|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
224-1600 |
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: 838.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 224 LLSKGTYWWMNAFIKTAHKKPI---DLRAIGK----LPIAMRALTNYQRLC---------------------EAFDAQVR 275
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsEMVVPVLVENWKKECkktrkqpvsavygkkdpskpkGSSQLDAN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 276 KDIQGTQGAR-------AIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLgkeNDVFQPKTQFlgvYFVSS 348
Cdd:TIGR00957 289 EEVEALIVKSphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFV---NDPMAPDWQG---YFYTG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 349 QEFLANAyvlavllflallLQRTFLQASYYVAIETGINLRGAIQTKIYNKImhLSTSNLSMGEMTAGQICNLVAIDTNQL 428
Cdd:TIGR00957 363 LLFVCAC------------LQTLILHQYFHICFVSGMRIKTAVMGAVYRKA--LVITNSARKSSTVGEIVNLMSVDAQRF 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 429 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 508
Cdd:TIGR00957 429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 509 LKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVT 588
Cdd:TIGR00957 509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 589 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIreeqcaphEPtpqgpaskyQAVEeglpslhssqpsgssppnhpqplrvv 668
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLSHEEL--------EP---------DSIE-------------------------- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 669 nrKRParedcrgltgplqslVPSADGDAdnccVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAA 748
Cdd:TIGR00957 626 --RRT---------------IKPGEGNS----ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 749 LGEMQKVSGAVfwsslpdseigedpsperetatdldiRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACS 828
Cdd:TIGR00957 685 LAEMDKVEGHV--------------------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 829 LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQ--AGILELLRDdkRTVV 906
Cdd:TIGR00957 739 LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRI 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 907 LVTHKLQYLPHADWIIAMKDGTI----------QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE-LEKE---TVT 966
Cdd:TIGR00957 817 LVTHGISYLPQVDVIIVMSGGKIsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEaKLIEngmLVT 896
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 967 ERKATEPPQGLSRAMSSRDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIP-------WracaKYLSSAGILLLSLLVF 1039
Cdd:TIGR00957 897 DVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGqvelsvyW----DYMKAIGLFITFLSIF 972
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1040 SQLLKHMVLVAIDYWLAKWTDSALT-LTPAARNCSLSqectldqtVYAmvftvlcSLGI---VLCLVTSVTVEWTGLKVA 1115
Cdd:TIGR00957 973 LFVCNHVSALASNYWLSLWTDDPMVnGTQNNTSLRLS--------VYG-------ALGIlqgFAVFGYSMAVSIGGIQAS 1037
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1195
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLL 1117
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1196 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1275
Cdd:TIGR00957 1118 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLEC 1197
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1276 IGACVVLIAAVTSISNslHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSL 1355
Cdd:TIGR00957 1198 VGNCIVLFAALFAVIS--RHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE------APWQ 1269
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1356 I-----PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGID 1430
Cdd:TIGR00957 1270 IqetapPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1431 IAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQL 1510
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQL 1429
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
1450
....*....|
gi 1189438336 1591 KdSVFASFVR 1600
Cdd:TIGR00957 1510 R-GIFYSMAK 1518
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
222-1601 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 733.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 222 VNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDiqgtqgarAIW--QALSHAFGRRL 299
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKP--------KPWllRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 300 VLSSTFRILADLLGFAGPLcifgIVDHLGKENDVFQPKTQ--------FLGVYFvssqeflanayvlavllflalllqRT 371
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPL----LLNLLLESMQNGEPAWIgyiyafsiFVGVVL------------------------GV 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 372 FLQASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 450
Cdd:PLN03130 356 LCEAQYFQNVmRVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMV 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 451 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEM 530
Cdd:PLN03130 434 LLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDEL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 531 TSLRAFAIYTSISIFMNTAIPIAAVLITFvGHVSFFKeADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:PLN03130 514 SWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLG-GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 611 SEFLSsAEirEEQCAPHEPtpqgpaskyqaVEEGLPSlhssqpsgssppnhpqplrvvnrkrparedcrgltgplqslvp 690
Cdd:PLN03130 592 EELLL-AE--ERVLLPNPP-----------LEPGLPA------------------------------------------- 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 691 sadgdadnccVQIMGGYFTWTPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAvfwsslpdsei 769
Cdd:PLN03130 615 ----------ISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA----------- 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 770 gedpsperetatdlDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI 849
Cdd:PLN03130 674 --------------SVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGV 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 850 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:PLN03130 740 NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 930 QREGTLKD-------FQrsecQLFEHWKTLMNRQDQELEKE---TVTERKATEPPQGLSRAMSSRDGLLQDeeeeeeeaa 999
Cdd:PLN03130 818 KEEGTYEElsnngplFQ----KLMENAGKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSKKKSKEG--------- 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1000 eseeddnlSSMLHQRAE-----IPWRACAKYLSS-AGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLT--PAARN 1071
Cdd:PLN03130 885 --------KSVLIKQEEretgvVSWKVLERYKNAlGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKThgPLFYN 956
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1072 cslsqectldqTVYAMVftvlcSLGIVLclVTSVTVEW---TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSS 1148
Cdd:PLN03130 957 -----------LIYALL-----SFGQVL--VTLLNSYWlimSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAK 1018
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1149 DCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAET 1228
Cdd:PLN03130 1019 DLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEA 1098
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1229 VEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIA---AVTSISNSLHRELSAGLVGLG 1305
Cdd:PLN03130 1099 LNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTasfAVMQNGRAENQAAFASTMGLL 1178
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1306 LTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNLSVRYDSSLK 1380
Cdd:PLN03130 1179 LSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSE------APLVIennrpPPGWPSSGSIKFEDVVLRYRPELP 1252
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1381 PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFN 1460
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1461 LDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENI 1540
Cdd:PLN03130 1333 LDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1541 LQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1601
Cdd:PLN03130 1413 IQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-1601 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 712.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDiqgtqgARAIWQALSHAFGRRLVLS 302
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRP------KPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 303 STFRILADLLGFAGPLcifgIVDHLGKENDVFQPK--------TQFLGVYFvssqeflanayvlavllflalllqRTFLQ 374
Cdd:PLN03232 307 GIFKIGHDLSQFVGPV----ILSHLLQSMQEGDPAwvgyvyafLIFFGVTF------------------------GVLCE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 375 ASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 453
Cdd:PLN03232 359 SQYFQNVgRVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLY 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 454 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSL 533
Cdd:PLN03232 437 QQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWF 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 534 RAFAIYTSISIFMNTAIPIAAVLITFvgHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEF 613
Cdd:PLN03232 517 RKAQLLSAFNSFILNSIPVVVTLVSF--GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEEL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 614 LSSaeirEEQCAPHEPtpqgpaskyqaveeglpslhssqpsgssppnhpqplrvvnrkrparedcrgltgPLQSLVPSad 693
Cdd:PLN03232 595 LLS----EERILAQNP------------------------------------------------------PLQPGAPA-- 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 694 gdadnccVQIMGGYFTW-TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMqkvsgavfwsslpdseiged 772
Cdd:PLN03232 615 -------ISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL-------------------- 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 773 pSPERETATDLdirkRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLS 852
Cdd:PLN03232 668 -SHAETSSVVI----RGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNIS 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 853 GGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 932
Cdd:PLN03232 743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 933 GTLKDFQRSEcQLFEHWKTLMNRQDQELEKETVTERKATEPP--------QGLSRAMSSRDGllqdeeeeeeeaaeseed 1004
Cdd:PLN03232 821 GTFAELSKSG-SLFKKLMENAGKMDATQEVNTNDENILKLGPtvtidvseRNLGSTKQGKRG------------------ 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1005 dnlSSMLHQRAE-----IPWRACAKYLSS-AGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSAltlTPAARNCSLsqec 1078
Cdd:PLN03232 882 ---RSVLVKQEEretgiISWNVLMRYNKAvGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQS---TPKSYSPGF---- 951
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 tldqtvYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIP 1158
Cdd:PLN03232 952 ------YIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVA 1025
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1159 STLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF 1238
Cdd:PLN03232 1026 NLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY 1105
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 RYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSI---SNSLHRELSAGLVGLGLTYALMVSNY 1315
Cdd:PLN03232 1106 KAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNITTL 1185
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1316 LNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSLIPKN-----WPDQGKIQIQNLSVRYDSSLKPVLKHVNALI 1390
Cdd:PLN03232 1186 LSGVLRQASKAENSLNSVERVGNYIDLPSE------ATAIIENNrpvsgWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFV 1259
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1391 APGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDS 1470
Cdd:PLN03232 1260 SPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDA 1339
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1471 TLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFA 1550
Cdd:PLN03232 1340 DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK 1419
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1551 DRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1601
Cdd:PLN03232 1420 SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
369-1601 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 647.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 369 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDT---NQLMWFfflCPNLWAMPVQI 445
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVeriNSFMQY---CMYLWSSPMVL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 446 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETT 525
Cdd:PTZ00243 375 LLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 526 RRKEMTSLRAFAIYTSISIFMNTAIP---IAAVLITF--VGHvsffkeaDFSPSVAFASLSLFHILVTPLFLLSSVVRST 600
Cdd:PTZ00243 455 RARELRYLRDVQLARVATSFVNNATPtlmIAVVFTVYylLGH-------ELTPEVVFPTIALLGVLRMPFFMIPWVFTTV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 601 VKALVSVQKLSEFLSS-----------AEIREEQcAPHEPT--------------------PQGPASKYQAVEEGLPSLh 649
Cdd:PTZ00243 528 LQFLVSIKRISTFLECdnatcstvqdmEEYWREQ-REHSTAcqlaavlenvdvtafvpvklPRAPKVKTSLLSRALRML- 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 650 sSQPSGSSPPNHPQPLRVVNR------KRPAREDCRGLTGPLQSLVPSADGDADnccVQIMGG--YFTWTPDGIptLSNI 721
Cdd:PTZ00243 606 -CCEQCRPTKRHPSPSVVVEDtdygspSSASRHIVEGGTGGGHEATPTSERSAK---TPKMKTddFFELEPKVL--LRDV 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 722 TIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfWSslpdseigedpspEREtatdldirkrgpVAYASQKPWLL 801
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WA-------------ERS------------IAYVPQQAWIM 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 802 NATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSAL 881
Cdd:PTZ00243 734 NATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 882 DIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEcqLFEHWKT-LMNRQDQel 960
Cdd:PTZ00243 814 DAHVGERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATLAAeLKENKDS-- 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 961 eKETVTERKATEppqglsraMSSRDGLLQDEEEEEEEAAESEEDDNLSSM------LHQRAE-----IPWRACAKYLSSA 1029
Cdd:PTZ00243 888 -KEGDADAEVAE--------VDAAPGGAVDHEPPVAKQEGNAEGGDGAALdaaagrLMTREEkasgsVPWSTYVAYLRFC 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1030 G-----ILLLSLLVFSQLlkhmVLVAIDYWLAKWTdsaltltpaarncslSQECTLDQTVYAMVFtvlcsLGIVLCLVTS 1104
Cdd:PTZ00243 959 GglhaaGFVLATFAVTEL----VTVSSGVWLSMWS---------------TRSFKLSAATYLYVY-----LGIVLLGTFS 1014
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1105 V----TVEWTGLKV-AKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVIS 1179
Cdd:PTZ00243 1015 VplrfFLSYEAMRRgSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTS 1094
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1180 YVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIAS 1259
Cdd:PTZ00243 1095 ASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCS 1174
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1260 LFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELS--AGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKR-- 1335
Cdd:PTZ00243 1175 YLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERll 1254
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1336 --IHGL-------LKTE---AESYEGLLA---------PSLIPKNWP---DQGKIQIQNLSVRYDSSLKPVLKHVNALIA 1391
Cdd:PTZ00243 1255 yyTDEVphedmpeLDEEvdaLERRTGMAAdvtgtvviePASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIA 1334
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1392 PGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDST 1471
Cdd:PTZ00243 1335 PREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAE 1414
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1472 LWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFI-MDEATASIDMATENILQKVVMTAFA 1550
Cdd:PTZ00243 1415 VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQATVMSAFS 1494
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1551 DRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1601
Cdd:PTZ00243 1495 AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1364-1603 |
4.58e-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: 4.58e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1523
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1524 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1603
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 ... |
1036-1337 |
6.51e-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: 446.67 E-value: 6.51e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1036 LLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVA 1115
Cdd:cd18602 3 LVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1195
Cdd:cd18602 83 RRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1196 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1275
Cdd:cd18602 163 YYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDY 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1276 IGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18602 243 LGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVL 304
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
701-928 |
1.71e-139 |
|
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: 428.67 E-value: 1.71e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 701 VQIMGGYFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSlpdseigedPSPERETA 780
Cdd:cd03290 1 VQVTNGYFSWGS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---------KNESEPSF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 781 TDLDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRIS 860
Cdd:cd03290 71 EATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 861 VARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
301-610 |
3.68e-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: 425.88 E-value: 3.68e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENDVFQPKTQFLGVYFVSSQEFLANAYVLAVLLFLALLLQRTFLQASYYVA 380
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVSYVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 381 IETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYT 540
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 541 SISIFMNTAIPIAAVLITFVGHVsFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYP-YLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
223-1603 |
5.20e-126 |
|
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: 430.49 E-value: 5.20e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRAltnyQRLCEAFDAQVRKDIQGTQGARAIWQALSHAFGRRLVLs 302
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSA----DNLSERLEREWDRELASAKKNPKLLNALRRCFFWRFVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 303 stfriladllgfagplciFGIVDHLGKENDVFQPktQFLGVYFVSSQEFLAN----AYVLAVLLFLALLLQRTFLQASYY 378
Cdd:TIGR01271 85 ------------------YGILLYFGEATKAVQP--LLLGRIIASYDPFNAPereiAYYLALGLCLLFIVRTLLLHPAIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 379 VAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGV 458
Cdd:TIGR01271 145 GLHHLGMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 459 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAi 538
Cdd:TIGR01271 223 NGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 539 ytSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHIL-VTPLFLLSSVVRSTVKALVSVQKLSEFLSSA 617
Cdd:TIGR01271 302 --YLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 618 EireeqcapheptpqgpaskYQAVEEGLPSLHSSQPSGSSPPNhpQPLRVVNRKRPAREDCRGltgplqslvpSADGDAd 697
Cdd:TIGR01271 380 E-------------------YKTLEYNLTTTEVEMVNVTASWD--EGIGELFEKIKQNNKARK----------QPNGDD- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 698 nccvqimGGYFT-WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwsslpdseigedpspe 776
Cdd:TIGR01271 428 -------GLFFSnFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG------------------- 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 777 retatdlDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 856
Cdd:TIGR01271 482 -------KIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQR 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 936
Cdd:TIGR01271 555 ARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFS 632
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 937 DFQRSE---------CQLFEHWK--------------------------------------------------------- 950
Cdd:TIGR01271 633 ELQAKRpdfsslllgLEAFDNFSaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasa 712
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 951 -------------------------------------------------------------------TLMNRQDQELEKE 963
Cdd:TIGR01271 713 rkfsfvqmgpqkaqattiedavrepserkfslvpedeqgeeslprgnqyhhglqhqaqrrqsvlqlmTHSNRGENRREQL 792
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 964 TVTERKATEPPQG---------LSRAMSSRDGLLQDEEEEEEEAAESEEDDnlssMLHQRAEIPWRACAKYLSSAG---- 1030
Cdd:TIGR01271 793 QTSFRKKSSITQQnelaseldiYSRRLSKDSVYEISEEINEEDLKECFADE----RENVFETTTWNTYLRYITTNRnlvf 868
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1031 ILLLSLLVF-SQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLG---IVLCLVTSVT 1106
Cdd:TIGR01271 869 VLIFCLVIFlAEVAASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIITPTSAYYIFYIYVGTAdsvLALGFFRGLP 948
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1107 VEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFL 1186
Cdd:TIGR01271 949 LVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIF 1028
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1187 VALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF----RYEARFQQKLLEYTdsnniASLFL 1262
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFgrqsYFETLFHKALNLHT-----ANWFL 1103
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1263 TAAN-RWLEVRMEYIgaCVVLIAAVTSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLK 1341
Cdd:TIGR01271 1104 YLSTlRWFQMRIDII--FVFFFIAVTFIAIGTNQD-GEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFID 1180
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1342 TEAESYE-------GLLAPSLIPKN------WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSS 1408
Cdd:TIGR01271 1181 LPQEEPRpsggggkYQLSTVLVIENphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST 1260
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1409 FSLAFFRMVDTfEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKAL 1488
Cdd:TIGR01271 1261 LLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQF 1339
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1489 PGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSAD 1568
Cdd:TIGR01271 1340 PDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQ 1419
|
1530 1540 1550
....*....|....*....|....*....|....*
gi 1189438336 1569 LVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1603
Cdd:TIGR01271 1420 QFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADR 1454
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1364-1584 |
4.46e-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: 4.46e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1523
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1524 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKP 1584
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
701-928 |
2.77e-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: 325.58 E-value: 2.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 701 VQIMGGYFTWTPDGI---PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseigedpsper 777
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 778 etatdldirkrGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQ 857
Cdd:cd03250 66 -----------GSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 858 RISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1085-1601 |
2.82e-95 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 320.19 E-value: 2.82e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1085 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1164
Cdd:COG1132 63 LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1165 SRSTLLCVSALAVISYVTP----VFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1240
Cdd:COG1132 143 VRSVVTLIGALVVLFVIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAE----LNGRLQESLSGIRVVKAFGR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1241 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMV 1320
Cdd:COG1132 219 EERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1321 RNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIPknwpDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICG 1400
Cdd:COG1132 299 NVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPP----VRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1401 RTGSGKSSF-SLaFFRM------------VDTfeghiiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPE 1464
Cdd:COG1132 374 PSGSGKSTLvNL-LLRFydptsgrilidgVDI------------RDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1465 RkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKV 1544
Cdd:COG1132 441 A--TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1545 VMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLsRKDSVFASFVRA 1601
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 ... |
1030-1337 |
1.36e-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: 287.48 E-value: 1.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1030 GILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSAltltpaarncslsqecTLDQTVYAMVFTVLCSLG-IVLCLVTSVTVE 1108
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSP----------------NSSSGYYLGVYAALLVLAsVLLVLLRWLLFV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1109 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVA 1188
Cdd:cd18580 65 LAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1189 LLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRW 1268
Cdd:cd18580 145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1269 LEVRMEYIGACVVLIAAVTSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
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, ... |
1036-1337 |
1.01e-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: 276.67 E-value: 1.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1036 LLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNcslsqectlDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVA 1115
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTE---------QRDYRLGVYGALGLGQAIFVFLGSLALALGCVRAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1195
Cdd:cd18603 74 RNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1196 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1275
Cdd:cd18603 154 YFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEF 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1276 IGACVVLIAAVTSIsnsLHRE-LSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
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; ... |
1031-1340 |
8.64e-81 |
|
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: 268.18 E-value: 8.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1031 ILLLSLLVFSQLLkhmvLVAIDYWLAKWT---DSALTLTPAARNcslsqectldQTVYAMVFTVLCSLGIVLCLVTSVTV 1107
Cdd:cd18604 2 ALLLLLFVLSQLL----SVGQSWWLGIWAsayETSSALPPSEVS----------VLYYLGIYALISLLSVLLGTLRYLLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1108 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLV 1187
Cdd:cd18604 68 FFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1188 ALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANR 1267
Cdd:cd18604 148 PAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1268 WLEVRMEYIGACVVLIAAVTSISNslhRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLL 1340
Cdd:cd18604 228 WLSVRIDLLGALFSFATAALLVYG---PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1083-1591 |
8.01e-80 |
|
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: 279.41 E-value: 8.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLE 1162
Cdd:COG2274 196 WVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAVISY----VTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAF 1238
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFysppLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQ----SLLVETLRGIETIKAL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 RYEARFQQK-------LLEYTDSNNIASLFLTAANRWLEVrmeyIGACVVLIAAVTSIsnsLHRELSAGlvglGLTYALM 1311
Cdd:COG2274 351 GAESRFRRRwenllakYLNARFKLRRLSNLLSTLSGLLQQ----LATVALLWLGAYLV---IDGQLTLG----QLIAFNI 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1312 VSNYLNWMVRNLADM--ELQ--LGAVKRIHGLLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSLKPVLKHVN 1387
Cdd:COG2274 420 LSGRFLAPVAQLIGLlqRFQdaKIALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGDSPPVLDNIS 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1388 ALIAPGQKIGICGRTGSGKSSFS---LAFFR------MVDTFEGhiiidgidiAKLPLHTLRSRLSIILQDPVLFSGTIR 1458
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLkllLGLYEptsgriLIDGIDL---------RQIDPASLRRQIGVVLQDVFLFSGTIR 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1459 FNL---DPERkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDM 1535
Cdd:COG2274 567 ENItlgDPDA--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1536 ATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
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 ... |
1360-1584 |
2.74e-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: 2.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1360 WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTL 1439
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1440 RSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEiaqlklvvkalpggldaiITEGGENFSQGQRQLFCLARAFVR 1519
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1520 KTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKP 1584
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
1031-1337 |
6.25e-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: 251.68 E-value: 6.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1031 ILLLSLLVFSQllkhmvlVAIDYWLAKWTDSAltltpaarNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWT 1110
Cdd:cd18605 5 LLSLILMQASR-------NLIDFWLSYWVSHS--------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALL 1190
Cdd:cd18605 70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1191 PLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLE 1270
Cdd:cd18605 150 PLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1271 VRMEYIGACVVLIAAVTSI-SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18605 230 IRLQLLGVLIVTFVALTAVvQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVR 297
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
301-610 |
8.07e-73 |
|
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: 245.09 E-value: 8.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENDvfQPKTQ-------FLGVYFVSSqeflanayvlavllflalllqrTFL 373
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD--EPLSEgyllalaLFLVSLLQS----------------------LLL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 374 QASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 453
Cdd:cd18579 57 HQYFFLSFRLGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 454 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSL 533
Cdd:cd18579 135 RLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKAL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 534 RAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEadFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
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 ... |
1031-1337 |
1.63e-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: 235.45 E-value: 1.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1031 ILLLSLLVFSQLLKhmvlVAIDYWLAKWTDSALTLTpaarncslsqectldQTVYAMVFTVLCSLGIVLCLVTSVTVEWT 1110
Cdd:cd18606 2 PLLLLLLILSQFAQ----VFTNLWLSFWTEDFFGLS---------------QGFYIGIYAGLGVLQAIFLFLFGLLLAYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALL 1190
Cdd:cd18606 63 GIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1191 PLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASlFLTAAN-RWL 1269
Cdd:cd18606 143 PLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAY-FLTIANqRWL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1270 EVRMEYIGACVVLIAAVTSISNSLHreLSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
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, ... |
1030-1337 |
2.87e-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: 235.92 E-value: 2.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1030 GILLLSLLVFSQLLKHMVLVAIDYWLAKW------TDSALTLTPAARNCSLSQECTLD--QTVYAMVFTVLcslgIVLCL 1101
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgNTTNNVDNSTVDSGNISDNPDLNfyQLVYGGSILVI----LLLSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1102 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV 1181
Cdd:cd18599 77 IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1182 TPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLF 1261
Cdd:cd18599 157 FPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1262 LTAANRWLEVRMEYIGACVVLIAAVTSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18599 237 FNCAMRWLAVRLDILAVLITLITALLVV--LLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERIL 310
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1364-1592 |
2.13e-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: 2.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLW-EALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1523 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1111-1591 |
5.95e-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: 220.01 E-value: 5.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP----VFL 1186
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWlsglILL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1187 VA--LLPLAIVcyFIQKYFRVASRdlQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASL---- 1260
Cdd:COG4988 166 VTapLIPLFMI--LVGKGAAKASR--RQWRALARLS--GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMkvlr 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1261 --FLTAAnrwleVrME---YIGACVVLIAAVTSisnslhreLSAGLVGL--GLTYALMVSNYLNWMvRNL-----ADMEL 1328
Cdd:COG4988 240 vaFLSSA-----V-LEffaSLSIALVAVYIGFR--------LLGGSLTLfaALFVLLLAPEFFLPL-RDLgsfyhARANG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1329 qLGAVKRIHGLLKTEAESyeglLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSS 1408
Cdd:COG4988 305 -IAAAEKIFALLDAPEPA----APAGTAPLPAAGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKST 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1409 FSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPERkcSDSTLWEALEIAQLKLVV 1485
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPDA--SDEELEAALEAAGLDEFV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1486 KALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTIL 1565
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
490 500
....*....|....*....|....*.
