLLVIVPVVVLVgTLYGSFLRKLSRRAQAQVAKA----TGVADEALGNIRTVRAFAMEDRelelYEEEVEKAAKLN 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
1057-1225 |
3.57e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 41.41 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1057 TLDQTVYAMVFTVLCSlgIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIP 1136
Cdd:cd18566 40 TLQVLVIGVVIAILLE--SLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1137 stleclSRSTLLCVSALAVISYVTPVF----------LVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAET 1206
Cdd:cd18566 117 ------GQALLALLDLPFVLIFLGLIWylggklvlvpLVLLGLFVLVAILLGPILRRALKERSRADERRQ----NFLIET 186
|
170
....*....|....*....
gi 1189438338 1207 VEGLTTIRAFRYEARFQQK 1225
Cdd:cd18566 187 LTGIHTIKAMAMEPQMLRR 205
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
824-900 |
3.75e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 824 ERGIN-LSGGQRQRISVARALYQHANVV--FLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWII 900
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1366-1521 |
4.11e-03 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 40.36 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1366 ALIAPGQKIGICGRTGSGKSSF--SLAFFRMVD--TFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL- 1439
Cdd:cd03297 18 DFDLNEEVTGIFGASGAGKSTLlrCIAGLEKPDggTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHlNVRENLa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1440 -------DPERKCSDSTLWEALEIAQLKlvvKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID 1512
Cdd:cd03297 98 fglkrkrNREDRISVDELLDLLGLDHLL---NRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
....*....
gi 1189438338 1513 MATENILQK 1521
Cdd:cd03297 164 RALRLQLLP 172
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
377-560 |
4.85e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 40.84 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 377 YVAIETGINLRgaiqTKIYNKIMHLSTSNlsMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAM-PVQIIVGVILLYYIL 455
Cdd:cd18548 65 KASQGFGRDLR----KDLFEKIQSFSFAE--IDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRaPIMLIGAIIMAFRIN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 456 GVSALIGAAVIILLAPVQYFVATK---LSQAQRSTLEYSNERLKqtnEMLRGIKLLKLYAWENIFRTRVETTRRKEM-TS 531
Cdd:cd18548 139 PKLALILLVAIPILALVVFLIMKKaipLFKKVQKKLDRLNRVVR---ENLTGIRVIRAFNREDYEEERFDKANDDLTdTS 215
|
170 180
....*....|....*....|....*....
gi 1189438338 532 LRAFAIYTSISIFMNTAIPIAAVLITFVG 560
Cdd:cd18548 216 LKAGRLMALLNPLMMLIMNLAIVAILWFG 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1344-1385 |
6.60e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.82 E-value: 6.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1189438338 1344 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKS 1385
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKS 50
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1344-1513 |
6.77e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 40.44 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1344 IQIQNLSVRY-------DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSfsLAffRMVDTFEGHIIIDGIDIAKlPLHT 1416
Cdd:PRK10419 4 LNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKST--LA--RLLVGLESPSQGNVSWRGE-PLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1417 L--------RSRLSIILQDP---VLFSGTIRFNLD-PERKCSDstLWEALEIAQLKLVVKALpgGLDA-IITEGGENFSQ 1483
Cdd:PRK10419 79 LnraqrkafRRDIQMVFQDSisaVNPRKTVREIIRePLRHLLS--LDKAERLARASEMLRAV--DLDDsVLDKRPPQLSG 154
|
170 180 190
....*....|....*....|....*....|
gi 1189438338 1484 GQRQLFCLARAFVRKTSIFIMDEATASIDM 1513
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1069-1244 |
7.59e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 40.07 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1069 VLCSLGIVLC-LVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTL 1147
Cdd:cd18548 46 LLLALLGLIAgILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 1148 LCVSALAVISYVTP----VFLVALLPLAIVCYFIQKYFRVASRDLQ-QLDDTTQLpllshFAETVEGLTTIRAF---RYE 1219
Cdd:cd18548 126 MLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKAIPLFKKVQkKLDRLNRV-----VRENLTGIRVIRAFnreDYE 200
|
170 180
....*....|....*....|....*.
gi 1189438338 1220 -ARFQQKLLEYTDsNNIASLFLTAAN 1244
Cdd:cd18548 201 eERFDKANDDLTD-TSLKAGRLMALL 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
824-915 |
8.19e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 39.92 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 824 ERGIN-LSGGQRQRISVARALYQ-------HANVVFLDDPFSALDI-------HLSDHLMQAGIlellrddkrTVVLVTH 888
Cdd:PRK03695 121 GRSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVaqqaaldRLLSELCQQGI---------AVVMSSH 191
|
90 100
....*....|....*....|....*...
gi 1189438338 889 KLQY-LPHADWIIAMKDGTIQREGTLKD 915
Cdd:PRK03695 192 DLNHtLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
817-905 |
8.52e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438338 817 GDQTQIGergiNLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHA 896
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGIT 458
|
....*....
gi 1189438338 897 DWIIAMKDG 905
Cdd:PRK10982 459 DRILVMSNG 467
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1344-1390 |
9.35e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 39.05 E-value: 9.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1189438338 1344 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLA 1390
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKT 45
|
|
| |