gi 1189438336 1566 SADLVIVLKRGAILEFDKPEKLLSRK 1591
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, ... |
301-610 |
1.54e-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: 209.63 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 301 LSSTFRILADLLGFAGPLcIFGIVDHLGKENDVFQPKTQFLGVYFvssqeFLANayvlavllflalLLQRTFLQASYYVA 380
Cdd:cd18595 1 LAALLKLLSDILLFASPQ-LLKLLINFVEDPDEPLWKGYLYAVLL-----FLVS------------IIQSLLLHQYFHRC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 381 IETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:cd18595 63 FRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYT 540
Cdd:cd18595 141 LAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLN 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 541 SISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18595 221 AVSSFLWTCAPFLVSLATFATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
1030-1336 |
5.86e-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: 209.10 E-value: 5.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1030 GILLLSLLVFSQLLKHMVLVAIDYWLAKWTDS-----ALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTS 1104
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLeeklnDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1105 VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPV 1184
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1185 FLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIA-SLFLT 1263
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAwFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1264 aANRWLEVRMEYIgaCVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1336
Cdd:cd18601 241 -TSRWLAVRLDAL--CALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
297-934 |
1.66e-58 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 213.10 E-value: 1.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 297 RRLVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDvFQPKTQFLGVYFVSsqeFLANAyvlavllflalllqrTFLQAS 376
Cdd:COG1132 21 GLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD-LSALLLLLLLLLGL---ALLRA---------------LLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 377 YYVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFF-FLCPNLWAMPVQIIVGVILLYYI 455
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 456 LGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FRTRVETTRRKEMT 531
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 532 SLRAFAIYTSISIFMNTaipIAAVLITFVGhVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLS 611
Cdd:COG1132 240 AARLSALFFPLMELLGN---LGLALVLLVG-GLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 612 EFLssaEIREEQCAPHEPTPQGPASkyQAVEeglpslhssqpsgssppnhpqpLRVVNrkrparedcrgltgplqslvps 691
Cdd:COG1132 316 ELL---DEPPEIPDPPGAVPLPPVR--GEIE----------------------FENVS---------------------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 692 adgdadnccvqimggyFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLaaLGEMQKVSGAVFWSSLPDSEI 769
Cdd:COG1132 347 ----------------FSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnLL--LRFYDPTSGRILIDGVDIRDL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 770 GEDpsperetatdlDIRKRgpVAYASQKPWLLNATVEENIifespfnkqRY-------KMVIEAC---SLQPDIDILPHG 839
Cdd:COG1132 408 TLE-----------SLRRQ--IGVVPQDTFLFSGTIRENI---------RYgrpdatdEEVEEAAkaaQAHEFIEALPDG 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 840 DQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHAD 919
Cdd:COG1132 466 YDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNAD 542
|
650
....*....|....*
gi 1189438336 920 WIIAMKDGTIQREGT 934
Cdd:COG1132 543 RILVLDDGRIVEQGT 557
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
371-934 |
1.01e-53 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 201.99 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 371 TFLQASYYVAIETGINLRgaIQTKIYNKIMHLSTSNL---SMGEMTA-----GQICNLVaidTNQLMWFFFLCPnlwamp 442
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDLASrfrdvESIREFL---TGSLLTALLDLL------ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 443 vQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRV 522
Cdd:COG2274 282 -FVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRW 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 523 ETTRRKEM-TSLRAFAIYTSISIFMNTAIPIAAVLITFVGhVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTV 601
Cdd:COG2274 361 ENLLAKYLnARFKLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 602 KALVSVQKLSEFLSSA-EIREEQCAPHEPTPQGpaskyqAVEeglpslhssqpsgssppnhpqplrvvnrkrparedCRG 680
Cdd:COG2274 440 DAKIALERLDDILDLPpEREEGRSKLSLPRLKG------DIE-----------------------------------LEN 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 681 LTgplqslvpsadgdadnccvqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVF 760
Cdd:COG2274 479 VS-------------------------FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 761 WSSLPDSEIgeDPSperetatdlDIRKRgpVAYASQKPWLLNATVEENIIFESP-FNKQRykmVIEAC---SLQPDIDIL 836
Cdd:COG2274 534 IDGIDLRQI--DPA---------SLRRQ--IGVVLQDVFLFSGTIRENITLGDPdATDEE---IIEAArlaGLHDFIEAL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 837 PHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLP 916
Cdd:COG2274 598 PMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKG--RTVIIIAHRLSTIR 674
|
570
....*....|....*...
gi 1189438336 917 HADWIIAMKDGTIQREGT 934
Cdd:COG2274 675 LADRIIVLDKGRIVEDGT 692
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1102-1597 |
1.09e-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: 198.79 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1102 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISY- 1180
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYy 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1181 ---VTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTtqlplLSHFA-ETVEGLTTIRAFRYEARFQQKLLEYTDSNN 1256
Cdd:TIGR02203 153 swqLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQ-----VTTVAeETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1257 IASLFLTAANRWLEVRMEYIG----ACVVLIAAVTSISNSLhrelSAG-LVGLGLTYALMVSNylnwmVRNLAD----ME 1327
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIAslalAVVLFIALFQAQAGSL----TAGdFTAFITAMIALIRP-----LKSLTNvnapMQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1328 LQLGAVKRIHGLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKS 1407
Cdd:TIGR02203 299 RGLAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1408 SFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPeRKCSDSTLWEALEIAQLKLV 1484
Cdd:TIGR02203 373 TLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDF 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1485 VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI 1564
Cdd:TIGR02203 452 VDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTI 531
|
490 500 510
....*....|....*....|....*....|...
gi 1189438336 1565 LSADLVIVLKRGAILEFDKPEKLLSRkDSVFAS 1597
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 ... |
372-610 |
5.91e-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: 184.96 E-value: 5.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMT 531
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 532 SLRAFAIYTSISIFMNTAIPIAAVLITFVghVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
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; ... |
311-608 |
2.35e-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: 183.85 E-value: 2.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 311 LLGFAGPLCIFGIVDHLgkENDVFQPKTQ---FLGVYFVSSqefLANAyvlavllflalllqrTFLQASYYVAIETGINL 387
Cdd:cd18596 11 VLSFAPPFFLNRLLRYL--EDPGEDATVRpwvWVLLLFLGP---LLSS---------------LLDQQYLWIGRRLSVRL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 388 RGAIQTKIYNKIMHL-----------------STSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 450
Cdd:cd18596 71 RAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 451 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEM 530
Cdd:cd18596 151 FLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEEL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 531 TSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEaDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18596 231 KWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQ-ELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLD 307
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1366-1576 |
6.97e-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: 6.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNLdperkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFI 1525
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1526 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRG 1576
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1086-1591 |
4.12e-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: 4.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1086 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1165
Cdd:PRK10790 68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1166 RSTLLCVSAL-AVISYVTPVFLVALL--PLAIVCYFIQKYF------RVASRdLQQLDDTtqlpllshFAETVEGLTTIR 1236
Cdd:PRK10790 148 RSAALIGAMLvAMFSLDWRMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEVINGMSVIQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1237 AFRYEARFQQKLLEYTDSNNIAslfltaanrwlevRMEYIGACVVLIAAVTSISNS--------LHRELSAGLVGLGLTY 1308
Cdd:PRK10790 219 QFRQQARFGERMGEASRSHYMA-------------RMQTLRLDGFLLRPLLSLFSAlilcgllmLFGFSASGTIEVGVLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1309 ALMvsNYLNWMVRNLADME-----LQLGAV--KRIHGLLKTEAESYegllAPSLIPKNwpdQGKIQIQNLSVRYDSSlKP 1381
Cdd:PRK10790 286 AFI--SYLGRLNEPLIELTtqqsmLQQAVVagERVFELMDGPRQQY----GNDDRPLQ---SGRIDIDNVSFAYRDD-NL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1382 VLKHVNALIAPGQKIGICGRTGSGKSSfsLAFFRM----VDTFEGHIIIDGIdiAKLPLHTLRSRLSIILQDPVLFSGTI 1457
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyypLTEGEIRLDGRPL--SSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1458 RFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1537
Cdd:PRK10790 432 LANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1538 ENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
Cdd:PRK10790 512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
712-942 |
5.77e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 178.41 E-value: 5.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpV 791
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA-----------SWRRQ--I 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:COG4988 414 AWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 871 VVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:COG4988 494 LLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1366-1597 |
1.39e-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: 167.79 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03253 1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNLDPER-KCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 1524
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1525 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKdSVFAS 1597
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG-GLYAE 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1364-1603 |
4.52e-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: 4.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTfEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1523
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1524 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1603
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, ... |
372-610 |
1.11e-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: 166.97 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLStsnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMT 531
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 532 SLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFfkEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
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 ... |
305-610 |
1.32e-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: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 305 FRILADLLGFAGPLCIFGIVDHLgkENDVFQPKTQFL--GVYFVSSqeFLAnayvlavllflalllqrTFLQASY-YVAI 381
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFL--EDSSEPLSDGYLyaLGLVLSS--LLG-----------------ALLSSHYnFQMN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 382 ETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFfflCPNL---WAMPVQIIVGVILLYYILGV 458
Cdd:cd18598 64 KVSLKVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 459 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAI 538
Cdd:cd18598 139 AFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKY 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 539 YTSISIFMNTAIPIAAVLITFVGHVsfFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18598 219 LDALCVYFWATTPVLISILTFATYV--LMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
714-939 |
9.72e-44 |
|
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: 161.18 E-value: 9.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAvfwsslpdseigedpsperetatdldIRKRGPVAY 793
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK--------------------------IKHSGRISF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVF 873
Cdd:cd03291 103 SSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 874 LDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 939
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1034-1316 |
1.08e-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: 160.50 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1034 LSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAArncslsqecTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLK 1113
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE---------TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1114 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLA 1193
Cdd:pfam00664 72 LSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1194 IVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRM 1273
Cdd:pfam00664 152 PLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGIT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1189438336 1274 EYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYL 1316
Cdd:pfam00664 232 QFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1114-1592 |
4.24e-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: 4.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1114 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP-VFLVALLPL 1192
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrLTMVTLINL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1193 AIVcYFIQK----YFRVASRDLQQ-LDDTTQLPLlshfaETVEGLTTIRAF---RYEA-RFQQKLLEYTDSN---NIASL 1260
Cdd:TIGR00958 312 PLV-FLAEKvfgkRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFaaeEGEAsRFKEALEETLQLNkrkALAYA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1261 FLTAANRWLE----VRMEYIGACVVLIAAVTSisnslhrelsAGLVGLgLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1336
Cdd:TIGR00958 386 GYLWTTSVLGmliqVLVLYYGGQLVLTGKVSS----------GNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKV 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1337 HGLL-KTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFF 1414
Cdd:TIGR00958 455 FEYLdRKPNIPLTGTLAPL------NLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1415 RMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPE-RKCSDSTLWEALEIAQLKLVVKALPGGLD 1493
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1494 AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILSADLVIVL 1573
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVL 686
|
490
....*....|....*....
gi 1189438336 1574 KRGAILEFDKPEKLLSRKD 1592
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1366-1601 |
7.91e-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: 7.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDPVLFSGTIRFNL---DPERkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1522 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKdSVFASFVRA 1601
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1366-1591 |
2.72e-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: 2.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPG--ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1523 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
708-927 |
3.20e-41 |
|
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: 149.84 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRK 787
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE-----------SLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RgpVAYASQKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQ 867
Cdd:cd03228 77 N--IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 868 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 927
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEA-LRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
445-934 |
6.64e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 160.32 E-value: 6.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 445 IIVGVILLYYILGVSALI---GAAVIILLAPVqyFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTR 521
Cdd:COG4987 143 ILAAVAFLAFFSPALALVlalGLLLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALAR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 522 VETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPS----VAFASLSLFHILVTplflLSSVV 597
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPllalLVLAALALFEALAP----LPAAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 598 RSTVKALVSVQKLSEFLSSAEIREEQCAPhEPTPQGPAskyqaveeglpslhssqpsgssppnhpqpLRVvnrkrpared 677
Cdd:COG4987 297 QHLGRVRAAARRLNELLDAPPAVTEPAEP-APAPGGPS-----------------------------LEL---------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 678 cRGLTgplqslvpsadgdadnccvqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSG 757
Cdd:COG4987 337 -EDVS-------------------------FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 758 AVFWSSLPDSEIGEDpsperetatdlDIRKRgpVAYASQKPWLLNATVEENIIFESPfNKQRYKM--VIEACSLQPDIDI 835
Cdd:COG4987 391 SITLGGVDLRDLDED-----------DLRRR--IAVVPQRPHLFDTTLRENLRLARP-DATDEELwaALERVGLGDWLAA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 836 LPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYL 915
Cdd:COG4987 457 LPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGL 533
|
490
....*....|....*....
gi 1189438336 916 PHADWIIAMKDGTIQREGT 934
Cdd:COG4987 534 ERMDRILVLEDGRIVEQGT 552
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
708-933 |
7.73e-41 |
|
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: 150.43 E-value: 7.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgeDPSperetatdlDIRK 787
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL--DPA---------DLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RgpVAYASQKPWLLNATVEENIIFESPF-NKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 866
Cdd:cd03245 79 N--IGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 933
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1095-1600 |
3.64e-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: 3.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1095 LGIVLCLVTSVTVEWTGLKVAKRLHRSL--------LNRIILAPMRFFETTPLGSILNRFSSDcNTIDQHIPSTLECLSR 1166
Cdd:TIGR03796 198 LGMGLTALLQGVLTWLQLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTAL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1167 STLLCV-SALAVISYVTPVFLVALLPLAI---VCYFIQKYFRVASRDLQQldDTTQLpllshFAETVEGLTTIR------ 1236
Cdd:TIGR03796 277 DAVMLVfYALLMLLYDPVLTLIGIAFAAInvlALQLVSRRRVDANRRLQQ--DAGKL-----TGVAISGLQSIEtlkasg 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1237 ----AFRYEARFQQKLLEytdsnniaslfltaANRWLEVRMEYIGacvVLIAAVTSISNSLHRELSAGLV-------GLG 1305
Cdd:TIGR03796 350 lesdFFSRWAGYQAKLLN--------------AQQELGVLTQILG---VLPTLLTSLNSALILVVGGLRVmegqltiGML 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1306 LTY-ALMVS-----NYLNWMVRNLADMElqlGAVKRIHGLLKTEAESYEGLLAP--SLIPKNWPDQGKIQIQNLSVRYDS 1377
Cdd:TIGR03796 413 VAFqSLMSSflepvNNLVGFGGTLQELE---GDLNRLDDVLRNPVDPLLEEPEGsaATSEPPRRLSGYVELRNITFGYSP 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1378 SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTI 1457
Cdd:TIGR03796 490 LEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTV 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1458 RFNL---DPerKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID 1534
Cdd:TIGR03796 570 RDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1535 MATEnilqKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRkDSVFASFVR 1600
Cdd:TIGR03796 648 PETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAV-GGAYARLIR 710
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1364-1578 |
5.17e-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: 5.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFR-------MVDTFEGhiiidgidiAKL 1434
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLklLAGLYkptsgsvLLDGTDI---------RQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1435 PLHTLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLF 1511
Cdd:cd03245 72 DPADLRRNIGYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1512 CLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1578
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
708-934 |
4.11e-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: 146.22 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAAlgemqkvsgavFWsslpdseigeDPSPERETATDLDI 785
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPR-----------FY----------DVDSGRILIDGHDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 786 RK------RGPVAYASQKPWLLNATVEENIIFESPfNKQRyKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQR 856
Cdd:cd03251 67 RDytlaslRRQIGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 857 QRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
318-610 |
1.10e-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: 143.93 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 318 LCIFGIVDHLGKendVFQPktQFLG---VYFV-SSQEFLANAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQT 393
Cdd:cd18594 2 LGILLFLEESLK---IVQP--LLLGrlvAYFVpDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 394 KIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPV 473
Cdd:cd18594 77 LIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 474 QYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIA 553
Cdd:cd18594 155 QAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 554 AVLITFVGHVsFFKEAdFSPSVAFASLSLFHILVTPL-FLLSSVVRSTVKALVSVQKL 610
Cdd:cd18594 235 VSFATFVPYV-LTGNT-LTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1168-1573 |
1.39e-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: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1168 TLLCVSALAVISYVTPVFLVALLPLAIVcYFIQKYFRVASRDLQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQK 1247
Cdd:TIGR02857 132 PLAILAAVFPQDWISGLILLLTAPLIPI-FMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1248 LLEYTDSNNIASL------FLTAAnrwlevRMEYIGACVVLIAAVTsISNSL---HRELSAGLVGLGLTYALmvsnYLNw 1318
Cdd:TIGR02857 209 IRRSSEEYRERTMrvlriaFLSSA------VLELFATLSVALVAVY-IGFRLlagDLDLATGLFVLLLAPEF----YLP- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1319 mVRNL-----ADMELQlGAVKRIHGLLkteaeSYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPG 1393
Cdd:TIGR02857 277 -LRQLgaqyhARADGV-AAAEALFAVL-----DAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1394 QKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERK-CSDSTL 1472
Cdd:TIGR02857 349 ERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPdASDAEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1473 WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR 1552
Cdd:TIGR02857 429 REALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR 508
|
410 420
....*....|....*....|.
gi 1189438336 1553 TVVTIAHRVHTILSADLVIVL 1573
Cdd:TIGR02857 509 TVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1366-1590 |
2.26e-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: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNLDPERKCSD-STLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 1524
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1525 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
376-617 |
3.19e-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: 142.36 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 376 SYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQL-MWFFFLcPNLWAMPVQIIVGVILLYY 454
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 455 ILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLR 534
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 535 AFAIYTSisifMNTAIP-IAAVLITFVGHVSFF-KEADFSPSVAFASLSLFHilvtplfllssVVRSTVKALV--SVQKL 610
Cdd:cd18593 217 RTSFLRA----LNMGLFfVSSKLILFLTFLAYIlLGNILTAERVFVTMALYN-----------AVRLTMTLFFpfAIQFG 281
|
....*..
gi 1189438336 611 SEFLSSA 617
Cdd:cd18593 282 SELSVSI 288
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1102-1591 |
4.34e-37 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 149.01 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1102 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV 1181
Cdd:PRK11176 84 ISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1182 T---PVFLVALLPL-AIVCYFIQKYFRVASRDLQ----QLDDTTQLPLLSHFAETVEGLTTIRAFRYEA---RFQQKLLE 1250
Cdd:PRK11176 164 SwqlSLILIVIAPIvSIAIRVVSKRFRNISKNMQntmgQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKvsnRMRQQGMK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1251 YTDSNN--------IASLFLtaanrwlevrmeyigACVVLIAAVTSISNslhrELSAGlvglglTYALMVSNYLNWM--V 1320
Cdd:PRK11176 244 MVSASSisdpiiqlIASLAL---------------AFVLYAASFPSVMD----TLTAG------TITVVFSSMIALMrpL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1321 RNLADMELQ----LGAVKRIHGLLKTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKI 1396
Cdd:PRK11176 299 KSLTNVNAQfqrgMAACQTLFAILDLEQEKDEGKRVIE------RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1397 GICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPERKCSDSTLWE 1474
Cdd:PRK11176 373 ALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEE 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1475 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 1554
Cdd:PRK11176 453 AARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS 532
|
490 500 510
....*....|....*....|....*....|....*..
gi 1189438336 1555 VTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
Cdd:PRK11176 533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1121-1591 |
7.39e-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: 7.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1121 SLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLeclsRSTLLCVSALAVISYV-----TPVFLVALLPL--- 1192
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTI----LSLFLDMWILVIVGLFlvrqnMLLFLLSLLSIpvy 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1193 AIVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYEA-RFQQ----------KLLEYTDSNNIASLF 1261
Cdd:TIGR01193 309 AVIIILFKRTFNKLNHDAMQ----ANAVLNSSIIEDLNGIETIKSLTSEAeRYSKidsefgdylnKSFKYQKADQGQQAI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1262 LTAANRWLEVRMEYIGACVVLIAAVTsisnslhrelsaglVGLGLTYALMVSNYLNwMVRNLADMELQLGAVK----RIH 1337
Cdd:TIGR01193 385 KAVTKLILNVVILWTGAYLVMRGKLT--------------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvannRLN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1338 GLLKTEAESYEGLLAPSLIPKNwpdqGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV 1417
Cdd:TIGR01193 450 EVYLVDSEFINKKKRTELNNLN----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1418 DTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPERKCSDSTLWEALEIAQLKLVVKALPGGLDAI 1495
Cdd:TIGR01193 525 QARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1496 ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL 1573
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSDKIIVL 681
|
490
....*....|....*...
gi 1189438336 1574 KRGAILEFDKPEKLLSRK 1591
Cdd:TIGR01193 682 DHGKIIEQGSHDELLDRN 699
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
714-934 |
3.08e-36 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 137.74 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEdpsperetatdldIRKRGPVAY 793
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR-------------KSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLLNATVEENIIFESPFNKQryKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 871 VVFLDDPFSALDIHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03254 160 ILILDEATSNIDTE-TEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1314-1580 |
6.26e-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: 146.12 E-value: 6.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1314 NYLNWMVR----NLADMElqlgavkRIHGLLKTEAESYEGLLAPSLIPKnwpdQGKIQIQNLSVRYDSSlKPVLKHVNAL 1389
Cdd:COG5265 313 NFLGFVYReirqALADME-------RMFDLLDQPPEVADAPDAPPLVVG----GGEVRFENVSFGYDPE-RPILKGVSFE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1390 IAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPErk 1466
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPD-- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1467 CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM 1546
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270
....*....|....*....|....*....|....
gi 1189438336 1547 TAFADRTVVTIAHRVHTILSADLVIVLKRGAILE 1580
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1093-1600 |
1.17e-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: 146.25 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1093 CSLGIVLCLVTSVTVEWT-GLKVAK-------RLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECL 1164
Cdd:TIGR03797 178 IALALLAAAVGAAAFQLAqSLAVLRletrmdaSLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLTT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1165 SRSTLLCVSALAVISYVTP---VFLVALLPLAIVCYFIQKYFRVA-SRDLQQLDDTTQLPLLshfaETVEGLTTIR---- 1236
Cdd:TIGR03797 257 LLSGIFALLNLGLMFYYSWklaLVAVALALVAIAVTLVLGLLQVRkERRLLELSGKISGLTV----QLINGISKLRvaga 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1237 ---AF-RYEARF-QQKLLEYtDSNNIASlFLTAANRWLEVRmeyigACVVLIAAVTSISNSLHreLSAGLVgLGLTYAL- 1310
Cdd:TIGR03797 333 enrAFaRWAKLFsRQRKLEL-SAQRIEN-LLTVFNAVLPVL-----TSAALFAAAISLLGGAG--LSLGSF-LAFNTAFg 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1311 MVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALI 1390
Cdd:TIGR03797 403 SFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVSLQI 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1391 APGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGID----IAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdperk 1466
Cdd:TIGR03797 477 EPGEFVAIVGPSGSGKSTL----LRLLLGFETPESGSVFYdgqdLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI----- 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1467 CSDSTL-----WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNIL 1541
Cdd:TIGR03797 548 AGGAPLtldeaWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRT 623
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1542 QKVVMTAFA--DRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRkDSVFASFVR 1600
Cdd:TIGR03797 624 QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR-EGLFAQLAR 683
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
712-934 |
1.23e-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: 130.35 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKS---SLLLAalgemqkvsgavFWsslpdseigeDPSPERETATDLDIRK- 787
Cdd:cd03249 14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKStvvSLLER------------FY----------DPTSGEILLDGVDIRDl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 -----RGPVAYASQKPWLLNATVEENIIFESPFNKQryKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRI 859
Cdd:cd03249 71 nlrwlRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 860 SVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
299-590 |
3.40e-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: 130.46 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 299 LVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDvfqPKTQFLGVYFVssqeFLANAYVLAVLlflalllqrtFLQASYY 378
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD---PETQALNVYSL----ALLLLGLAQFI----------LSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 379 VAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGV 458
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 459 S-ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFA 537
Cdd:pfam00664 142 KlTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 538 IYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPL 590
Cdd:pfam00664 222 VANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
449-934 |
4.26e-33 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 136.77 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 449 VILLYYILGVSAligaaVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTN----EMLRGIKLLKLYAWENIFRTRVE- 523
Cdd:TIGR02203 147 IVLLYYSWQLTL-----IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaeETLQGYRVVKLFGGQAYETRRFDa 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 524 ---TTRRKEMTSLRAFAIYTSISIFmntaipIAAVLITFVGHVSFFKEADFSPSVA-FASLSLFHILV-TPLFLLSSVVR 598
Cdd:TIGR02203 222 vsnRNRRLAMKMTSAGSISSPITQL------IASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALiRPLKSLTNVNA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 599 STVKALVSVQKLSEFLSSAeireeqcapheptpqgpaskyQAVEEGLpslhssqpsgssppnhpqplRVVNRKRpAREDC 678
Cdd:TIGR02203 296 PMQRGLAAAESLFTLLDSP---------------------PEKDTGT--------------------RAIERAR-GDVEF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 679 RGLTgplqslvpsadgdadnccvqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEmqkvs 756
Cdd:TIGR02203 334 RNVT-------------------------FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYE----- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 757 gavfwsslPDS-EIGEDPSPERE-TATDLdirkRGPVAYASQKPWLLNATVEENIIFESP--FNKQRYKMVIEACSLQPD 832
Cdd:TIGR02203 384 --------PDSgQILLDGHDLADyTLASL----RRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDF 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 833 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKL 912
Cdd:TIGR02203 452 VDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE-SERLVQAALERLMQG--RTTLVIAHRL 528
|
490 500
....*....|....*....|..
gi 1189438336 913 QYLPHADWIIAMKDGTIQREGT 934
Cdd:TIGR02203 529 STIEKADRIVVMDDGRIVERGT 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
712-924 |
4.69e-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: 135.88 E-value: 4.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpV 791
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-----------SWRDQ--I 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPWLLNATVEENIIFESPFNKQ-RYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 871 VVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAM 924
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEA-LRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
707-934 |
1.11e-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: 127.73 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvSGAVfwsslpdsEIGedpsperetatDLD 784
Cdd:cd03253 7 TFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIlrLLFRFYDVS--SGSI--------LID-----------GQD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 IRK------RGPVAYASQKPWLLNATVEENIIFESP--FNKQrykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSG 853
Cdd:cd03253 65 IREvtldslRRAIGVVPQDTVLFNDTIGYNIRYGRPdaTDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 854 GQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 933
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERG 217
|
.
gi 1189438336 934 T 934
Cdd:cd03253 218 T 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
716-934 |
1.45e-32 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 135.26 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIgedpsperetaTDLDIRKRGP-VAYA 794
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR---LDGADL-----------SQWDREELGRhIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 SQKPWLLNATVEENIifeSPFNKQRYKMVIEACSLqpdIDI------LPHGDQTQIGERGINLSGGQRQRISVARALYQH 868
Cdd:COG4618 412 PQDVELFDGTIAENI---ARFGDADPEKVVAAAKL---AGVhemilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 869 ANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAA--IRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1117-1560 |
1.05e-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: 132.10 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1117 RLHRSLLnRIILAPMRFFETtplGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVC 1196
Cdd:TIGR02868 91 RVYERLA-RQALAGRRRLRR---GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1197 YFIQKYF-----RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEV 1271
Cdd:TIGR02868 167 GFVAPLVslraaRAAEQALARLRGE----LAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1272 RMEYIGACVVLIAAVTSISNSLHRELSAG------LVGLGLTYALMVsnylnwmvrnLADMELQLGAVK----RIHGLLK 1341
Cdd:TIGR02868 243 LTLLAAGLAVLGALWAGGPAVADGRLAPVtlavlvLLPLAAFEAFAA----------LPAAAQQLTRVRaaaeRIVEVLD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1342 TEAESYEGLL-APSLIPKNWPDqgkIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTF 1420
Cdd:TIGR02868 313 AAGPVAEGSApAAGAVGLGKPT---LELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1421 EGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEG 1499
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1500 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1560
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1035-1335 |
1.33e-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: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1035 SLLVFSQLLKHMVLVAIDYWLAKWTDSaltltpaarncslSQECTLDQT-VYAMVFTVLCSLGIVLCLVTSVTVEWTGLK 1113
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDD-------------PVNGPQEHGqVYLSVLGALAILQGITVFQYSMAVSIGGIF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1114 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVAlLPLA 1193
Cdd:cd18559 69 ASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1194 IVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDsNNIASLFLTAANRWLEVRM 1273
Cdd:cd18559 148 LLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1274 EYIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKR 1335
Cdd:cd18559 227 WCVGPCIVLFASFFAY---VSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEV 285
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1363-1601 |
1.22e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 129.70 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1363 QGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSR 1442
Cdd:PRK13657 332 KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDPVLFSGTIRFNLDPERK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1522 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE---FDKpeklLSRKDSVFASF 1598
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAAL 566
|
...
gi 1189438336 1599 VRA 1601
Cdd:PRK13657 567 LRA 569
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
713-942 |
3.85e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.58 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSperetatdldiRKRGPVA 792
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF-------GKPPR-----------RARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQK---PWLLNATVEE--------NIIFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRISV 861
Cdd:COG1121 79 YVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADR-PIGE----LSGGQQQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIqREGTLKDFQR 940
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVReYFDRVLLLNRGLV-AHGPPEEVLT 227
|
..
gi 1189438336 941 SE 942
Cdd:COG1121 228 PE 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
708-932 |
5.74e-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: 120.58 E-value: 5.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpDSEIGEDPSPERetatdldirk 787
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV----DGKPVTGPGPDR---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 rgpvAYASQK----PWLlnaTVEENIIF------ESPfnKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGG 854
Cdd:COG1116 83 ----GVVFQEpallPWL---TVLDNVALglelrgVPK--AERRERArelLELVGLAGFEDAYPH-----------QLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 855 QRQRISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAMKD--GTI 929
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSArpGRI 219
|
...
gi 1189438336 930 QRE 932
Cdd:COG1116 220 VEE 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
708-928 |
7.67e-30 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 118.34 E-value: 7.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslPDSEIGEDPSPERetatdldirk 787
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV---DGKDLTKLSLKEL---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RGPVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 857
Cdd:cd03225 74 RRKVGLVFQNPddQFFGPTVEEEVAF-GLENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 858 RISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 928
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1110-1336 |
1.55e-29 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 121.06 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1110 TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVAL 1189
Cdd:cd18600 97 TLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLAT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1190 LPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFR----YEARFQQKLLEYTdsnniASLFL-TA 1264
Cdd:cd18600 177 VPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHT-----ANWFLyLS 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1265 ANRWLEVRMEYIgaCVVLIAAVTSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1336
Cdd:cd18600 252 TLRWFQMRIEMI--FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1366-1576 |
2.01e-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: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDS---SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAffrmvdtfeghiiidgiDIAKLPLH----T 1438
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSA-----------------LLGELEKLsgsvS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDPVLFSGTIRFN------LDPERkcsdstLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFC 1512
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENilfgkpFDEER------YEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILSADLVIVLKRG 1576
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
707-942 |
3.27e-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: 117.59 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssLPDseiGEDpspereTATDLDIR 786
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV----LVD---GHD------LALADPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 KRGPVAYASQKPWLLNATVEENIIFESPFNKQRykMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 863
Cdd:cd03252 74 LRRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 864 ALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
709-934 |
3.59e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 117.84 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 709 TWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsPERETAtdldiRKr 788
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL-----SRRELA-----RR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 gpVAYASQK---PWLLnaTVEENII--------FESPFNKQRYKMVIEACslqpdidilphgDQTQIG---ERGIN-LSG 853
Cdd:COG1120 77 --IAYVPQEppaPFGL--TVRELVAlgryphlgLFGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 854 GQRQRISVARALYQHANVVFLDDPFSALDIHlsdHlmQAGILELLRD----DKRTVVLVTHKL-QYLPHADWIIAMKDGT 928
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKDGR 215
|
....*.
gi 1189438336 929 IQREGT 934
Cdd:COG1120 216 IVAQGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
712-938 |
3.81e-29 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 117.05 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETatdlDIRKRgpV 791
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-------GKDITKKNLR----ELRRK--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPW--LLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 861
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAF-GPENlglpreeiRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTIQREGTLKDF 938
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
379-934 |
8.63e-29 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 123.23 E-value: 8.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 379 VAIETGINLRGAIQTKIYNKIMhlsTSNLSMGEMTAGQICNlvaiDTNQLMWF--------FFLCPnlWaMPVQIIVgVI 450
Cdd:TIGR01842 69 VLVRIGEKLDGALNQPIFAASF---SATLRRGSGDGLQALR----DLDQLRQFltgpglfaFFDAP--W-MPIYLLV-CF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 451 LLYYILGVSALIGAAVIILLAPV-QYFVATKLSQAQrstlEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRK- 528
Cdd:TIGR01842 138 LLHPWIGILALGGAVVLVGLALLnNRATKKPLKEAT----EASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKy 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 529 ----EMTSLRAFAIYTSISIFMNtaipIAAVLITFVG-HVSFFKEAdfSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 603
Cdd:TIGR01842 214 lsaqSAASDRAGMLSNLSKYFRI----VLQSLVLGLGaYLAIDGEI--TPGMMIAGSILVGRALAPIDGAIGGWKQFSGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 604 LVSVQKLSEFLSSAEIREEQCAPhePTPQGPASKYQAVeeglpslhssqpsgsspPNHPQPLRvvnrkrparedcrgltg 683
Cdd:TIGR01842 288 RQAYKRLNELLANYPSRDPAMPL--PEPEGHLSVENVT-----------------IVPPGGKK----------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 684 plqslvpsadgdadnccvqimggyftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwss 763
Cdd:TIGR01842 332 --------------------------------PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 764 lpdseigedpspeRETATDL---DIRKRGP-VAYASQKPWLLNATVEENII-FESPFNKQRykmVIEACSL---QPDIDI 835
Cdd:TIGR01842 376 -------------RLDGADLkqwDRETFGKhIGYLPQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILR 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 836 LPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYL 915
Cdd:TIGR01842 440 LPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA--IKALKARGITVVVITHRPSLL 517
|
570
....*....|....*....
gi 1189438336 916 PHADWIIAMKDGTIQREGT 934
Cdd:TIGR01842 518 GCVDKILVLQDGRIARFGE 536
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
305-610 |
1.17e-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: 117.70 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 305 FRILADLLGFAGPLCIFGIVdhlGKENDVFQPKTQ---FLGVYFVS--SQEFLANAYvlavllflalllqrtflqasYYV 379
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLL---WFDDPVNGPQEHgqvYLSVLGALaiLQGITVFQY--------------------SMA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 380 AIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVS 459
Cdd:cd18559 62 VSIGGIFASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 460 ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIY 539
Cdd:cd18559 140 AAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 540 TSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18559 220 RALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
712-934 |
2.10e-28 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 114.90 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpV 791
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-----------DLRSR--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPWLLNATVEENIifeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 868
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 869 ANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03244 158 SKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
696-934 |
2.47e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 122.26 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 696 ADNCCVqimggyftWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQ-----KVSGAVFwsslpdseig 770
Cdd:PRK11174 352 AEDLEI--------LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIEL---------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 771 edpsperetaTDLDIRK-RGPVAYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERG 848
Cdd:PRK11174 414 ----------RELDPESwRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 849 INLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA--LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
....*.
gi 1189438336 929 IQREGT 934
Cdd:PRK11174 561 IVQQGD 566
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1186-1580 |
5.79e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.97 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1186 LVALLPLAIVCYFIQKY-------FRVASRDLQQLDDTTQlpllshfaetvEGLTTIR---AFRYE----ARFQQKLLEY 1251
Cdd:PRK10789 141 LLALLPMPVMAIMIKRYgdqlherFKLAQAAFSSLNDRTQ-----------ESLTSIRmikAFGLEdrqsALFAADAEDT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1252 TDSN------------------NIASLFLTAANRWLevrmeyigacvVLIAAVTSisnslhRELSAGLVGLGLTYALMVS 1313
Cdd:PRK10789 210 GKKNmrvaridarfdptiyiaiGMANLLAIGGGSWM-----------VVNGSLTL------GQLTSFVMYLGLMIWPMLA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1314 nyLNWMVrNLadMELQLGAVKRIHGLLKTEAESYEGLLApslIPknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPG 1393
Cdd:PRK10789 273 --LAWMF-NI--VERGSAAYSRIRAMLAEAPVVKDGSEP---VP---EGRGELDVNIRQFTYPQTDHPALENVNFTLKPG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1394 QKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpERKCSDSTLW 1473
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI--ALGRPDATQQ 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1474 EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAf 1549
Cdd:PRK10789 420 EIEHVARLASVhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHNLRQWG- 498
|
410 420 430
....*....|....*....|....*....|.
gi 1189438336 1550 ADRTVVTIAHRVHTILSADLVIVLKRGAILE 1580
Cdd:PRK10789 499 EGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1349-1578 |
6.49e-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: 113.33 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1349 GLLAPSLIpknwpdQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVDTFEGHIIID 1427
Cdd:cd03248 1 GSLAPDHL------KGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVV----ALLENFYQPQGGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1428 GIDIAK-LPLHT---LRSRLSIILQDPVLFSGTIRFNLD-PERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGEN 1502
Cdd:cd03248 71 VLLDGKpISQYEhkyLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1503 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1578
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
718-932 |
6.57e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 113.34 E-value: 6.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssLPDSEIGEDPSPERetatdldirkrgpvAYASQK 797
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV----LVDGEPVTGPGPDR--------------GYVFQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 ----PWLlnaTVEENIIFesPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 864
Cdd:cd03293 82 dallPWL---TVLDNVAL--GLElqgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 865 LYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM--KDGTIQRE 932
Cdd:cd03293 146 LAVDPDVLLLDEPFSALD-ALTREQLQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
716-934 |
2.00e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 119.43 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpVAYAS 795
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLD-----------SWRSR--LAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFL 874
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 875 DDPFSALDIHlSDHlmqaGILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK10789 476 DDALSAVDGR-TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
718-933 |
4.71e-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: 109.45 E-value: 4.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsPERETAtdldiRKrgpVAYASQk 797
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-----SPKELA-----RK---IAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 pwllnatveeniifespfnkqrykmVIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQRISVARALYQHANVVFLDD 876
Cdd:cd03214 81 -------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 877 PFSALDIHlsdhlMQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 933
Cdd:cd03214 124 PTSHLDIA-----HQIELLELLRRLARergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
715-929 |
5.89e-27 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 110.27 E-value: 5.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKV-SGAVFwsslpdseI-GEDPSPERETATDLDIRKRgpVA 792
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVR--------VdGTDISKLSEKELAAFRRRH--IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLLNA-TVEENI----IFESPFNKQRYKMVIEACslqpdidilphgDQTQIGERgIN-----LSGGQRQRISVA 862
Cdd:cd03255 86 FVFQSFNLLPDlTALENVelplLLAGVPKKERRERAEELL------------ERVGLGDR-LNhypseLSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
708-929 |
6.54e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.91 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpSPEretatdlDIRK 787
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM----PPP-------EWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RgpVAYASQKPWLLNATVEENIIF-----ESPFNKQRYKMVIEACSLQPDIdiLphgdQTQIGErginLSGGQRQRISVA 862
Cdd:COG4619 75 Q--VAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI--L----DKPVER----LSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEEL-LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
718-941 |
9.75e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.54 E-value: 9.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPEREtatdlDIRKRgpVAYASQK 797
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-------GEDVARDPA-----EVRRR--IGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWL-LNATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARALYQHA 869
Cdd:COG1131 82 PALyPDLTVRENLRFfarlyglPRKEARERIDELLELFGLTDAAD-------RKVG----TLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 870 NVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKDFQRS 941
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
708-933 |
1.45e-26 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 109.15 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRK 787
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-------GRD-------VTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RGpVAYASQK----PWLlnaTVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQR 856
Cdd:cd03259 72 RN-IGMVFQDyalfPHL---TVAENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 933
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
718-942 |
1.85e-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: 109.51 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETAtDLDIRKRgpVAYASQK 797
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-------GEDISGLSEAE-LYRLRRR--MGMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLLNA-TVEENIIFesPFN----------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:cd03261 86 GALFDSlTVFENVAF--PLRehtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASG-----VIDDLIRSLKKelglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
.
gi 1189438336 942 E 942
Cdd:cd03261 228 D 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
713-925 |
4.07e-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: 108.00 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSeigedpsperetatdldiRKRGPVA 792
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------------------KERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQK---PWLLNATVEE--------NIIFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRISV 861
Cdd:cd03235 72 YVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALER---VGLSELADR-QIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHlsdhlMQAGILEL---LRDDKRTVVLVTHKL-QYLPHADWIIAMK 925
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPK-----TQEDIYELlreLRREGMTILVVTHDLgLVLEYFDRVLLLN 206
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
381-956 |
4.38e-26 |
|
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: 116.21 E-value: 4.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 381 IETGINlrGAIQTKIYNKIMHL--------STSNLSMGEMTAGQICNLVAIDT-NQLMWFFFLCPNLWampvqiivgviL 451
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLG-----------L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAWENIFRTRVE 523
Cdd:TIGR03797 270 MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 524 TTRRKEM------TSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFkeadfspsVAFASLSlfhilvtplfllsSVV 597
Cdd:TIGR03797 350 LELSAQRienlltVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFN--------TAFGSFS-------------GAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 598 RSTVKALVSVQklseflssaeireeQCAPHeptpqgpaskyqaVEEGLPSLHSsqpsgssppnhpQPLRVVNRKRPARed 677
Cdd:TIGR03797 409 TQLSNTLISIL--------------AVIPL-------------WERAKPILEA------------LPEVDEAKTDPGK-- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 678 crgLTGPLqslvpsadgDADNCCvqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSG 757
Cdd:TIGR03797 448 ---LSGAI---------EVDRVT-------FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 758 AVFWSslpdseiGEDPSperetatDLDI----RKRGPVAYASQkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPDI 833
Cdd:TIGR03797 509 SVFYD-------GQDLA-------GLDVqavrRQLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 834 DILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:TIGR03797 572 RAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLS 646
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1189438336 914 YLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEhwktLMNRQ 956
Cdd:TIGR03797 647 TIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQ----LARRQ 685
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1366-1580 |
8.37e-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: 8.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPlHTLRSRLSI 1445
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNLdperkcsdstlwealeiaqlklvvkalpggldaiitegGENFSQGQRQLFCLARAFVRKTSIFI 1525
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1526 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE 1580
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
708-937 |
9.70e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 114.35 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKvsgavfwsslpdSEIGEDPSPERE-TATDLd 784
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDIDE------------GEILLDGHDLRDyTLASL- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 irkRGPVAYASQKPWLLNATVEENIIFESpfnKQRY--KMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRI 859
Cdd:PRK11176 416 ---RNQVALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 860 SVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
708-942 |
2.45e-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: 113.68 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKvsGAVFWSSLpDSEIGeDPSPERetatdldi 785
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQH--GQVLVDGV-DLAIA-DPAWLR-------- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 786 RKRGPVAyasQKPWLLNATVEENIIFESPfnKQRYKMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRISVA 862
Cdd:TIGR01846 531 RQMGVVL---QENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIA 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1366-1601 |
2.62e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 113.02 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVR-YDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF------------SLaffrMVDTFEGhiiidgidiA 1432
Cdd:PRK11174 350 IEAEDLEILsPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSLlnallgflpyqgSL----KINGIEL---------R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1433 KLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQ 1509
Cdd:PRK11174 415 ELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1510 LFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE---FDKpek 1586
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE--- 569
|
250
....*....|....*
gi 1189438336 1587 lLSRKDSVFASFVRA 1601
Cdd:PRK11174 570 -LSQAGGLFATLLAH 583
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
712-912 |
4.11e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 111.68 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpV 791
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD-----------EVRRR--V 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438336 871 VVFLDDPFSALDIHLSDHLmqagiLELLRD--DKRTVVLVTHKL 912
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADEL-----LEDLLAalSGRTVVLITHHL 530
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1366-1578 |
9.86e-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: 9.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdtfeghiiidgidiAKLPLHTLRsrlsi 1445
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTL----------------------ARLILGLLR----- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ilqdPVlfSGTIRfnLDperkCSDSTLWEALEIAQLklvVKALPGglDAIITEG--GEN-FSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03246 54 ----PT--SGRVR--LD----GADISQWDPNELGDH---VGYLPQ--DDELFSGsiAENiLSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1523 IFIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1578
Cdd:cd03246 117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1361-1592 |
1.68e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.30 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1361 PDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSS-FSLAffrmvdTFEGHIIIDGIDIAKLPLH-- 1437
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTlLQLL------TRAWDPQQGEILLNGQPIAdy 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 ---TLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQL-KLVvkALPGGLDAIITEGGENFSQGQRQL 1510
Cdd:PRK11160 408 seaALRQAISVVSQRVHLFSATLRDNLllaAPN--ASDEALIEVLQQVGLeKLL--EDDKGLNAWLGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
...
gi 1189438336 1590 RKD 1592
Cdd:PRK11160 563 QQG 565
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
715-933 |
4.12e-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: 102.58 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETatDLDIRkRGPVAYA 794
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-------GKDLLKLSRR--LRKIR-RKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 SQKPWL-LNA--TVEENI-----IFESPFNKQRYKMVI--EACSLQPDIDIL---PHGdqtqigerginLSGGQRQRISV 861
Cdd:cd03257 88 FQDPMSsLNPrmTIGEQIaeplrIHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKDGTIQREG 933
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKLQEelglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
716-934 |
4.26e-24 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 109.02 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgeDPSperetatdlDIRKRgpVAYAS 795
Cdd:TIGR02204 354 PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL--DPA---------ELRAR--MALVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLLNATVEENIIFESPfnKQRYKMVIEAC-SLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 872
Cdd:TIGR02204 421 QDPVLFAASVMENIRYGRP--DATDEEVEAAArAAHAHefISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 873 FLDDPFSALDIhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:TIGR02204 499 LLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVAQGT 557
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
707-934 |
5.91e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.07 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATdLDIR 786
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-------GKDLTKLSRRSL-RELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 KR-GPV---AYASqkpwlLNA--TVEEnIIFESPFN------KQRYKMV---IEACSLQPD-IDILPHGdqtqigergin 850
Cdd:COG1123 342 RRvQMVfqdPYSS-----LNPrmTVGD-IIAEPLRLhgllsrAERRERVaelLERVGLPPDlADRYPHE----------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 851 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIA 923
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvRYI--ADRVAV 477
|
250
....*....|.
gi 1189438336 924 MKDGTIQREGT 934
Cdd:COG1123 478 MYDGRIVEDGP 488
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
715-932 |
9.27e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.27 E-value: 9.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKV-SGAVFW-----SSLPDSEIGEdpsperetatdldIRKR 788
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVLIdgqdiSSLSERELAR-------------LRRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 gPVAYASQKPWLL-NATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 860
Cdd:COG1136 87 -HIGFVFQFFNLLpELTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 861 VARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 932
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
716-929 |
1.03e-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: 99.60 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdldiRKRGPVAYAS 795
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN-------------ELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVVFLD 875
Cdd:cd03246 83 QDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 876 DPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03246 122 EPNSHLDVEGERALNQA--IAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
714-928 |
1.62e-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: 98.47 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpDSEIGEDPSPERetatdldirkRGPVAY 793
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID---GKDIAKLPLEEL----------RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVVF 873
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 874 LDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 928
Cdd:cd00267 104 LDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
714-937 |
1.73e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 107.90 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwsslpdsEIGEDPSPeretATDLDIRK-RGPVA 792
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSG----------EILLNGFS----LKDIDRHTlRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLLNATVEENIIFESPFNKQRyKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHA 869
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 870 NVVFLDDPFSALDIhlsdhLMQAGILE-LLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:TIGR01193 631 KVLILDESTSNLDT-----ITEKKIVNnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
712-941 |
2.76e-23 |
|
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: 100.45 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgeDPSPERetatdldiRKRGpv 791
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ--DPVELR--------RKIG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 aYASQKPWLL-NATVEENII-------FESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRISV 861
Cdd:cd03295 79 -YVIQQIGLFpHMTVEENIAlvpkllkWPKEKIRERADELLALVGLDPAefADRYPH-----------ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQR 940
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
.
gi 1189438336 941 S 941
Cdd:cd03295 226 S 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1226-1590 |
3.89e-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: 105.99 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1226 AETVEGLTTIRAFRyeARFQQKLLEYTDSNNIASL---FLTAANRWLEVRMEYI----GACVVLiaavtsisnslHRELS 1298
Cdd:COG4618 204 AEVIEAMGMLPALR--RRWQRANARALALQARASDragGFSALSKFLRLLLQSAvlglGAYLVI-----------QGEIT 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1299 AGlvglgltyALMVSNYLnwMVRNLADMELQLG----------AVKRIHGLLKTEAESYEGLLAPslipknwPDQGKIQI 1368
Cdd:COG4618 271 PG--------AMIAASIL--MGRALAPIEQAIGgwkqfvsarqAYRRLNELLAAVPAEPERMPLP-------RPKGRLSV 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1369 QNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdtfeghiiidgidiAKL-------------- 1434
Cdd:COG4618 334 ENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTL----------------------ARLlvgvwpptagsvrl 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1435 ---PLHTL-RSRLSIIL----QDPVLFSGTI-----RF-NLDPERkcsdstlweALEIAQL----KLVVKaLPGGLDAII 1496
Cdd:COG4618 392 dgaDLSQWdREELGRHIgylpQDVELFDGTIaeniaRFgDADPEK---------VVAAAKLagvhEMILR-LPDGYDTRI 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1497 TEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILSADLVIVLKR 1575
Cdd:COG4618 462 GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRD 541
|
410
....*....|....*
gi 1189438336 1576 GAILEFDKPEKLLSR 1590
Cdd:COG4618 542 GRVQAFGPRDEVLAR 556
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
708-941 |
4.50e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 100.26 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATdldirk 787
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD-------GRPVTRRRRKAF------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RGPVAYASQKPWL-LNA--TVEENI-----IFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtQigerginLSGGQRQR 858
Cdd:COG1124 78 RRRVQMVFQDPYAsLHPrhTVDRILaeplrIHGLPDREERIAELLEQVGLPPSFlDRYPH----Q-------LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 859 ISVARALYQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEEL 221
|
....*...
gi 1189438336 934 TLKDFQRS 941
Cdd:COG1124 222 TVADLLAG 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
708-933 |
7.82e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 97.38 E-value: 7.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdldIRK 787
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA------------LSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RgpVAYASQKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQ 867
Cdd:cd03247 76 L--ISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 868 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 933
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSL-IFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
712-939 |
1.04e-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: 98.79 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpDSEIGEDPSPEretatdldIRK-RGP 790
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID---GTDINKLKGKA--------LRQlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLLN-ATVEENI---------IFESPFN------KQRykmvieACSLQPDIDILPHGDQtqigeRGINLSGG 854
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVlsgrlgrrsTWRSLFGlfpkeeKQR------ALAALERVGLLDKAYQ-----RADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 855 QRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 933
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL-LKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDG 227
|
....*.
gi 1189438336 934 TLKDFQ 939
Cdd:cd03256 228 PPAELT 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
718-879 |
1.58e-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: 95.41 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATdldirkRGPVAYASQK 797
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD-------GQDLTDDERKSL------RKEIGYVFQD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLLNA-TVEENIIFESPFnKQRYKMVIEAcslQPDIDI----LPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 872
Cdd:pfam00005 68 PQLFPRlTVRENLRLGLLL-KGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 1189438336 873 FLDDPFS 879
Cdd:pfam00005 144 LLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1366-1590 |
8.45e-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: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD---TFEGHIIIDGIDIAKLPLHTLRSR 1442
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDP--VLFSGTIRFNLD--PERKCSDSTLWEALEIAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFV 1518
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAEARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1519 RKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:COG1123 159 LDPDLLIADEPTTALDVTT----QAEILDLLRElqrergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
718-929 |
1.18e-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: 93.62 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPEREtatdlDIRKRgpVAYASQK 797
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-------GKDIKKEPE-----EVKRR--IGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLL-NATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHANVVFLDD 876
Cdd:cd03230 82 PSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 877 PFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:cd03230 122 PTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
716-942 |
1.54e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLpdsEIGEDPSpeRETATDLDIRKrgpvayas 795
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGL---DVATTPS--RELAKRLAILR-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWL-LNATVEENIIF-ESPFNKQR-----YKMVIEAcslqpdIDILphgDQTQIGERGIN-LSGGQRQRISVARALYQ 867
Cdd:COG4604 82 QENHInSRLTVRELVAFgRFPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 868 HANVVFLDDPFSALDIHLSDHLMQagILELLRDDK-RTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1366-1592 |
1.90e-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: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAF------------FRMVDTfeghiiidgidiAK 1433
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkptsgevlVDGKDI------------TK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPLHTLRSRLSIILQDPV--LFSGTIR---------FNLDPErkcsdstlwEALEIAQ--LKLVvkalpgGLDAIITEGG 1500
Cdd:COG1122 68 KNLRELRRKVGLVFQNPDdqLFAPTVEedvafgpenLGLPRE---------EIRERVEeaLELV------GLEHLADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDpRGRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
250
....*....|....
gi 1189438336 1579 LEFDKPEKLLSRKD 1592
Cdd:COG1122 213 VADGTPREVFSDYE 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
713-934 |
2.03e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.84 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFWsslpDseiGEDpsperetATDLDIRKRGp 790
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrmIAGLEDPT--SGEILI----G---GRD-------VTDLPPKDRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLL-NATVEENIIF------ESPfnKQRYKMVIEAcslqpdIDILphgdqtQIGE----RGINLSGGQRQRI 859
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFplklrkVPK--AEIDRRVREA------AELL------GLEDlldrKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 860 SVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQREG 933
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVE-MRAEIKRLHRRLGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQVG 216
|
.
gi 1189438336 934 T 934
Cdd:COG3839 217 T 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
712-929 |
3.51e-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: 94.07 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvsgavfwsslpDSEIGEDPSPeretATDLDIRK-R 788
Cdd:cd03248 25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQ------------GGQVLLDGKP----ISQYEHKYlH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 GPVAYASQKPWLLNATVEENIIFESPfnKQRYKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARAL 865
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 866 YQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03248 166 IRNPQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1367-1576 |
5.61e-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: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSII 1446
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1447 LQdpvlfsgtirfnldperkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFIM 1526
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1527 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTI-LSADLVIVLKRG 1576
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
833-1603 |
7.40e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 100.10 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 833 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKL 912
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 913 QYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVTERKATEPP----QGLSRA-MSSRDGL 987
Cdd:PTZ00265 641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSyiieQGTHDAlMKNKNGI 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 988 -----------------------------------------------LQDEEEEEEEAAESEEDDNLSS----------- 1009
Cdd:PTZ00265 721 yytminnqkvsskkssnndndkdsdmkssaykdsergydpdemngnsKHENESASNKKSCKMSDENASEnnaggklpflr 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1010 -MLHQRAEIP------WRACAKYLSSAGILLLSLLVFSQLLKhmvLVAIDYwlAKWTDSALTLTPAARNCSlsqectlDQ 1082
Cdd:PTZ00265 801 nLFKRKPKAPnnlrivYREIFSYKKDVTIIALSILVAGGLYP---VFALLY--AKYVSTLFDFANLEANSN-------KY 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVftvlcslgIVLCLVTSVTVE-----WTGLKVAKRLHRSLLNRIILAPMRFFEttplgsilnrfsSDCNT---ID 1154
Cdd:PTZ00265 869 SLYILV--------IAIAMFISETLKnyynnVIGEKVEKTMKRRLFENILYQEISFFD------------QDKHApglLS 928
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1155 QHIPSTLECLSRSTllcVSALAVISYVTPVFLVALLplaivcyfIQKYFrvasrdlqqlddttqLPLLshfAETVEGLTT 1234
Cdd:PTZ00265 929 AHINRDVHLLKTGL---VNNIVIFTHFIVLFLVSMV--------MSFYF---------------CPIV---AAVLTGTYF 979
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1235 I--RAFRYEARF-QQKLLEYTDSNNIASLFL-----------------------TAANRWLEvrmEYIgaCVVLIAAVTS 1288
Cdd:PTZ00265 980 IfmRVFAIRARLtANKDVEKKEINQPGTVFAynsddeifkdpsfliqeafynmnTVIIYGLE---DYF--CNLIEKAIDY 1054
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1289 ISNSLHRE--LSAGLVGLGLTYALMVSNYLNW----MVRN----LADMELQL----------GAVKRIHGLLKTEAESYE 1348
Cdd:PTZ00265 1055 SNKGQKRKtlVNSMLWGFSQSAQLFINSFAYWfgsfLIRRgtilVDDFMKSLftflftgsyaGKLMSLKGDSENAKLSFE 1134
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1349 G----LLAPSLIP---------KNWPD-QGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAF 1413
Cdd:PTZ00265 1135 KyyplIIRKSNIDvrdnggiriKNKNDiKGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLL 1214
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1414 FRMVD-------------------------------------TFEGHIIIDGIDIAKL-----------------PLHTL 1439
Cdd:PTZ00265 1215 MRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnEFSLTKEGGSGEDSTVfknsgkilldgvdicdyNLKDL 1294
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1440 RSRLSIILQDPVLFSGTIRFNLDPERKcsDSTLWE---ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARA 1516
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENIKFGKE--DATREDvkrACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1517 FVRKTSIFIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL----KRGAILEFDKP-EKLLS 1589
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAHGThEELLS 1452
|
970
....*....|....
gi 1189438336 1590 RKDSVFASFVRADK 1603
Cdd:PTZ00265 1453 VQDGVYKKYVKLAK 1466
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
713-944 |
8.17e-21 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 93.38 E-value: 8.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETAtdldiRKRgpVA 792
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-------GEDVRKEPREA-----RRQ--IG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWL-LNATVEENIIFESPFN-------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARA 864
Cdd:COG4555 78 VLPDERGLyDRLTVRENIRYFAELYglfdeelKKRIEELIELLGLEEFLDRRVGE-----------LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 865 LYQHANVVFLDDPFSALDIhLSDHLMQaGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSEC 943
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDV-MARRLLR-EILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
.
gi 1189438336 944 Q 944
Cdd:COG4555 225 E 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
708-945 |
1.33e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 97.67 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALG---EMQKVSGAVFWSslpdseiGEDPsperetaTDLD 784
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLD-------GRDL-------LELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 IRKRGP-VAYASQKPW--LLNATVEENIIfESPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 853
Cdd:COG1123 78 EALRGRrIGMVFQDPMtqLNPVTVGDQIA-EALENlglsraeaRARVLELLEAVGLERRLDRYPH-----------QLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 854 GQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQY-LPHADWIIAMKDGT 928
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTT-----QAEILDLLRELQRergtTVLLITHDLGVvAEIADRVVVMDDGR 220
|
250
....*....|....*..
gi 1189438336 929 IQREGTLKDFQRSECQL 945
Cdd:COG1123 221 IVEDGPPEEILAAPQAL 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
714-928 |
2.01e-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: 90.32 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDLdirkRGPVAY 793
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------GEDLTDLEDELPPL----RRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLL-NATVEENIIFespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHANVV 872
Cdd:cd03229 81 VFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 873 FLDDPFSALDIhlsdhLMQAGILELLRD----DKRTVVLVTHKLQYLPH-ADWIIAMKDGT 928
Cdd:cd03229 123 LLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
710-929 |
2.38e-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: 90.93 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 710 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPsperetATDLdirkRG 789
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI---EIDGIDISTIP------LEDL----RS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 PVAYASQKPWLLNATVEENIifeSPFNKQRYKMVIEACSlqpdidilphgdqtqIGERGINLSGGQRQRISVARALYQHA 869
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 870 NVVFLDDPFSALDIHlSDHLMQAGILELLRDDkrTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03369 145 RVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
718-948 |
2.48e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 94.44 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgEMQKvSGAVFWSslpdseiGEDpspereTATDLDIRKRGpVAYAS 795
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLriIAGL-ETPD-SGRIVLN-------GRD------LFTNLPPRERR-VGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLL-NATVEENIIF----ESPFNKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQ 867
Cdd:COG1118 82 QHYALFpHMTVAENIAFglrvRPPSKAEIRARVeelLELVQLEGLADRYPS-----------QLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 868 HANVVFLDDPFSALDIHLSDHLMQaGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDfqrsecqLF 946
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRR-WLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDE-------VY 222
|
..
gi 1189438336 947 EH 948
Cdd:COG1118 223 DR 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1366-1590 |
3.16e-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: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEG----HIIIDGIDIAKLPLHtLRS 1441
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTL----LRMLAGLLKpdsgSILIDGEDVRKEPRE-ARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDPVLFSG-TIRFNLD---PERKCSDSTLWEALEIaqlklVVKALpgGLDAIITEGGENFSQGQRQLFCLARAF 1517
Cdd:COG4555 75 QIGVLPDERGLYDRlTVRENIRyfaELYGLFDEELKKRIEE-----LIELL--GLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1518 VRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDvMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
718-942 |
3.77e-20 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 91.19 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDlDIRKRgpVAYASQK 797
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-------GQDITGLSEKELY-ELRRR--IGMLFQG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLLNA-TVEENIIFesPFN----------KQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALY 866
Cdd:COG1127 91 GALFDSlTVFENVAF--PLRehtdlseaeiRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 867 QHANVVFLDDPFSALDIHLS---DHLmqagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSaviDEL----IRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1366-1587 |
7.56e-20 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 90.32 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHII--------IDGIDIAKLPLH 1437
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDegevlldgKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 tLRSRLSIILQDPVLFSGTIRFNLD--------PERKCSDSTLWEALEIAQLKLVVKALPGGLDaiiteggenFSQGQRQ 1509
Cdd:cd03260 79 -LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1510 LFCLARAFVRKTSIFIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKL 1587
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
718-913 |
1.02e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 89.93 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFWSSLPDSEIGEDPsperetatdLDIRKRgpVA 792
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDV---------LELRRR--VG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLLNATVEENI-----IFESPFNKQRYKMVIEACS---LQPDIDILPHGDQtqigerginLSGGQRQRISVARA 864
Cdd:cd03260 85 MVFQKPNPFPGSIYDNVayglrLHGIKLKEELDERVEEALRkaaLWDEVKDRLHALG---------LSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438336 865 LYQHANVVFLDDPFSALDIHlSDHLMQAGILELlrDDKRTVVLVTHKLQ 913
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQ 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1367-1576 |
2.66e-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: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSII 1446
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1447 LQDP--VLFSGTIR----FNLdPERKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRK 1520
Cdd:cd03225 81 FQNPddQFFGPTVEeevaFGL-ENLGLPEEEIEERVEEA-LELV------GLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1521 TSIFIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
708-947 |
4.86e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.04 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPdseigedpsperETATDL-DIR 786
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA------------ITDDNFeKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 KRGPVAYASQKPWLLNATVEENIIFESPFNKQRY-KMVIEACSLQPDIDILPHGD-QTQigergiNLSGGQRQRISVARA 864
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYdEMHRRVSEALKQVDMLERADyEPN------ALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 865 LYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQ 944
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
...
gi 1189438336 945 LFE 947
Cdd:PRK13648 236 LTR 238
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
713-912 |
6.93e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdseigedpspERETATdldirkrgPVA 792
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------------RRAGGA--------RVA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQK---PWLLNATVEENIIF-----ESPFNKQRY--KMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISVA 862
Cdd:NF040873 59 YVPQRsevPDSLPLTVRDLVAMgrwarRGLWRRLTRddRAAVDDALERVGLADLAG---RQLGE----LSGGQRQRALLA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHLSDHLmqAGILELLRDDKRTVVLVTHKL 912
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDL 179
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
712-936 |
7.25e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.86 E-value: 7.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgEDPSPEREtatdldirkrgpV 791
Cdd:TIGR00958 492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY-DHHYLHRQ------------V 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPWLLNATVEENIIFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMaAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 871 VVFLDDPFSALDIHlSDHLMQagilELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 936
Cdd:TIGR00958 638 VLILDEATSALDAE-CEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
718-910 |
1.35e-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: 85.99 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETAtdldirkRGPVAYASQK 797
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-------GEPIRDAREDY-------RRRLAYLGHA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLLNA-TVEENIIF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHANV 871
Cdd:COG4133 84 DGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1189438336 872 VFLDDPFSALDIHLSDHLmqAGILELLRDDKRTVVLVTH 910
Cdd:COG4133 153 WLLDEPFTALDAAGVALL--AELIAAHLARGGAVLLTTH 189
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
701-934 |
1.49e-18 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 91.93 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 701 VQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALgeMQKVSGAVFWSSLPDSEIgedpSPERE 778
Cdd:TIGR03796 478 VELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIakLVAGL--YQPWSGEILFDGIPREEI----PREVL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 779 TATdldirkrgpVAYASQKPWLLNATVEENIIFESPFNKQryKMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQ 855
Cdd:TIGR03796 552 ANS---------VAMVDQDIFLFEGTVRDNLTLWDPTIPD--ADLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQ 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 856 RQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:TIGR03796 621 RQRLEIARALVRNPSILILDEATSALDP-----ETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
713-924 |
1.77e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.31 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpSPERetatdldirKRGPVA 792
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL----KPEI---------YRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQ----PDidilphgdqtQIGERGIN-LSGGQRQRISVARALYQ 867
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLErfalPD----------TILTKNIAeLSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 868 HANVVFLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 924
Cdd:PRK10247 155 MPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
707-934 |
2.09e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEdpsperetaTDLdir 786
Cdd:PRK11160 345 SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---------AAL--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 kRGPVAYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDIlPHGDQTQIGERGINLSGGQRQRISVARAL 865
Cdd:PRK11160 413 -RQAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 866 YQHANVVFLDDPFSALDIHLSDHlmqagILELLRD---DKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQ-----ILELLAEhaqNK-TVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
713-933 |
4.38e-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: 84.61 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFwsslpdseIGEdpsperETATDLDIRKRGp 790
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLrmIAGLEEPT--SGRIY--------IGG------RDVTDLPPKDRD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLL-NATVEENIIFESPFNKQRyKMVIE------ACSLQpdIDILPHGDQTQigerginLSGGQRQRISVAR 863
Cdd:cd03301 74 IAMVFQNYALYpHMTVYDNIAFGLKLRKVP-KDEIDervrevAELLQ--IEHLLDRKPKQ-------LSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 864 ALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 933
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
713-937 |
4.73e-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: 84.98 E-value: 4.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIgedpsperetaTDLDIRKRgPVA 792
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL---LDGKDI-----------TNLPPHKR-PVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLL-NATVEENIIF-----ESPFNKQRYKmVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRISVARAL 865
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFglrlkKLPKAEIKER-VAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 866 YQHANVVFLDDPFSALDIHLSDHlMQagiLELLRDDKR---TVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKD-MQ---LELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
713-934 |
5.34e-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: 87.46 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRgPVA 792
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-------GRD-------VTGLPPEKR-NVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQK----PWLlnaTVEENIIF------ESPfnKQRYKMVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRISV 861
Cdd:COG3842 81 MVFQDyalfPHL---TVAENVAFglrmrgVPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 862 ARALyqhAN---VVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKlQY--LPHADWIIAMKDGTIQREGT 934
Cdd:COG3842 147 ARAL---APeprVLLLDEPLSALDAKLREE-MREELRRLQRELGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
713-934 |
1.04e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 84.31 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRGpVA 792
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-------GED-------ATDVPVQERN-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLL-NATVEENIIF--------ESPFN---KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 860
Cdd:cd03296 78 FVFQHYALFrHMTVFDNVAFglrvkprsERPPEaeiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 861 VARALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKEL-RRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
716-934 |
1.04e-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: 89.11 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvSGAVFwsslpdseIGedpsperetatDLDIRKrgpVAY 793
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRIL--------ID-----------GQDIRD---VTQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 AS---------QKPWLLNATVEENIIFESPFNKQRykMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISV 861
Cdd:COG5265 428 ASlraaigivpQDTVLFNDTIAYNIAYGRPDASEE--EVEAAaraAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAI 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSR-TERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
712-910 |
1.56e-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: 83.23 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDLDIRKRGpV 791
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-------GQDVSDLRGRAIPYLRRKIG-V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKpWLLNATVEENIIF------ESPFN-KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARA 864
Cdd:cd03292 83 VFQDFR-LLPDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438336 865 LYQHANVVFLDDPFSALDihlSDHlmQAGILELLRD-DKR--TVVLVTH 910
Cdd:cd03292 151 IVNSPTILIADEPTGNLD---PDT--TWEIMNLLKKiNKAgtTVVVATH 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
728-933 |
2.03e-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: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 728 GQLTMIVGQVGCGKSSLL--LAAL-----GEMqKVSGAVfwssLPDSEIGEDPSPERetatdldiRKrgpVAYASQKPWL 800
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLrcIAGLekpdgGTI-VLNGTV----LFDSRKKINLPPQQ--------RK---IGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 801 L-NATVEENIIFESPFNKQRYKMVIEAcslqpdiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHANVVFLDDPF 878
Cdd:cd03297 87 FpHLNVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 879 SALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL---QYLphADWIIAMKDGTIQREG 933
Cdd:cd03297 160 SALDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
718-968 |
2.04e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFW--SSLPDSEIgeDPSperetatdlDIRKRgp 790
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFhgKNLYAPDV--DPV---------EVRRR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLLNATVEENIIFESPFNKQRYKM--VIEACSLQPdidILPHGDQTQIGERGINLSGGQRQRISVARALYQH 868
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIAYGARINGYKGDMdeLVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 869 ANVVFLDDPFSALdihlsDHLMQAGILELLRDDKR--TVVLVTHKLQYLPHADWIIAM----KDGTIQREGTLKDFQRSE 942
Cdd:PRK14243 170 PEVILMDEPCSAL-----DPISTLRIEELMHELKEqyTIIIVTHNMQQAARVSDMTAFfnveLTEGGGRYGYLVEFDRTE 244
|
250 260
....*....|....*....|....*.
gi 1189438336 943 cqlfehwkTLMNRQDQELEKETVTER 968
Cdd:PRK14243 245 --------KIFNSPQQQATRDYVSGR 262
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
718-942 |
2.47e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 84.30 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdsEIGEDPSPERETATDL-DIRKRgpVAYASQ 796
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV--------TIGERVITAGKKNKKLkPLRKK--VGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 797 KP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALY 866
Cdd:PRK13634 93 FPehQLFEETVEKDICF-GPMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLKD-FQRS 941
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEM-FYKLHKEKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREiFADP 237
|
.
gi 1189438336 942 E 942
Cdd:PRK13634 238 D 238
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
718-934 |
2.75e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGED-------------PSPEretatdlD 784
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlarrlallpqhhLTPE-------G 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 IRKRGPVAYAsQKPWL-----LnatveeniifeSPFNKQRYKMVIEacslqpdidilphgdQTQIGE----RGINLSGGQ 855
Cdd:PRK11231 91 ITVRELVAYG-RSPWLslwgrL-----------SAEDNARVNQAME---------------QTRINHladrRLTDLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 856 RQRISVARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
711-928 |
3.00e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAAL---GemqkvSGAVfwsSLPDSEigedpsperetatdldi 785
Cdd:COG4178 372 TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLraIAGLwpyG-----SGRI---ARPAGA----------------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 786 rkrgPVAYASQKPWLLNATVEENIIF---ESPFNKQRYKMVIEACSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVA 862
Cdd:COG4178 427 ----RVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLG---HLAERLDEEADWDQV--LSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--TTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1383-1531 |
5.46e-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: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1383 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL 1461
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1462 DPERKC---SDSTLWEALEIAQLKLvvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1531
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 ... |
1366-1577 |
5.76e-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: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHI--IIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIIL--QDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:cd03290 80 SVAYaaQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1522 SIFIMDEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVIVLKRGA 1577
Cdd:cd03290 160 NIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
718-958 |
6.15e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemQKVSGAVFWSSLPDSEI---GEdpSPERETATDLDIRK-RGPVAY 793
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKSAGSHIellGR--TVQREGRLARDIRKsRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLLNA-TVEENIIF----ESPFNKQRYKMVIEAcSLQPDIDILphgdqTQIG------ERGINLSGGQRQRISVA 862
Cdd:PRK09984 91 IFQQFNLVNRlSVLENVLIgalgSTPFWRTCFSWFTRE-QKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVM-----DTLRDinqnDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQ 239
|
250 260
....*....|....*....|.
gi 1189438336 938 FQRSEcqlFEHWKTLMNRQDQ 958
Cdd:PRK09984 240 FDNER---FDHLYRSINRVEE 257
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
717-942 |
7.42e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.72 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 717 TLSNITIR-----------IPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDI 785
Cdd:COG3840 3 RLDDLTYRygdfplrfdltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-------GQD-------LTALPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 786 RKRgPVAYASQK----PWLlnaTVEENIIFE-------SPFNKQRYKMVIEACSLQPDIDILPhgDQtqigerginLSGG 854
Cdd:COG3840 69 AER-PVSMLFQEnnlfPHL---TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 855 QRQRISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 933
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPALRQE-MLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADG 212
|
....*....
gi 1189438336 934 TLKDFQRSE 942
Cdd:COG3840 213 PTAALLDGE 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
703-929 |
9.53e-17 |
|
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: 85.51 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 703 IMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGeMQKVSGAVFWsslpdseIGEDPSPERETAtD 782
Cdd:COG4172 287 IKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRF-------DGQDLDGLSRRA-L 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 783 LDIRKRGPVA----YASQKPWLlnaTVEEnIIFE---------SPfnKQRYKMVIEACS---LQPD-IDILPHgdqtqig 845
Cdd:COG4172 358 RPLRRRMQVVfqdpFGSLSPRM---TVGQ-IIAEglrvhgpglSA--AERRARVAEALEevgLDPAaRHRYPH------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 846 ErginLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRD--DKR--TVVLVTHKLQ---YLphA 918
Cdd:COG4172 425 E----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV-----QAQILDLLRDlqREHglAYLFISHDLAvvrAL--A 493
|
250
....*....|.
gi 1189438336 919 DWIIAMKDGTI 929
Cdd:COG4172 494 HRVMVMKDGKV 504
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1358-1573 |
1.01e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.62 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1358 KNWPDQGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAK-LP 1435
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 LHTLRSRLSIILQDPVLFSGTIRFN----------------------------LDPERKC--------------SDSTLW 1473
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdlealsnyynedgndsqenKNKRNSCrakcagdlndmsntTDSNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1474 -------------EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1537
Cdd:PTZ00265 535 iemrknyqtikdsEVVDVSKKVLIhdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270
....*....|....*....|....*....|....*...
gi 1189438336 1538 ENILQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL 1573
Cdd:PTZ00265 615 EYLVQKTInnLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
708-924 |
1.09e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.60 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQ---KVSGAVFwssLPDSEIgedpsperetaTDLD 784
Cdd:COG4136 7 LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVL---LNGRRL-----------TALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 IRKRGpVAYASQKPWLL-NATVEENIIF---ESPFNKQRYKMVIEAcsLQpDIDiLPHgdqtqIGERGIN-LSGGQRQRI 859
Cdd:COG4136 73 AEQRR-IGILFQDDLLFpHLSVGENLAFalpPTIGRAQRRARVEQA--LE-EAG-LAG-----FADRDPAtLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 860 SVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 924
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQ-FREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
716-910 |
1.31e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.45 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssLPDSEIGEDPSPERetatdldirkrGPVAyas 795
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI----TLDGVPVTGPGADR-----------GVVF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QK----PWLlnaTVEENIIFESPFNK----QRYKMVIEACSLqpdIDiLPHGDQTQIGErginLSGGQRQRISVARALYQ 867
Cdd:COG4525 83 QKdallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VG-LADFARRRIWQ----LSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1189438336 868 HANVVFLDDPFSALDIhLSDHLMQAGILELLRDDKRTVVLVTH 910
Cdd:COG4525 152 DPRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
716-934 |
2.59e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.24 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaALgeMQKVSgavfwsslpdseigeDPSPERETATDLDIRK------RG 789
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI--NL--LQRVF---------------DPQSGRILIDGTDIRTvtraslRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 PVAYASQKPWLLNATVEENIIFESPfNKQRYKMVIEACSLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 867
Cdd:PRK13657 410 NIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 868 HANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAA--LDELMKG-RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
725-933 |
2.84e-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: 79.46 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 725 IPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERetatdldirkrgPVAYASQKPWLL-NA 803
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV---LINGVDVTAAPPADR------------PVSMLFQENNLFaHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 804 TVEENI-------IFESPFNKQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALYQHANVVFLDD 876
Cdd:cd03298 86 TVEQNVglglspgLKLTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 877 PFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:cd03298 155 PFAALDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
707-937 |
3.27e-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: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSPERETAtdldiR 786
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVL---VDGTDLTLLSGKELRKA-----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 KRgpVAYASQKPWLLNA-TVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQR 858
Cdd:cd03258 82 RR--IGMIFQHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 859 ISVARALYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223
|
....
gi 1189438336 934 TLKD 937
Cdd:cd03258 224 TVEE 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
714-929 |
3.34e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.85 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEdpspERETATDLDIRKRGpVAY 793
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-------GK----EVSFASPRDARRAG-IAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVVF 873
Cdd:cd03216 80 VYQ------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 874 LDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:cd03216 106 LDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
712-937 |
3.56e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.51 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSperetaTDLDIRKRGPV 791
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL---IKGEPIKYDKK------SLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:PRK13639 83 VFQNPDDQLFAPTVEEDVAF-GPLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 864 ALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKE 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
718-931 |
4.46e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKVSGAVFWSSLPD-SEIGEDpsperetatDLDIRKRGPVAYASQ 796
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDKPTSGTYRVAGQDvATLDAD---------ALAQLRREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 797 KPWLL-NATVEENIifESPF---------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:PRK10535 94 RYHLLsHLTAAQNV--EVPAvyaglerkqRLLRAQELLQRLGLEDRVEYQPS-----------QLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQR 931
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
712-937 |
4.69e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.28 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPdseigedpsperetatdLDIRKRGpv 791
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-----------------IDYSRKG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 ayasqkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPhgdQTQIGER--------GIN---------LSGG 854
Cdd:PRK13636 77 --------LMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLP---EDEVRKRvdnalkrtGIEhlkdkpthcLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 855 QRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 933
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL-LVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
|
....
gi 1189438336 934 TLKD 937
Cdd:PRK13636 225 NPKE 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1366-1581 |
5.00e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 79.09 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD------TFEGHIIIDGIDIAKLPLh 1437
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiIFDGKDLLKLSRRLRKIR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 tlRSRLSIILQDPvlFSgtirfNLDPERKCSDStLWEALEI--------AQLKLVVKALPG-GLDAII-----TEggenF 1503
Cdd:cd03257 81 --RKEIQMVFQDP--MS-----SLNPRMTIGEQ-IAEPLRIhgklskkeARKEAVLLLLVGvGLPEEVlnrypHE----L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1504 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
...
gi 1189438336 1579 LEF 1581
Cdd:cd03257 225 VEE 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
711-910 |
5.61e-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: 77.19 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMqkvsgavfWSsLPDSEIGedpSPERETatdldirkrgp 790
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGL--------WP-WGSGRIG---MPEGED----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLLNATVEENIIFespfnkqrykmvieacslqpdidilPHGDqtqigergiNLSGGQRQRISVARALYQHAN 870
Cdd:cd03223 66 LLFLPQRPYLPLGTLREQLIY-------------------------PWDD---------VLSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438336 871 VVFLDDPFSALDIHLSDHLMQagileLLRDDKRTVVLVTH 910
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGH 146
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
718-929 |
6.85e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGemQKVSGAVFWSSLPDSEIGEDpsperetaTDLDIRKrgpvayAS 795
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLrlLAGLE--TPSAGELLAGTAPLAEARED--------TRLMFQD------AR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWllnATVEENIIFESPFN-KQRYKMVIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQHANVVFL 874
Cdd:PRK11247 92 LLPW---KKVIDNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 875 DDPFSALDIhLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 929
Cdd:PRK11247 158 DEPLGALDA-LTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
720-934 |
8.79e-16 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 79.22 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpspereTATDL-DIRKRgPVAYASQKP 798
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAM---------SRKELrELRRK-KISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 799 WLL-NATVEENIIF------ESPFNKQRYKM-VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHAN 870
Cdd:cd03294 112 ALLpHRTVLENVAFglevqgVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 871 VVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03294 181 ILLMDEAFSALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
733-934 |
1.21e-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: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 733 IVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPsPEREtatdldirkrgPVAYASQKPWLL-NATVEENIIF 811
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIM---LDGEDVTNVP-PHLR-----------HINMVFQSYALFpHMTVEENVAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 812 ESPFNK----QRYKMVIEACSLqpdidilphgdqTQIGERG----INLSGGQRQRISVARALYQHANVVFLDDPFSALDI 883
Cdd:TIGR01187 66 GLKMRKvpraEIKPRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 884 HLSDhLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 934
Cdd:TIGR01187 134 KLRD-QMQLELKTIQEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
708-934 |
1.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.07 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllAALgemqkVSGAVFWSSLPDSEIGEDpSPERETATDLDIRK 787
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTI--SKL-----INGLLLPDDNPNSKITVD-GITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RGPVAYASQKPWLLNATVEENIIFESPfNKQ--RYKMVIEACSLQPDIDILPHGDQTQIgergiNLSGGQRQRISVARAL 865
Cdd:PRK13640 85 KVGIVFQNPDNQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 866 YQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKL-IRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
701-934 |
1.58e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.77 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 701 VQIMGGYFTW-TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKS---SLLL---------------AALGEMQK------- 754
Cdd:PTZ00265 1166 IEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKStvmSLLMrfydlkndhhivfknEHTNDMTNeqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 755 ------VSGAVFWSSLPDSEIGEDPSPERETAT---------DLDIRK-RGPVAYASQKPWLLNATVEENIIF-ESPFNK 817
Cdd:PTZ00265 1246 eeqnvgMKNVNEFSLTKEGGSGEDSTVFKNSGKilldgvdicDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFgKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 818 QRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILEL 897
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDI 1404
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1189438336 898 LRDDKRTVVLVTHKLQYLPHADWIIAM----KDGT-IQREGT 934
Cdd:PTZ00265 1405 KDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGT 1446
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
706-932 |
1.68e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 78.31 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 706 GYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgeDPSPERETATDLD- 784
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL--DRKQRRAFRRDVQl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 IRKRGPVAYASQKP--WLLNATVEENIIFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISV 861
Cdd:TIGR02769 93 VFQDSPSAVNPRMTvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 932
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
720-942 |
1.70e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSpeRETAtdldiRKRGPVAYasqkpw 799
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW---LDGEHIQHYAS--KEVA-----RRIGLLAQ------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 800 llNATVEENIIFESPFNKQRYKMvieacslQP--------DIDILPHGDQ----TQIGERGIN-LSGGQRQRISVARALY 866
Cdd:PRK10253 89 --NATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 867 QHANVVFLDDPFSALDIhlsDHlmQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:PRK10253 160 QETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
.
gi 1189438336 942 E 942
Cdd:PRK10253 235 E 235
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
720-941 |
1.70e-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: 81.86 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLLlaalGEMQKVSGAVFWSSLPDseiGEDPSpereTATDLDIRKrgPVAYASQKPW 799
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLI----NLLQRVYDPTVGQILID---GIDIN----TVTRESLRK--SIATVFQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 800 LLNATVEENIIF--ESPFNKQRYKMViEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDP 877
Cdd:TIGR01192 420 LFNRSIRENIRLgrEGATDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 878 FSALDIHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:TIGR01192 499 TSALDVETEARVKNA--IDALRKN-RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1362-1592 |
1.89e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.49 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1362 DQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRS 1441
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDP-VLFSGT-----IRFNLdpERKCSDSTLWEALeIAQLKLVVkalpgGLDAIITEGGENFSQGQRQLFCLAR 1515
Cdd:PRK13632 84 KIGIIFQNPdNQFIGAtveddIAFGL--ENKKVPPKKMKDI-IDDLAKKV-----GMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1516 AFVRKTSIFIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
711-937 |
2.72e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.59 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVFWSsLPDSEIGEDPSPERETATDL----- 783
Cdd:PRK13651 16 LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNAL--LLPDTGTIEWI-FKDEKNKKKTKEKEKVLEKLviqkt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 784 ---------DIRKRGPVAYASQKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLqpDIDILPHGDqtqige 846
Cdd:PRK13651 93 rfkkikkikEIRRRVGVVFQFAEYQLFEQTIEKDIIF-GPVSmgvskeeaKKRAAKYIELVGL--DESYLQRSP------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 847 rgINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMK 925
Cdd:PRK13651 164 --FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFK 239
|
250
....*....|....*.
gi 1189438336 926 DGTIQREG----TLKD 937
Cdd:PRK13651 240 DGKIIKDGdtydILSD 255
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
714-938 |
2.91e-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: 76.70 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGED----PSPEREtatdldirKRG 789
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-------GRDitglPPHERA--------RAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 pVAYASQKPWLL-NATVEENIIF-ESPFNKQRYKMVIE-ACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVARALY 866
Cdd:cd03224 77 -IGYVPEGRRIFpELTVEENLLLgAYARRRAKRKARLErVYELFPRL-------KERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 938
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEA--IRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
712-933 |
3.37e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 76.63 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFW-----SSLPDSEIgedpsperetatdLDIR 786
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlSRLKRREI-------------PYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 KR-GPVAyasQKPWLL-NATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 857
Cdd:COG2884 79 RRiGVVF---QDFRLLpDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 858 RISVARALyqhAN---VVFLDDPFSALDIHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPHADW-IIAMKDGTIQ 930
Cdd:COG2884 145 RVAIARAL---VNrpeLLLADEPTGNLDPETSW-----EIMELLEEINRrgtTVLIATHDLELVDRMPKrVLELEDGRLV 216
|
...
gi 1189438336 931 REG 933
Cdd:COG2884 217 RDE 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
712-934 |
5.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSeigeDPSPEREtatdldIRKRGPV 791
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG----DFSKLQG------IRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPWLLNATVEENIIFeSPFNkqrykmvieACslQPDIDILPHGDQTqIGERGI---------NLSGGQRQRISVA 862
Cdd:PRK13644 82 VFQNPETQFVGRTVEEDLAF-GPEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1366-1590 |
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 1189438336 1366 IQIQNLSVRYDSSLK---PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD------TFEGHIIIDGIDIAklpL 1436
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRptsgsiLFDGKDLTKLSRRS---L 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1437 HTLRSRLSIILQDPvlFSGtirfnLDPERKCSDStLWEALEIAQL-------KLVVKAL------PGGLDAIITEggenF 1503
Cdd:COG1123 338 RELRRRVQMVFQDP--YSS-----LNPRMTVGDI-IAEPLRLHGLlsraerrERVAELLervglpPDLADRYPHE----L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1504 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSV----QAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDG 481
|
250
....*....|....
gi 1189438336 1577 AILEFDKPEKLLSR 1590
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
718-937 |
9.21e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 75.45 E-value: 9.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRGpVAYASQK 797
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN-------GKD-------ITNLPPEKRD-ISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLL-NATVEENIIF----ESPFNKQRYKMVIE-ACSLqpDIDILPHGDQTqigergiNLSGGQRQRISVARALYQHANV 871
Cdd:cd03299 80 YALFpHMTVYKNIAYglkkRKVDKKEIERKVLEiAEML--GIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 872 VFLDDPFSALDIHLSDHLMqagilELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLR-----EELKKIRKefgvTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1104-1336 |
1.39e-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: 76.31 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1104 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV-- 1181
Cdd:cd18552 60 TYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdw 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1182 --TPVFLVALLPLAIVCYFIQKYFRVASRDLQ-QLDDttqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSN--- 1255
Cdd:cd18552 140 klTLIALVVLPLAALPIRRIGKRLRKISRRSQeSMGD-----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLrrl 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1256 NIASLFLTAANRWLevrMEYIGACVVLIAAVTSISNSLHRELSAG-LVGLgLTYALMVSNYLnwmvRNLADM--ELQ--L 1330
Cdd:cd18552 215 SMKIARARALSSPL---MELLGAIAIALVLWYGGYQVISGELTPGeFISF-ITALLLLYQPI----KRLSNVnaNLQrgL 286
|
....*.
gi 1189438336 1331 GAVKRI 1336
Cdd:cd18552 287 AAAERI 292
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
709-933 |
3.03e-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: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 709 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERetatdldirkr 788
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI---KVNDQSHTGLAPYQR----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 gPVAYASQKPWLL-NATVEENIIFE-SPFNK----QRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRIS 860
Cdd:TIGR01277 71 -PVSMLFQENNLFaHLTVRQNIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRVA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 861 VARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:TIGR01277 139 LARCLVRPNPILLLDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1366-1589 |
3.66e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.64 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSL------------AFFRMVDTFEghiiidgidIAK 1433
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALhlngllrpqkgkVLVSGIDTGD---------FSK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPlhTLRSRLSIILQDP-VLFSG-TIRFNL--DPERKCSDSTlwealEIAqlKLVVKALPG-GLDAIITEGGENFSQGQR 1508
Cdd:PRK13644 72 LQ--GIRKLVGIVFQNPeTQFVGrTVEEDLafGPENLCLPPI-----EIR--KRVDRALAEiGLEKYRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKL 1587
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
..
gi 1189438336 1588 LS 1589
Cdd:PRK13644 223 LS 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
713-910 |
3.83e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSPERetatdldirkrgPVA 792
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM---LDGVDLSHVPPYQR------------PIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLL-NATVEENIIFESPFNK-------QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 864
Cdd:PRK11607 95 MMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438336 865 LYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH 910
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDR-MQLEVVDILERVGVTCVMVTH 208
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1085-1336 |
4.73e-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: 74.51 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1085 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1164
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1165 SRSTLLCVSALAVISYVTPV-FLVALLPLAIVCYFIQKYF---RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1240
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWKlTLVALLLLPLYVLILRYFRrriRKASREVRESLAE----LSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1241 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGlvglGLTYALMVSNYLNWMV 1320
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG----ELVAFLAYLGMLFGPI 272
|
250 260
....*....|....*....|
gi 1189438336 1321 RNLADMELQ----LGAVKRI 1336
Cdd:cd07346 273 QRLANLYNQlqqaLASLERI 292
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
713-913 |
4.99e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.97 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDseigEDPSPEREtatdldirkrgpVA 792
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAERG------------VV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQK--PWLlnaTVEENIIFespfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHA 869
Cdd:PRK11248 76 FQNEGllPWR---NVQDNVAF-----GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438336 870 NVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
710-914 |
5.35e-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: 72.20 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 710 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFwsslpdseIGEDPSPEREtatdldIRK 787
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLnaLAGRRTGLGVSGEVL--------INGRPLDKRS------FRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 RgpVAYASQKPWLL-NATVEENIIFespfnkqrykmvieACSLQpdidilphgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:cd03213 83 I--IGYVPQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY 914
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSS 173
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
711-910 |
6.38e-14 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 74.70 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALG---EMQKVSGAVFW-----SSLPDSEIgedpsperetat 781
Cdd:COG0444 13 TRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFdgedlLKLSEKEL------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 782 dLDIRKRGpVAYASQKPwlLNA-----TVEEniIFESPFN-------KQRYKMVIEA---CSLQPDIDIL---PHgdqtq 843
Cdd:COG0444 81 -RKIRGRE-IQMIFQDP--MTSlnpvmTVGD--QIAEPLRihgglskAEARERAIELlerVGLPDPERRLdryPH----- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 844 igergiNLSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTH 910
Cdd:COG0444 150 ------ELSGGMRQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITH 209
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
708-938 |
7.85e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 7.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQ---KVSGAVfwsslpdsEIGEDPSPERETATD 782
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELEsevRVEGRV--------EFFNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 783 ldiRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKM----VIEACSLQPDI-DILPHgdqtQIGERGINLSGGQRQ 857
Cdd:PRK14258 85 ---RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLwDEIKH----KIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 858 RISVARALYQHANVVFLDDPFSALDIHLS---DHLMQAGILEllrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQ 233
|
....
gi 1189438336 935 LKDF 938
Cdd:PRK14258 234 LVEF 237
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1366-1590 |
1.12e-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: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSL--KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPvlfsgtiRFNLDPeRKCSDSTLWEALEIAQLKLVVKALPGGLDAIiteG-GENF--------SQGQRQLFCLA 1514
Cdd:COG1124 82 QMVFQDP-------YASLHP-RHTVDRILAEPLRIHGLPDREERIAELLEQV---GlPPSFldryphqlSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1515 RAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQaeilNLLKD--LREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
.
gi 1189438336 1590 R 1590
Cdd:COG1124 229 G 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
721-941 |
1.20e-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: 74.38 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 721 ITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFWSSLPDSEIGEDPSPERetatdldiRKrgpVAYASQKP 798
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIrlIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEK--------RR---IGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 799 WLL-NATVEENIIF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHANVV 872
Cdd:TIGR02142 85 RLFpHLSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 873 FLDDPFSALDIHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1366-1575 |
1.46e-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: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSS--LKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKlPLHTLRSRL 1443
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLERPTSGEVLVDGE-PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFS-GTIRFN--LDPERKCSDSTlwEALEIAQ--LKLVvkalpgGLdaiitEGGENF-----SQGQRQLFCL 1513
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGLELQGVPKA--EARERAEelLELV------GL-----SGFENAyphqlSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1514 ARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILSADLVIVLKR 1575
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
721-924 |
1.83e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 721 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssLPDSEIGEDPSPERETATDLDIRKRGPVAyaSQKPWL 800
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW--LGKDLLGMKDDEWRAVRSDIQMIFQDPLA--SLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 801 lnaTVEEnIIFEsPFN-----------KQRYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVARALYQH 868
Cdd:PRK15079 116 ---TIGE-IIAE-PLRtyhpklsrqevKDRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 869 ANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 924
Cdd:PRK15079 180 PKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
713-934 |
1.91e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGemqkvsgavfWSSLPDSEIGEDPSPeRETATDLDIRKRgpVA 792
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG----------YYPLTEGEIRLDGRP-LSSLSHSVLRQG--VA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 872
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 873 FLDDPFSALDIHLSDHLMQAgiLELLRdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQA--LAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
718-929 |
2.16e-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: 71.02 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVfwsslpdsEIGEDPSPERETATDLdIRKRgpVAYAS 795
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTI--------IIDGLKLTDDKKNINE-LRQK--VGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLL-NATVEENIIfESP---FNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHANV 871
Cdd:cd03262 83 QQFNLFpHLTVLENIT-LAPikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 872 VFLDDPFSALDIHlsdhlMQAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:cd03262 157 MLFDEPTSALDPE-----LVGEVLDVMKDlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
707-937 |
2.75e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.95 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvSGAVFwssLPDSEIgedpspERETATDLd 784
Cdd:PRK13632 14 SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIskILTGLLKPQ--SGEIK---IDGITI------SKENLKEI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 irkRGPVAYASQKP--WLLNATVEENIIFeSPFNKQ--RYKM--VIEACSLQPDI-DILPHGDQtqigergiNLSGGQRQ 857
Cdd:PRK13632 82 ---RKKIGIIFQNPdnQFIGATVEDDIAF-GLENKKvpPKKMkdIIDDLAKKVGMeDYLDKEPQ--------NLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 858 RISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI-MVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
709-912 |
3.22e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 709 TWTpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwsslpdsEIGEDPSPERETAtdldirKR 788
Cdd:PRK15056 15 TWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG----------KISILGQPTRQAL------QK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 GPVAYASQKP---WLLNATVEENII---------FESPfnKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQR 856
Cdd:PRK15056 78 NLVAYVPQSEevdWSFPVLVEDVVMmgryghmgwLRRA--KKRDRQIVTAALARVDMVEFRH---RQIGE----LSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKL 912
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNL 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1366-1589 |
4.45e-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: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKL----------- 1434
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTL----LRAL--------------AGLlkpssgevlld 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1435 --PLHTLRSR-----LSIILQDPVL-FSGTIR--------------FNLDPE-RKCSDSTLwEALEIAQLKlvvkalpgg 1491
Cdd:COG1120 62 grDLASLSRRelarrIAYVPQEPPApFGLTVRelvalgryphlglfGRPSAEdREAVEEAL-ERTGLEHLA--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1492 lDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA----TENILQKvvMTAFADRTVVTIAHRV-HTILS 1566
Cdd:COG1120 132 -DRPVDE----LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARY 204
|
250 260
....*....|....*....|...
gi 1189438336 1567 ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:COG1120 205 ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
713-937 |
4.46e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.67 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRgPVA 792
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-------GQD-------ITHVPAENR-HVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLL-NATVEENIIF-----ESPfNKQRYKMVIEA---CSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:PRK09452 90 TVFQSYALFpHMTVFENVAFglrmqKTP-AAEITPRVMEAlrmVQLEEFAQRKPH-----------QLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 864 ALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQ-MQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
711-945 |
4.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.73 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIgEDPSPERETATdldIRKRGP 790
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV---TVDDITI-THKTKDKYIRP---VRKRIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLLNATVEENIIFeSPFNkqrYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARALYQHA 869
Cdd:PRK13646 89 MVFQFPESQLFEDTVEREIIF-GPKN---FKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 870 NVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSECQL 945
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRL-LKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
714-942 |
4.59e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqKV-SGAVfwssLPDS-EI---GEdpspERETATDLDIRKR 788
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLM--------KIlSGVY----QPDSgEIlldGE----PVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 GpVAYASQKPWLL-NATVEENIIFESPFNK----QRYKMVIEACSL--QPDIDILPHgdqTQIGErginLSGGQRQRISV 861
Cdd:COG1129 80 G-IAIIHQELNLVpNLSVAENIFLGREPRRggliDWRAMRRRARELlaRLGLDIDPD---TPVGD----LSVAQQQLVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQR 940
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAELTE 229
|
..
gi 1189438336 941 SE 942
Cdd:COG1129 230 DE 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
707-948 |
4.87e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.20 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdsEIGEDPSPEretATDLDIR 786
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--------TVGGMVLSE---ETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 KRgpVAYASQKP--WLLNATVEENIIF--EspfNKQ--RYKMV------IEACSLQPDIDILPHgdqtqigergiNLSGG 854
Cdd:PRK13635 81 RQ--VGMVFQNPdnQFVGATVQDDVAFglE---NIGvpREEMVervdqaLRQVGMEDFLNREPH-----------RLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 855 QRQRISVARALYQHANVVFLDDPFSALDihlsdhlmQAG---ILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDG 927
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLD--------PRGrreVLETVRQLKEqkgiTVLSITHDLDEAAQADRVIVMNKG 216
|
250 260
....*....|....*....|.
gi 1189438336 928 TIQREGTLKdfqrsecQLFEH 948
Cdd:PRK13635 217 EILEEGTPE-------EIFKS 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
714-933 |
4.90e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.95 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseIGEDPSPERETATdldIRKRgpVAY 793
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL--------VAGDDVEALSARA---ASRR--VAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWL-LNATVEENIIFESPFNKQRYKMVIEACSLQPDiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHANV 871
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 872 VFLDDPFSALDIHlsdHLMQAgiLELLR---DDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 933
Cdd:PRK09536 161 LLLDEPTASLDIN---HQVRT--LELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAG 221
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1086-1336 |
5.38e-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: 71.44 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1086 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1165
Cdd:cd18557 39 ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1166 RSTLLCVSA---LAVISY-VTPVFLVALLPLAIVCYFIQKYFRVASRDLQQlddttQLPLLSHFA-ETVEGLTTIRAF-- 1238
Cdd:cd18557 119 RNILQVIGGliiLFILSWkLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQD-----ALAKAGQVAeESLSNIRTVRSFsa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 -RYE-ARFQQKLLEYTDSnNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSlhrELSAGLVGLGLTYALMVSNYL 1316
Cdd:cd18557 194 eEKEiRRYSEALDRSYRL-ARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSG---QLTVGELTSFILYTIMVASSV 269
|
250 260
....*....|....*....|
gi 1189438336 1317 NWMVRNLADMELQLGAVKRI 1336
Cdd:cd18557 270 GGLSSLLADIMKALGASERV 289
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
718-940 |
6.35e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.04 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSpeRETATDldiRKRGPV--AYAs 795
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-------GTDVS--RLHARD---RKVGFVfqHYA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 qkpWLLNATVEENIIF--------ESPFN---KQRYKMVIEACSLQPDIDILPhgdqTQigerginLSGGQRQRISVARA 864
Cdd:PRK10851 85 ---LFRHMTVFDNIAFgltvlprrERPNAaaiKAKVTQLLEMVQLAHLADRYP----AQ-------LSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 865 LYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQR 940
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKEL-RRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
840-933 |
6.68e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.38 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 840 DQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-A 918
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvS 219
|
90
....*....|....*
gi 1189438336 919 DWIIAMKDGTIQREG 933
Cdd:PRK10619 220 SHVIFLHQGKIEEEG 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1361-1576 |
7.25e-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: 7.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1361 PDQGKIQIQNLSVRyDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKLPLH--- 1437
Cdd:COG4178 358 SEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LRAI--------------AGLWPYgsg 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 --TLRSRLSIIL--QDPVLFSGTIRFNL---DPERKCSDSTLWEALEIAQLKlvvkALPGGLDAIiTEGGENFSQGQRQL 1510
Cdd:COG4178 419 riARPAGARVLFlpQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLG----HLAERLDEE-ADWDQVLSLGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRG 1576
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
718-951 |
8.08e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFwssLPDSEIGEDPSPEretatdldIRKRGPVA 792
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVY---LDGQDIFKMDVIE--------LRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPwLLNATVEENIIFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVAR 863
Cdd:PRK14247 88 FQIPNP-IPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 864 ALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDdkRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKD-F 938
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD--MTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREvF 233
|
250
....*....|...
gi 1189438336 939 QRSECQLFEHWKT 951
Cdd:PRK14247 234 TNPRHELTEKYVT 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1350-1585 |
8.15e-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: 72.79 E-value: 8.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1350 LLA--PSLIPKNWPDQGK--IQIQNLSVRYD---SSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRM 1416
Cdd:COG4172 256 LLAaePRGDPRPVPPDAPplLEARDLKVWFPikrGLFRRTVGHVKAVdgvsltLRRGETLGLVGESGSGKSTLGLALLRL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1417 VDT-----FEGHIIIDGIDIAKLPlhtLRSRLSIILQDPvlFSgtirfNLDPERKCSDsTLWEALEIAQLKL-------- 1483
Cdd:COG4172 336 IPSegeirFDGQDLDGLSRRALRP---LRRRMQVVFQDP--FG-----SLSPRMTVGQ-IIAEGLRVHGPGLsaaerrar 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1484 VVKAL------PGGLDAIITEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATenilQKVVMTAFA------- 1550
Cdd:COG4172 405 VAEALeevgldPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV----QAQILDLLRdlqrehg 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1551 --------DRTVV-TIAHRvhtilsadlVIVLKRGAILE-------FDKPE 1585
Cdd:COG4172 477 laylfishDLAVVrALAHR---------VMVMKDGKVVEqgpteqvFDAPQ 518
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
718-911 |
9.07e-13 |
|
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: 69.61 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQK---VSGAVFWSslpdseiGEDPSPERetatdldIRKRgpVAYA 794
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFN-------GQPRKPDQ-------FQKC--VAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 SQKPWLL-NATVEENIIFESPF-------NKQRYKMVieacslqpDIDILPHGDQTQIGERGI-NLSGGQRQRISVARAL 865
Cdd:cd03234 87 RQDDILLpGLTVRETLTYTAILrlprkssDAIRKKRV--------EDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438336 866 YQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHK 911
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1366-1589 |
9.51e-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: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLrsrLSI 1445
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKS------------------------------TL---LKA 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 IL--QDPVlfSGTIRFNLDPERKCSDStlwealeIA---QLKLVVKALP--------GGLD--------------AIITE 1498
Cdd:COG1121 52 ILglLPPT--SGTVRLFGKPPRRARRR-------IGyvpQRAEVDWDFPitvrdvvlMGRYgrrglfrrpsradrEAVDE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1499 -----GGENF--------SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTI 1564
Cdd:COG1121 123 alervGLEDLadrpigelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAV 202
|
250 260
....*....|....*....|....*.
gi 1189438336 1565 LS-ADLVIVLKRGaILEFDKPEKLLS 1589
Cdd:COG1121 203 REyFDRVLLLNRG-LVAHGPPEEVLT 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
718-913 |
9.69e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.07 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFwssLPDSEI---GEDPsperetatdLDIRKRg 789
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLrclnrMNDLIPGARVEGEIL---LDGEDIydpDVDV---------VELRRR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 pVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEA--------CSLQPDI-DILphgdqtqiGERGINLSGGQRQRIS 860
Cdd:COG1117 94 -VGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVkDRL--------KKSALGLSGGQQQRLC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 861 VARALYQHANVVFLDDPFSALDIHLSdhlmqAGILELLRD--DKRTVVLVTHKLQ 913
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPIST-----AKIEELILElkKDYTIVIVTHNMQ 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
718-910 |
1.20e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVfwsSLPDSEIgEDPSPeretatdldirkRGPVAYAS 795
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLrlIAGL--LPPAAGTI---KLDGGDI-DDPDV------------AEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 Q----KPWLlnaTVEENIIFESPFNKQRYKMV---IEACSLQPDIDiLPHGdqtqigergiNLSGGQRQRISVARALYQH 868
Cdd:PRK13539 80 HrnamKPAL---TVAENLEFWAAFLGGEELDIaaaLEAVGLAPLAH-LPFG----------YLSAGQKRRVALARLLVSN 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1189438336 869 ANVVFLDDPFSALDIH--------LSDHLMQAGIlellrddkrtVVLVTH 910
Cdd:PRK13539 146 RPIWILDEPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1363-1591 |
1.42e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.56 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1363 QGKIQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTF-----EGHIIIDGIDIAKLPLH 1437
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 TLRSRLSIILQDP------VLFSGT---IRFN-LDPERKCSDSTLWEALEIAQLKLVVKalpGGLDAiiteGGENFSQGQ 1507
Cdd:PRK14247 79 ELRRRVQMVFQIPnpipnlSIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVK---DRLDA----PAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1508 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtilsADLVIVLKRGAILE- 1580
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEw 226
|
250
....*....|....*..
gi 1189438336 1581 ------FDKPEKLLSRK 1591
Cdd:PRK14247 227 gptrevFTNPRHELTEK 243
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
713-910 |
1.53e-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: 68.15 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEigEDPSPEREtatdldirkrgpVA 792
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE--QRDEPHEN------------IL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLLNA-TVEENIIFESPFNKQRYKMVIEACslqpdidilphgdqTQIGERGIN------LSGGQRQRISVARAL 865
Cdd:TIGR01189 77 YLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARLW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 866 YQHANVVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTH 910
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
717-913 |
1.53e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.42 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 717 TLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQ------KVSGAVFWSslpdseiGEDP-SPERETatdLDIRKRg 789
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLL-RSINRMNdlnpevTITGSIVYN-------GHNIySPRTDT---VDLRKE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 pVAYASQKPWLLNATVEENIIFESPFN----KQRYKMVIEACSLQPDI-----DILpHgdqtqigERGINLSGGQRQRIS 860
Cdd:PRK14239 88 -IGMVFQQPNPFPMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdevkDRL-H-------DSALGLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 861 VARALYQHANVVFLDDPFSALDiHLSDHLMQAGILELlrDDKRTVVLVTHKLQ 913
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQ 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1367-1579 |
1.92e-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: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLRSRLSII 1446
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKS------------------------------TLLKTLAGL 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1447 LQdpvLFSGTIRFNLDPERKcsdstlWEALEIAQLKLVV----KALpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03214 49 LK---PSSGEILLDGKDLAS------LSPKELARKIAYVpqalELL--GLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1523 IFIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILSADLVIVLKRGAIL 1579
Cdd:cd03214 118 ILLLDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1366-1587 |
2.63e-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: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLA----------FFRMVDTFEGHIIIdgidiak 1433
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLlrLIVgllrpdsgevLIDGEDISGLSEAE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 lpLHTLRSRLSIILQDPVLFSG-TIR----FNLDPERKCSDSTLweaLEIAQLKLVVKALPGGLDAIITEggenFSQGQR 1508
Cdd:cd03261 72 --LYRLRRRMGMLFQSGALFDSlTVFenvaFPLREHTRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE----LSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPE 1585
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
..
gi 1189438336 1586 KL 1587
Cdd:cd03261 223 EL 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
716-937 |
3.31e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.96 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLpdseigeDPSPERETatdLDIRKRGPVAYAS 795
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL-------DTSDEENL---WDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQ 867
Cdd:PRK13633 94 PDNQIVATIVEEDVAF-GPENlgippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 868 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
695-934 |
4.31e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.26 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 695 DADNCCVQImggyftwtpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPS 774
Cdd:PRK13548 4 EARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV---RLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 775 PEREtatdldiRKRgpvAYASQK-----PWllnaTVEENI---IFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQige 846
Cdd:PRK13548 72 AELA-------RRR---AVLPQHsslsfPF----TVEEVVamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQ--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 847 rginLSGGQRQRISVARALYQHAN------VVFLDDPFSALDIHlsdHlmQAGILELLRD----DKRTVVLVTHKL---- 912
Cdd:PRK13548 135 ----LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLA---H--QHHVLRLARQlaheRGLAVIVVLHDLnlaa 205
|
250 260
....*....|....*....|..
gi 1189438336 913 QYlphADWIIAMKDGTIQREGT 934
Cdd:PRK13548 206 RY---ADRIVLLHQGRLVADGT 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1367-1578 |
5.10e-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: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRM-----------VDTFEGHIIIDGIDIAKLP 1435
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTL----LKAilgllkptsgsIRVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 LHTLRSRLS-IILQDPVLFSGTIRFNLDPERKCSDstlWEALEIAqLKLVvkalpgGLDAI----ITEggenFSQGQRQL 1510
Cdd:cd03235 75 QRRSIDRDFpISVRDVVLMGLYGHKGLFRRLSKAD---KAKVDEA-LERV------GLSELadrqIGE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-SADLVIVLKRGAI 1578
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLeYFDRVLLLNRTVV 210
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
716-929 |
5.22e-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: 68.01 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsPERETATDLDIrkrgpvayAS 795
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-----PLHTLRSRLSI--------IL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLD 875
Cdd:cd03288 102 QDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 876 DPFSALDIhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03288 182 EATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1366-1590 |
5.52e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.29 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTL---RSR 1442
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVwdiREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDP-VLFSGT-----IRFNLDpERKCSDSTLwealeiaqLKLVVKALP--GGLDAIITEGgENFSQGQRQLFCLA 1514
Cdd:PRK13640 86 VGIVFQNPdNQFVGAtvgddVAFGLE-NRAVPRPEM--------IKIVRDVLAdvGMLDYIDSEP-ANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1515 RAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
707-934 |
6.10e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIgedPSPERETATDLDIR 786
Cdd:PRK13645 16 YAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI---VGDYAI---PANLKKIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 KRGPVAYASQKPWLLNATVEENIIFeSPFN-----KQRYKMVIEACSLQPdidiLPhgdQTQIGERGINLSGGQRQRISV 861
Cdd:PRK13645 90 KEIGLVFQFPEYQLFQETIEKDIAF-GPVNlgenkQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
712-933 |
7.53e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.84 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLL--AALGEMQKVSGAVFwsslpdseiGEDPSPERETatdlDIRKRg 789
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLhlNGIYLPQRGRVKVM---------GREVNAENEK----WVRSK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 pVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 859
Cdd:PRK13647 81 -VGLVFQDPddQVFSSTVWDDVAF-GPVNmgldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 860 SVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 933
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1079-1248 |
7.58e-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: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 TLDQTVYAM--VFTV--LCSLGIVLCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID 1154
Cdd:cd18573 39 SLKTFALALlgVFVVgaAANFGRVYLLRIA------GERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1155 QHIPSTLECLSRSTLLCVSALAVISYVTP-VFLVALL---PLAIVCYFIQKYFRVASRDLQQ-LDDTTQLPllshfAETV 1229
Cdd:cd18573 113 KSLTQNLSDGLRSLVSGVGGIGMMLYISPkLTLVMLLvvpPIAVGAVFYGRYVRKLSKQVQDaLADATKVA-----EERL 187
|
170 180
....*....|....*....|...
gi 1189438336 1230 EGLTTIRAF---RYE-ARFQQKL 1248
Cdd:cd18573 188 SNIRTVRAFaaeRKEvERYAKKV 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1366-1582 |
7.67e-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: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEG----HIIIDGIDIAKLPLHtlRS 1441
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLERpdsgEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDPVLFS-----GTIRFNLD----PERKCSDSTLwEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1512
Cdd:cd03259 73 NIGMVFQDYALFPhltvaENIAFGLKlrgvPKAEIRARVR-ELLELVGLEGLLNRYPHEL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFD 1582
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
720-946 |
7.94e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.59 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRGpVAYASQKPW 799
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-------GED-------VTHRSIQQRD-ICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 800 LL-NATVEENIIF-------ESPFNKQRYKmviEACSLqpdIDILPHGDQ--TQIgerginlSGGQRQRISVARALYQHA 869
Cdd:PRK11432 89 LFpHMSLGENVGYglkmlgvPKEERKQRVK---EALEL---VDLAGFEDRyvDQI-------SGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 870 NVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLF 946
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
711-934 |
8.03e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.34 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERETATDL------- 783
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI---QVGDIYIGDKKNNHELITNPYskkiknf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 784 -DIRKRgpVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPD-IDILPHGdqtqigerginL 851
Cdd:PRK13631 112 kELRRR--VSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 852 SGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagileLLRDDK---RTVVLVTHKL-QYLPHADWIIAMKDG 927
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-----LILDAKannKTVFVITHTMeHVLEVADEVIVMDKG 252
|
....*..
gi 1189438336 928 TIQREGT 934
Cdd:PRK13631 253 KILKTGT 259
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1366-1584 |
8.62e-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: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRSR 1442
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDpvlfsgtirFNLDPE----------RKCSDSTLW------------EALEIaqLKLVvkalpgGLDAIITEGG 1500
Cdd:cd03256 80 IGMIFQQ---------FNLIERlsvlenvlsgRLGRRSTWRslfglfpkeekqRALAA--LERV------GLLDKAYQRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILS-ADLVIVL 1573
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGL 218
|
250
....*....|.
gi 1189438336 1574 KRGAILeFDKP 1584
Cdd:cd03256 219 KDGRIV-FDGP 228
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1034-1336 |
9.21e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 67.57 E-value: 9.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1034 LSLLVFSQLLKhmvlVAIDYWLAKWTDSALTltpaarncSLSQEcTLDQTVYAMV-FTVLCSL--GIVLCLVTSVTVewt 1110
Cdd:cd18572 2 FVFLVVAALSE----LAIPHYTGAVIDAVVA--------DGSRE-AFYRAVLLLLlLSVLSGLfsGLRGGCFSYAGT--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 glKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP----VFL 1186
Cdd:cd18572 66 --RLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWrltlLAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1187 VALLPLAIVCYFIQKYFRVASRDLQQ-LDDTTQLpllshfAETVEGL-TTIRAF---RYEA-RFQQKLLEYTDSN---NI 1257
Cdd:cd18572 144 ITVPVIALITKVYGRYYRKLSKEIQDaLAEANQV------AEEALSNiRTVRSFateEREArRYERALDKALKLSvrqAL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1258 ASLFLTAANRWLevrmEYIGACVVLIAAVTSIsnsLHRELSAG-LVGLGLtYALMVSNYLNWMVRNLADMELQLGAVKRI 1336
Cdd:cd18572 218 AYAGYVAVNTLL----QNGTQVLVLFYGGHLV---LSGRMSAGqLVTFML-YQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
718-935 |
1.01e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsperETATDLDIRKRgPVAYASQK 797
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKL--------SSAAKAELRNQ-KLGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLL-NATVEENIIFESPFNKQRYKMVIEACSlqpdiDILPH-GDQTQIGERGINLSGGQRQRISVARALYQHANVVFLD 875
Cdd:PRK11629 96 HHLLpDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 876 DPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 935
Cdd:PRK11629 171 EPTGNLDARNADSIFQL-LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1381-1577 |
1.03e-11 |
|
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: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1381 PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIidgidiaklplHTlrSRLSIILQDPVLFSGTIRFN 1460
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------HS--GRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1461 L------DPERKCSdstlweALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID 1534
Cdd:cd03291 118 IifgvsyDEYRYKS------VVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438336 1535 MATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGA 1577
Cdd:cd03291 192 VFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
718-951 |
1.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAV--FWSSLPDSEIgeDPsperetatdLDIRKRGP 790
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVrlFGRNIYSPDV--DP---------IEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLlNATVEENIIFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISV 861
Cdd:PRK14267 89 MVFQYPNPFP-HLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 862 ARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKR--TVVLVTHK-LQYLPHADWIIAMKDGTIQREG-TLKD 937
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANI-----DPVGTAKIEELLFELKKeyTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpTRKV 235
|
250
....*....|....
gi 1189438336 938 FQRSECQLFEHWKT 951
Cdd:PRK14267 236 FENPEHELTEKYVT 249
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1089-1336 |
1.21e-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: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1089 FTVLCSLGIVLCLVTSV---TVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1165
Cdd:cd18575 39 FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1166 RSTLLCVSALAVISYVTP---VFLVALLPLAIV-CYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAFRY 1240
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQdRLADLS-----AFAEETLSAIKTVQAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1241 EARFQQKLLEYTDSNniaslfLTAANRWLEVRMEYIGACVVLI-AAVTSI-----SNSLHRELSAGLVGLGLTYALMVSN 1314
Cdd:cd18575 194 EDAERQRFATAVEAA------FAAALRRIRARALLTALVIFLVfGAIVFVlwlgaHDVLAGRMSAGELSQFVFYAVLAAG 267
|
250 260
....*....|....*....|..
gi 1189438336 1315 YLNWMVRNLADMELQLGAVKRI 1336
Cdd:cd18575 268 SVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
718-956 |
1.21e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.70 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERETATdldIRK-RGPVAYASQ 796
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI---RVGDITIDTARSLSQQKGL---IRQlRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 797 KPWLL-NATVEENIIfESPF---NKQRYKMVIEACSLQPDIDIlpHGDQTQIGERginLSGGQRQRISVARALYQHANVV 872
Cdd:PRK11264 93 NFNLFpHRTVLENII-EGPVivkGEPKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 873 FLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKdfqrsecQLFEHWKT 951
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK-------ALFADPQQ 237
|
....*
gi 1189438336 952 LMNRQ 956
Cdd:PRK11264 238 PRTRQ 242
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
707-937 |
1.45e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.99 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDldIR 786
Cdd:PRK13637 12 YMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-------GVDITDKKVKLSD--IR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 KRgpVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDI--DILPhgdqtqigergINLSGG 854
Cdd:PRK13637 83 KK--VGLVFQYPeyQLFEETIEKDIAF-GPINlglseeeiENRVKRAMNIVGLDYEDykDKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 855 QRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227
|
....
gi 1189438336 934 TLKD 937
Cdd:PRK13637 228 TPRE 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
711-939 |
1.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLpdseIGEDPSPERETATdldIRKRGP 790
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDI----VVSSTSKQKEIKP---VRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLLnatvEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARALYQHA 869
Cdd:PRK13643 88 VVFQFPESQLF----EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 870 NVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQ 939
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDvFQ 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1366-1576 |
1.69e-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: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLlrCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSG-TIRFNLdperkcsdstlwealeiaqlklvvkALPggldaiiteggenFSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------------------ALG-------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1523 IFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
718-924 |
1.88e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 67.45 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRGPVA----- 792
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD-------GQD-------ITGLSGRELRPLRrrmqm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 -----YASqkpwlLNA--TVEEnIIFEsPF-------NKQRYKMV---IEACSLQPD-IDILPHgdqtqigErginLSGG 854
Cdd:COG4608 100 vfqdpYAS-----LNPrmTVGD-IIAE-PLrihglasKAERRERVaelLELVGLRPEhADRYPH-------E----FSGG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 855 QRQRISVARALYQHANVVFLDDPFSALDihLSdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 924
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALD--VS---IQAQVLNLLEDLQDelglTYLFISHDLSVVRHiSDRVAVM 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1366-1576 |
2.22e-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: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdtfeghiiidgidiaklplhTLRSRLSI 1445
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTT-----------------------------LIKIILGL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDpvlfSGTIR-FNLDPERkcsdstlwealEIAQLKLVVKALPGGlDAIITE--GGEN--FSQGQRQLFCLARAFVRK 1520
Cdd:cd03230 50 LKPD----SGEIKvLGKDIKK-----------EPEEVKRRIGYLPEE-PSLYENltVRENlkLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1521 TSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
378-610 |
2.38e-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: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 378 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYIL 456
Cdd:cd07346 61 YLAARLGQRVVFDLRRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIGALVILFYLN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 457 GVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWE----NIFRTRVETTRRKEMTS 532
Cdd:cd07346 139 WKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 533 LRAFAIYTSISIFMNTaipIAAVLITFVGHVSFFKEaDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd07346 219 ARLSALFSPLIGLLTA---LGTALVLLYGGYLVLQG-SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
713-910 |
3.84e-11 |
|
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: 64.05 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEigEDPSPEREtatdldirkrgpVA 792
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--QRDSIARG------------LL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLLNA-TVEENIIFESPFNKQrykmviEACslqpdIDILPHGDQTQIGERGIN-LSGGQRQRISVARALYQHAN 870
Cdd:cd03231 77 YLGHAPGIKTTlSVLENLRFWHADHSD------EQV-----EEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRP 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1189438336 871 VVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTH 910
Cdd:cd03231 146 LWILDEPTTALDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1280-1580 |
3.98e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1280 VVLIAAVTSISNSLHRELSAGLvglgltyaLMVSNYLNwMVRNLAD--MELQLGAV---KRIHGLLKTEAESY-EGLLA- 1352
Cdd:PRK15134 189 VSVQAQILQLLRELQQELNMGL--------LFITHNLS-IVRKLADrvAVMQNGRCveqNRAATLFSAPTHPYtQKLLNs 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1353 -PSLIPKNWPDQGK--IQIQNLSV---------RYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDT- 1419
Cdd:PRK15134 260 ePSGDPVPLPEPASplLDVEQLQVafpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSq 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1420 ----FEGHIIIDGIDIAKLPlhtLRSRLSIILQDPvlfsgtiRFNLDPeRKCSDSTLWEALEIAQLKL--------VVKA 1487
Cdd:PRK15134 340 geiwFDGQPLHNLNRRQLLP---VRHRIQVVFQDP-------NSSLNP-RLNVLQIIEEGLRVHQPTLsaaqreqqVIAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1488 LPG-GLDAII-----TEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASID-------MATENILQKVVMTAFadrtv 1554
Cdd:PRK15134 409 MEEvGLDPETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY----- 479
|
330 340
....*....|....*....|....*..
gi 1189438336 1555 VTIAHRVHTILS-ADLVIVLKRGAILE 1580
Cdd:PRK15134 480 LFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1366-1590 |
4.42e-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: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLK--PVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFE-------GHIIIDGIDIAKLPL 1436
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsgsvLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1437 HTLRSRLSIILQDPVLFS-----GTIRFNLD---PERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQR 1508
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKP 1584
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 1189438336 1585 EKLLSR 1590
Cdd:cd03258 226 EEVFAN 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1366-1560 |
6.30e-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: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKL-PLHT------ 1438
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRAL--------------AGLwPWGSgrigmp 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDPVLFSGTIRfnldperkcsdstlwealeiaqlklvvkalpgglDAIITEGGENFSQGQRQLFCLARAFV 1518
Cdd:cd03223 62 EGEDLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438336 1519 RKTSIFIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1560
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1366-1534 |
6.65e-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: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHII---IDGIDIAKLPLHTLRSR 1442
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILAGLLPPSAgevLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDPVLFSG-TIRFNLD-----PERKCSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLFCLARA 1516
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAV-----------GLAGLADLPVRQLSAGQKRRVALARL 145
|
170
....*....|....*...
gi 1189438336 1517 FVRKTSIFIMDEATASID 1534
Cdd:COG4133 146 LLSPAPLWLLDEPFTALD 163
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
720-933 |
7.05e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.82 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMqkVSGAVFwsslpdseIGEdpsperETATDLDIRKRGpVAYASQK 797
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLrmIAGLEDI--TSGDLF--------IGE------KRMNDVPPAERG-VGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 ----PWLlnaTVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARALY 866
Cdd:PRK11000 84 yalyPHL---SVAENMSFglklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 933
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
711-911 |
8.69e-11 |
|
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: 66.70 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLAALGEMQKVSGAVfwsslpdseigedpsperetatdLDIRKRGP 790
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGR-----------------------LTKPAKGK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLLNATVEENIIF-ESPFNKQRYKMvieacSLQPDIDILPHGDQTQIGERGIN----------LSGGQRQRI 859
Cdd:TIGR00954 517 LFYVPQRPYMTLGTLRDQIIYpDSSEDMKRRGL-----SDKDLEQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 860 SVARALYQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTHK 911
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVD-----VEGYMYRLCREFGITLFSVSHR 638
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
718-938 |
1.09e-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: 63.47 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFwssLPDSEIGEDPsperetaTDLD-IRKRgpVAYA 794
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTIT---VDGEDLTDSK-------KDINkLRRK--VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 SQK----PwllNATVEENIIfESP-----FNKQrykmviEACSLQpdIDILphgDQTQIGERG----INLSGGQRQRISV 861
Cdd:COG1126 83 FQQfnlfP---HLTVLENVT-LAPikvkkMSKA------EAEERA--MELL---ERVGLADKAdaypAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIHLSdhlmqAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELV-----GEVLDVMRDlakEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEE 222
|
.
gi 1189438336 938 F 938
Cdd:COG1126 223 F 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
714-942 |
1.27e-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: 63.22 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSPEretatdldIRKRGpVAY 793
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL---FDGEDITGLPPHE--------IARLG-IGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLL-NATVEENII----------FESPFNKQRYKMVIEACSlqpdiDILphgDQTQIGERG----INLSGGQRQR 858
Cdd:cd03219 80 TFQIPRLFpELTVLENVMvaaqartgsgLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 859 ISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKD 937
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDE 229
|
....*
gi 1189438336 938 FQRSE 942
Cdd:cd03219 230 VRNNP 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
718-924 |
1.53e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.60 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLllAALGEM--QKVSGAVFWSslpdseiGED-PSPERETATDLdiRKR------ 788
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL--ARLLTMieTPTGGELYYQ-------GQDlLKADPEAQKLL--RQKiqivfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 GPvaYASQKP-WLLNATVEENIIFESPFNKQRYKMVIEA----CSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVA 862
Cdd:PRK11308 100 NP--YGSLNPrKKVGQILEEPLLINTSLSAAERREKALAmmakVGLRPEhYDRYPH-----------MFSGGQRQRIAIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 924
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQelglSYVFISHDLSVVEHiADEVMVM 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1361-1600 |
2.01e-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: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1361 PDQGKIQIQNLSVRYDSSLK--PVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKL---- 1434
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLI--------------AGLekpt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1435 ---------PLHTLRSRLSIILQDPVLF-----SGTIRFNLDPERKCSDstlwEALEIAQ--LKLV-----VKALPGGLd 1493
Cdd:COG1116 65 sgevlvdgkPVTGPGPDRGVVFQEPALLpwltvLDNVALGLELRGVPKA----ERRERARelLELVglagfEDAYPHQL- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1494 aiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILSADLV 1570
Cdd:COG1116 140 ----------SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDeAVFLADRV 209
|
250 260 270
....*....|....*....|....*....|....*..
gi 1189438336 1571 IVLKRG-----AILEFD--KPEKLLSRKDSVFASFVR 1600
Cdd:COG1116 210 VVLSARpgrivEEIDVDlpRPRDRELRTSPEFAALRA 246
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
718-937 |
2.40e-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: 62.79 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGA---VFwsslpdseiGEdpspERETATDLDIRKR-GPVAY 793
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLF---------GE----RRGGEDVWELRKRiGLVSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLLNATVEENII---FESPFNKQRY--KMVIEACSLQPDIDILPHGDQTqIGErginLSGGQRQRISVARALYQH 868
Cdd:COG1119 86 ALQLRFPRDETVLDVVLsgfFDSIGLYREPtdEQRERARELLELLGLAHLADRP-FGT----LSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 869 ANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP----HAdwiIAMKDGTIQREGTLKD 937
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLAL-LDKLAAEGAPTLVLVTHHVEEIPpgitHV---LLLKDGRVVAAGPKEE 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1366-1578 |
3.16e-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: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLrsrLSI 1445
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKS------------------------------TL---MKI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 I--LQDPVlfSGTIRFNldpERKCSDSTLWEALE-----IAQLklvvkalpggldaiiteggenfSQGQRQLFCLARAFV 1518
Cdd:cd03216 46 LsgLYKPD--SGEILVD---GKEVSFASPRDARRagiamVYQL----------------------SVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1519 RKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:cd03216 99 RNARLLILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
709-912 |
3.26e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 709 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperETATDLDIRkr 788
Cdd:PRK10771 8 TWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-------GQD-----HTTTPPSRR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 gPVAYASQKPWLLN-ATVEENI-------IFESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 860
Cdd:PRK10771 72 -PVSMLFQENNLFShLTVAQNIglglnpgLKLNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 861 VARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRD--DKR--TVVLVTHKL 912
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDPAL-----RQEMLTLVSQvcQERqlTLLMVSHSL 190
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
718-910 |
3.40e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.56 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAAL-----GEMqKVSGAVFwSSLPDSEIgedpspeREtatdldIRKRgp 790
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLLerptsGSV-LVDGVDL-TALSEREL-------RA------ARRK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLLNA-TVEENIIFesPF------NKQRYKMVIEACSLqpdIDILPHGDQ--TQigerginLSGGQRQRISV 861
Cdd:COG1135 84 IGMIFQHFNLLSSrTVAENVAL--PLeiagvpKAEIRKRVAELLEL---VGLSDKADAypSQ-------LSGGQKQRVGI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 862 ARALyqhAN---VVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTH 910
Cdd:COG1135 152 ARAL---ANnpkVLLCDEATSALDPETTR-----SILDLLKDINRelglTIVLITH 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
719-919 |
4.08e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 719 SNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVFWSSLPdseigedpsperetatdldIRKRGPvAYASQ 796
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLriLAGL--ARPDAGEVLWQGEP-------------------IRRQRD-EYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 797 KPWL--LNA-----TVEENIIFespfnkqrykmvieACSLQPDIDilphGDQT-----QIGERGI------NLSGGQRQR 858
Cdd:PRK13538 76 LLYLghQPGiktelTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQRR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 859 ISVARALYQHANVVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTHklQYLPHAD 919
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH--QDLPVAS 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1366-1559 |
4.51e-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: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdtfeghiiidgidiaklplhtlrsrLSI 1445
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNldperkcsdstlwEALEIAQLklvvkalpggldaiiteggENFSQGQRQLFCLARAFVRKTSIFI 1525
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 1189438336 1526 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1559
Cdd:cd03221 94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
720-937 |
4.51e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 63.20 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLL--LAAL-----GEMQkVSGAVfwssLPDSEIGEDPSPERetatdldirkRgPVA 792
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLraIAGLerpdsGRIR-LGGEV----LQDSARGIFLPPHR----------R-RIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQK----PWLlnaTVEENIIF---ESPFNKQRYKM--VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:COG4148 81 YVFQEarlfPHL---SVRGNLLYgrkRAPRAERRISFdeVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 864 ALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRT-VVLVTHKL---QYLphADWIIAMKDGTIQREGTLKD 937
Cdd:COG4148 147 ALLSSPRLLLMDEPLAALDLARKAEILP--YLERLRDELDIpILYVSHSLdevARL--ADHVVLLEQGRVVASGPLAE 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
713-934 |
5.15e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.05 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVF----------WSSLPdSEIGEdPSPE---- 776
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvLRGMDQYEPTSGRIIyhvalcekcgYVERP-SKVGE-PCPVcggt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 777 -RETATDL---------DIRKRgpVAYASQKPWLL--NATVEENIIfeSPFNKQRYKmviEACSLQPDIDILphgDQTQI 844
Cdd:TIGR03269 89 lEPEEVDFwnlsdklrrRIRKR--IAIMLQRTFALygDDTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 845 GER----GINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDhLMQAGILELLRDDKRTVVLVTHKLQYLPH-AD 919
Cdd:TIGR03269 159 SHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSD 237
|
250
....*....|....*
gi 1189438336 920 WIIAMKDGTIQREGT 934
Cdd:TIGR03269 238 KAIWLENGEIKEEGT 252
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1366-1578 |
5.86e-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: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRSR 1442
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDpvlfsgtirFNLDPERKCSDSTLWeALEIAQL--KLVVKALPGGLDAIITEGGEN-----FSQGQRQLFCLAR 1515
Cdd:cd03292 80 IGVVFQD---------FRLLPDRNVYENVAF-ALEVTGVppREIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1516 AFVRKTSIFIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRvhtilsadlVIVLKRGAI 1578
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHR---------VIALERGKL 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
718-949 |
7.14e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.18 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-------LAALGEMQkVSGAVFwsslpdsEIGEDPSPEretatdlDIRK-RG 789
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLrvlnlleMPRSGTLN-IAGNHF-------DFSKTPSDK-------AIRElRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 PVAYASQK----PWLlnaTVEENIIfESPFN---------KQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQR 856
Cdd:PRK11124 83 NVGMVFQQynlwPHL---TVQQNLI-EAPCRvlglskdqaLARAEKLLERLRLKPYADRFP-----------LHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTL 935
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
250
....*....|....
gi 1189438336 936 KDFQRSECQLFEHW 949
Cdd:PRK11124 226 SCFTQPQTEAFKNY 239
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1085-1247 |
7.50e-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: 62.02 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1085 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1164
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1165 SRSTLLCVSALAVISYV----TPVFLVALLPLAIVCYFIQKYFRVASRDL-QQLDDttqlpLLSHFAETVEGLTTIRAFR 1239
Cdd:cd18544 123 IGDLLLLIGILIAMFLLnwrlALISLLVLPLLLLATYLFRKKSRKAYREVrEKLSR-----LNAFLQESISGMSVIQLFN 197
|
....*...
gi 1189438336 1240 YEARFQQK 1247
Cdd:cd18544 198 REKREFEE 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
718-948 |
1.56e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.47 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpSPERETATDLDIR---KRGPVAYA 794
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL----NRAQRKAFRRDIQmvfQDSISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 SQKpwllnaTVEEnIIFE--------SPFNKQ-RYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVARA 864
Cdd:PRK10419 104 PRK------TVRE-IIREplrhllslDKAERLaRASEMLRAVDLDDSVlDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 865 LYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLkdfq 939
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQqfgtACLFITHDLRLVERfCQRVMVMDNGQIVETQPV---- 236
|
....*....
gi 1189438336 940 rSECQLFEH 948
Cdd:PRK10419 237 -GDKLTFSS 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
718-935 |
1.90e-09 |
|
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: 58.49 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAalgemqkvsgaVFWSSLPDSEIGEDPSPERETATDLDirkrgpvayasqk 797
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-----------GLYASGKARLISFLPKFSRNKLIFID------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 pwllnatveeniifespfnkqrykmvieacSLQPDIDI----LPHGDQTQigergiNLSGGQRQRISVARALYQHA-NVV 872
Cdd:cd03238 67 ------------------------------QLQFLIDVglgyLTLGQKLS------TLSGGELQRVKLASELFSEPpGTL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 873 F-LDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 935
Cdd:cd03238 111 FiLDEPSTGLHQQDINQLL--EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKV 172
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1104-1251 |
2.06e-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: 60.58 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1104 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP 1183
Cdd:cd18576 57 IYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1184 ---VFLVALLP-LAIVCYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAF---RYEA-RFQQKLLEY 1251
Cdd:cd18576 137 kltLLMLATVPvVVLVAVLFGRRIRKLSKKVQdELAEAN-----TIVEETLQGIRVVKAFtreDYEIeRYRKALERV 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
713-942 |
2.26e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 59.61 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGED---PSPERetatdldIRKRG 789
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-------GEDitgLPPHR-------IARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 pVAYASQK----PWLlnaTVEENII--FESPFNKQRYKMVIEACslqpdIDILPhgdqtQIGER----GINLSGGQRQRI 859
Cdd:COG0410 80 -IGYVPEGrrifPSL---TVEENLLlgAYARRDRAEVRADLERV-----YELFP-----RLKERrrqrAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 860 SVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 938
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFE--IIRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAEL 223
|
....
gi 1189438336 939 QRSE 942
Cdd:COG0410 224 LADP 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
718-933 |
2.33e-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: 59.13 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGqLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETatdldIRKRgpVAYASQK 797
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRID-------GQDVLKQPQK-----LRRR--IGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 P-WLLNATVEENIIF-------ESPFNKQRYKMVIEAcslqpdIDILPHGDQtQIGErginLSGGQRQRISVARALYQHA 869
Cdd:cd03264 81 FgVYPNFTVREFLDYiawlkgiPSKEVKARVDEVLEL------VNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 870 NVVFLDDPFSALD----IHLSDHLMQAGilellrdDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 933
Cdd:cd03264 150 SILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1366-1564 |
2.37e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM------------VDTFEGHIIIDgidiaK 1433
Cdd:PRK14258 8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesevrvegrVEFFNQNIYER-----R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPLHTLRSRLSIILQDPVLFSGTI---------------RFNLDP--ERKCSDSTLWEalEIAQlKLVVKALpggldaii 1496
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVydnvaygvkivgwrpKLEIDDivESALKDADLWD--EIKH-KIHKSAL-------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1497 teggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1564
Cdd:PRK14258 150 -----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1365-1590 |
2.59e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.03 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1365 KIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDP-VLFSGT-----IRFNLDpERKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFV 1518
Cdd:PRK13635 85 MVFQNPdNQFVGAtvqddVAFGLE-NIGVPREEMVERVDQA-LRQV------GMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1519 RKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
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 ... |
1366-1579 |
2.63e-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: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFeghiiidgidiaklplhtLRSRL 1443
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGL------------------LEPDA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIIL-------QDPVLFSGTIRFNLDPERKCSDSTLWEALEI---------AQLKLVVKALPGGLD--AIITEGGENFSQ 1505
Cdd:cd03266 60 GFATvdgfdvvKEPAEARRRLGFVSDSTGLYDRLTARENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFST 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1506 GQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAIL 1579
Cdd:cd03266 140 GMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
718-934 |
3.07e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQ----KVSGAVFWsslpdseIGEDpsperetATDLD-IRKRGP 790
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYdskiKVDGKVLY-------FGKD-------IFQIDaIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKP-WLLNATVEENIIFesPF------NKQRYKMVIEACSLQPDIDILPHgdqTQIGERGINLSGGQRQRISVAR 863
Cdd:PRK14246 92 VGMVFQQPnPFPHLSIYDNIAY--PLkshgikEKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 864 ALYQHANVVFLDDPFSALDIhLSDHLMQAGILELlrDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 934
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDI-VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1112-1248 |
3.09e-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: 60.15 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1112 LKVAKRLHRSLL----NRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPST-LECLSRSTLLCVSALAVISYVTPVFL 1186
Cdd:cd18570 67 LKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1187 VALLPL---AIVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFRYEARFQQKL 1248
Cdd:cd18570 146 ITLLIIplyILIILLFNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKKI 206
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
718-924 |
3.17e-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: 58.81 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSL---LLAALGEMQKVSGavfWSSLPDSEIGEDPSPERETATDLdirkrGPVAYA 794
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdTIYAEGQRRYVES---LSAYARQFLGQMDKPDVDSIEGL-----SPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 SQKPWLLN-----ATVEE-----NIIFESPFNKQRYKMVIEacslqpdidilphgdqtqIG------ERGIN-LSGGQRQ 857
Cdd:cd03270 83 DQKTTSRNprstvGTVTEiydylRLLFARVGIRERLGFLVD------------------VGlgyltlSRSAPtLSGGEAQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 858 RISVARALyqHANVV----FLDDPFSALdiHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 924
Cdd:cd03270 145 RIRLATQI--GSGLTgvlyVLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
707-942 |
3.36e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.76 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIgedpspeRETATDLDIR 786
Cdd:PRK13649 12 YQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV---RVDDTLI-------TSTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 K-RGPVAYASQKPWllNATVEENIIFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 864
Cdd:PRK13649 82 QiRKKVGLVFQFPE--SQLFEETVLKDVAFGPQNFGVsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 865 LYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRSE 942
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDiFQDVD 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
718-937 |
3.89e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.43 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSlpdseigedpsperETATDLDIRK-RGPVAYASQ 796
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG--------------EPITKENIREvRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 797 KP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:PRK13652 86 NPddQIFSPTVEQDIAF-GPINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEE 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1366-1591 |
3.95e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY---DSSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP- 1435
Cdd:PRK10261 314 LQVRNLVTRFplrSGLLNRVTREVHAVekvsfdLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 --LHTLRSRLSIILQDPVLfsgtirfNLDPERKCSDSTLwEALEIAQLkLVVKALPGGLDAIITEGG----------ENF 1503
Cdd:PRK10261 394 gkLQALRRDIQFIFQDPYA-------SLDPRQTVGDSIM-EPLRVHGL-LPGKAAAARVAWLLERVGllpehawrypHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1504 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NI---LQKVVMTAFA----DRTVVT-IAHRVHTILSADLVI 1571
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLlldLQRDFGIAYLfishDMAVVErISHRVAVMYLGQIVE 544
|
250 260
....*....|....*....|
gi 1189438336 1572 VLKRGAIleFDKPEKLLSRK 1591
Cdd:PRK10261 545 IGPRRAV--FENPQHPYTRK 562
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
718-934 |
3.96e-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: 59.17 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSL----LLAAL-----------GEMQKVSGAVFWSSLPD---SEIGEDPSPERET 779
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtLYPALarrlhlkkeqpGNHDRIEGLEHIDKVIVidqSPIGRTPRSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 780 ATDL--DIR---------KRgpvaYASQKpwL------------LNATVEENIIFESPFNKQRYKmvieacsLQPDIDIl 836
Cdd:cd03271 91 YTGVfdEIRelfcevckgKR----YNRET--LevrykgksiadvLDMTVEEALEFFENIPKIARK-------LQTLCDV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 837 phG-DQTQIGERGINLSGGQRQRISVARALYQHAN---VVFLDDPFSALdiHLSD--HLMQagILELLRDDKRTVVLVTH 910
Cdd:cd03271 157 --GlGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL--HFHDvkKLLE--VLQRLVDKGNTVVVIEH 230
|
250 260 270
....*....|....*....|....*....|
gi 1189438336 911 KLQYLPHADWIIAM------KDGTIQREGT 934
Cdd:cd03271 231 NLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
718-942 |
4.80e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdseigeDPSPERETATDL-DIRKRGPVAYASQ 796
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV------------KIDGELLTAENVwNLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 797 KPWLLNATVEENIIF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHANVV 872
Cdd:PRK13642 91 DNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDF-----KTREPAR---LSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 873 FLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 942
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRV-IHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSElFATSE 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
716-942 |
5.01e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.36 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPEretaTDLDIRKRGPVAYAS 795
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID-------GDLLTEE----NVWDIRHKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLLNATVEENIIF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHANV 871
Cdd:PRK13650 90 PDNQFVGATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDF-----KEREPAR---LSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 872 VFLDDPFSALDihlsdhlmQAGILELLRDDKR-------TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 942
Cdd:PRK13650 162 IILDEATSMLD--------PEGRLELIKTIKGirddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSRGN 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
714-933 |
5.05e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseIGEDPSPERETATDLDirkrGPVAY 793
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL--------IDGQEMRFASTTAALA----AGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLL-NATVEENII---FESPFNKQRYKMVIEACSLQPD---IDILPhgdQTQIGErginLSGGQRQRISVARALY 866
Cdd:PRK11288 84 IYQELHLVpEMTVAENLYlgqLPHKGGIVNRRLLNYEAREQLEhlgVDIDP---DTPLKY----LSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLqylphaDWIIAMKDG-TIQREG 933
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
713-934 |
5.11e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 58.15 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKVSGAVFwsslpdseiGEDPSpeRETAtdlDIRKRgp 790
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTikMLTTLLKPTSGRATVA---------GHDVV--REPR---EVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLLNA-TVEENI-IFESPFN------KQRYKMVIEAcslqpdIDILPHGDqtqigERGINLSGGQRQRISVA 862
Cdd:cd03265 75 IGIVFQDLSVDDElTGWENLyIHARLYGvpgaerRERIDELLDF------VGLLEAAD-----RLVKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 863 RALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGT 934
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGT 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
710-929 |
5.17e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 58.60 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 710 WTPDGIPT-LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGemQKVSGAVFWSslpdseiGEDPSP--ERETATdld 784
Cdd:COG4181 19 GTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLglLAGLD--RPTSGTVRLA-------GQDLFAldEDARAR--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 IRKRGpVAYASQKPWLLNA-TVEENI-----IFESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQR 858
Cdd:COG4181 87 LRARH-VGFVFQSFQLLPTlTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 859 ISVARALYQHANVVFLDDPFSALDIHLSDHlmqagILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQ-----IIDLLFELNRergtTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1366-1578 |
5.73e-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: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03262 1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDpvlfsgtirFNLDPE--------------RKCSDStlwEALEIAQ--LKLVvkalpgGLDAIITEGGENFSQGQ 1507
Cdd:cd03262 79 GMVFQQ---------FNLFPHltvlenitlapikvKGMSKA---EAEERALelLEKV------GLADKADAYPAQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1508 RQLFCLARAFVRKTSIFIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:cd03262 141 QQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1385-1578 |
7.10e-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: 57.50 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1385 HVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKLPLHTLRSR--LSIILQDPVLFSG-TIRFNL 1461
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL----LNLIAGFETPQSGRVLINGVDVTAAPPADrpVSMLFQENNLFAHlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1462 DPERkcsdSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIL 1541
Cdd:cd03298 92 GLGL----SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438336 1542 QKVVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:cd03298 168 LDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
851-927 |
8.83e-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: 8.83e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 851 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 927
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINL-MLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1366-1588 |
9.46e-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: 57.79 E-value: 9.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF-SLAFFRM-----------------VDTFEghiiid 1427
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLpptygndvrlfgerrggEDVWE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1428 gidiaklplhtLRSRLSII---LQDPVLFSGTIR-------FnldperkcsDST-LWEALEIAQLKLVVKALPG-GLDAI 1495
Cdd:COG1119 76 -----------LRKRIGLVspaLQLRFPRDETVLdvvlsgfF---------DSIgLYREPTDEQRERARELLELlGLAHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1496 ItegGENF---SQGQRQLFCLARAFVRKTSIFIMDEATASIDM-ATENILQkvVMTAFA---DRTVVTIAHRVHTILSA- 1567
Cdd:COG1119 136 A---DRPFgtlSQGEQRRVLIARALVKDPELLILDEPTAGLDLgARELLLA--LLDKLAaegAPTLVLVTHHVEEIPPGi 210
|
250 260
....*....|....*....|.
gi 1189438336 1568 DLVIVLKRGAILEFDKPEKLL 1588
Cdd:COG1119 211 THVLLLKDGRVVAAGPKEEVL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
713-882 |
1.09e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.89 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLA---ALGEMQKVSGAVFWSSLPDSEIGEdpsperetatdldiRKRG 789
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYNGIPYKEFAE--------------KYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 PVAYASQK----PWLlnaTVEENIIFespfnkqrykmvieACSLQpdidilphGDQTQigeRGInlSGGQRQRISVARAL 865
Cdd:cd03233 84 EIIYVSEEdvhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEAL 133
|
170
....*....|....*..
gi 1189438336 866 YQHANVVFLDDPFSALD 882
Cdd:cd03233 134 VSRASVLCWDNSTRGLD 150
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1366-1591 |
1.13e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHT------- 1438
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpdvdpie 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDPVLFSG-TIRFNLDPERKCSD--STLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLAR 1515
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1516 AFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILSADLVIVLKRGAILE-------FDKPEKL 1587
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgptrkvFENPEHE 242
|
....
gi 1189438336 1588 LSRK 1591
Cdd:PRK14267 243 LTEK 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
713-940 |
1.38e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.31 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQkvsgavfwsslPDSeiGEdpsperetatdldiRKRGP-- 790
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE-----------PDS--GT--------------VKLGEtv 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 -VAYASQKPWLL--NATVEENIifeSPFNKQRYKMVIEACsLQpdiDILPHGDQ--TQIGergiNLSGGQRQRISVARAL 865
Cdd:COG0488 379 kIGYFDQHQEELdpDKTVLDEL---RDGAPGGTEQEVRGY-LG---RFLFSGDDafKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 866 YQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ-REGTLKDF 938
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHdryfldRV-----ATRILEFEDGGVReYPGGYDDY 517
|
..
gi 1189438336 939 QR 940
Cdd:COG0488 518 LE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
713-928 |
1.40e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 55.15 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSlpdseigedpsperetatdldirkRGPVA 792
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVV 872
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 873 FLDDPFSALDIHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGT 928
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEA-----LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1366-1578 |
1.44e-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: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLrsrL 1443
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS------------------------------TL---L 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SII--LQDPVlfSGTIRFNLDPERKCSDSTLWE--------------------ALEIAQLKLVVKALPG----------- 1490
Cdd:cd03255 48 NILggLDRPT--SGEVRVDGTDISKLSEKELAAfrrrhigfvfqsfnllpdltALENVELPLLLAGVPKkerreraeell 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1491 ---GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRvHT 1563
Cdd:cd03255 126 ervGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTHD-PE 202
|
250
....*....|....*.
gi 1189438336 1564 ILS-ADLVIVLKRGAI 1578
Cdd:cd03255 203 LAEyADRIIELRDGKI 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1370-1576 |
1.83e-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: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1370 NLSVRYDSSL----KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVdtfEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03213 8 NLTVTVKSSPsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTG---LGVSGEVLINGRPLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFsgtirfnldperkcSDSTLWEALEI-AQLKlvvkalpgGLdaiiteggenfSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03213 85 GYVPQDDILH--------------PTLTVRETLMFaAKLR--------GL-----------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1523 IFIMDEATASIDMATENILQKVVMtAFAD--RTVVTIAHRVHTIL--SADLVIVLKRG 1576
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
718-934 |
1.86e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 58.51 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsperetaTDLDIR--KRGPVAYAS 795
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKI-----------SDAELRevRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLL-NATVEENIIFESPFN----KQRYKMVIEACSlQPDIDILPHGDQTQigerginLSGGQRQRISVARALYQHAN 870
Cdd:PRK10070 113 QSFALMpHMTVLDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 871 VVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
715-932 |
1.94e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.71 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFWSSLPDSEIGEDPSPEretatdldIRKRGpVA 792
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLaiLAGLDDGS--SGEVSLVGQPLHQMDEEARAK--------LRAKH-VG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWL---LNATveENIIFESPFNKQRykmviEACSLQPDIDILphgDQTQIGER----GINLSGGQRQRISVARAL 865
Cdd:PRK10584 92 FVFQSFMLiptLNAL--ENVELPALLRGES-----SRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 866 YQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 932
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADL-LFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
718-910 |
2.39e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpdsEIGEDPSPERETATDlDIRKRGPVAYASQk 797
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------DVPDNQFGREASLID-AIGRKGDFKDAVE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 pwLLNAT-VEENIIFESPFNkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHANVVFLDD 876
Cdd:COG2401 118 --LLNAVgLSDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 1189438336 877 PFSALDIHLSdHLMQAGILELLRDDKRTVVLVTH 910
Cdd:COG2401 163 FCSHLDRQTA-KRVARNLQKLARRAGITLVVATH 195
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
852-929 |
2.44e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.86 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 852 SGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKRT----VVLVTHKL---QYLPHAdwIIAM 924
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225
|
....*
gi 1189438336 925 KDGTI 929
Cdd:PRK11701 226 KQGRV 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1366-1603 |
2.50e-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: 56.54 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSG-TIRFN--LDPerkcsdsTL--WEALEIAQ-----LKLVvkalpgGLDaiITEGGENF----SQGQRQLF 1511
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVP-------KLlkWPKEKIREradelLALV------GLD--PAEFADRYphelSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1512 CLARAFVRKTSIFIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILSADLVIVLKRGAILEFDKP 1584
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTP 220
|
250 260
....*....|....*....|
gi 1189438336 1585 EKLLSRKDSVF-ASFVRADK 1603
Cdd:cd03295 221 DEILRSPANDFvAEFVGADR 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
718-937 |
2.52e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.15 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLllaalgeMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQK 797
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTL-------MQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALYQHA 869
Cdd:PRK13641 96 AQLFENTVLKDVEF-GPKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 870 NVVFLDDPFSALDIHLSDHLMQagileLLRDDKR---TVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQ-----LFKDYQKaghTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKE 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
718-963 |
2.67e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.54 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslPDSEIG----EDPSPERETATD---------LD 784
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP--KGLRIGylpqEPPLDDDLTVLDtvldgdaelRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 IRKRgpVAYASQKPwllnATVEENII--------FESpfnkqrykmvIEACSLQPDIDI------LPHGDQTQ-IGErgi 849
Cdd:COG0488 92 LEAE--LEELEAKL----AEPDEDLErlaelqeeFEA----------LGGWEAEARAEEilsglgFPEEDLDRpVSE--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 850 nLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlsdhlmqaGIL---ELLRDDKRTVVLVTH------KLqylphADW 920
Cdd:COG0488 153 -LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE--------SIEwleEFLKNYPGTVLVVSHdryfldRV-----ATR 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1189438336 921 IIAMKDGTIQR-EGTLKDFQRSECQLFEHWKTLMNRQDQELEKE 963
Cdd:COG0488 219 ILELDRGKLTLyPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKE 262
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
716-933 |
3.29e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.25 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVfwssLPDSEIGEDPSperetATDLDIRKRGPVAY 793
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcINKLEEIT--SGDL----IVDGLKVNDPK-----VDERLIRQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 asQKPWLL-NATVEENIIFeSPFnkqRYKMVIEACSLQPDIDILphgDQTQIGERG----INLSGGQRQRISVARALYQH 868
Cdd:PRK09493 84 --QQFYLFpHLTALENVMF-GPL---RVRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 869 ANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDG 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1366-1594 |
3.30e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.68 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPV-LFSGTI-----RFNLDPErkcsdstlweALEIAQLKLVVKALPGGLDAIITEGGE--NFSQGQRQLFCLARAF 1517
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENH----------AVPYDEMHRRVSEALKQVDMLERADYEpnALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1518 VRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSV 1594
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
718-942 |
3.51e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKVSGAvfwsslpdsEIGEDPSPERETATDLDIRKrgpVAYASQK 797
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPPSEG---------EILLDAQPLESWSSKAFARK---VAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 -PWLLNATVEENI-IFESP-------FNKQRYKMVIEACSLqpdIDILPhgdqtqIGERGIN-LSGGQRQRISVARALYQ 867
Cdd:PRK10575 94 lPAAEGMTVRELVaIGRYPwhgalgrFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 868 HANVVFLDDPFSALDI-HLSDHLmqAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:PRK10575 165 DSRCLLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
715-913 |
3.67e-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: 56.19 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdSEIGEDPSPEREtatdlDIRKRGPVAYA 794
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-------RVAGLVPWKRRK-----KFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 --SQKPWLLNATVEENI---IFESPfnKQRYKMVIEACSlqpdiDILPHGDQTQIGERgiNLSGGQRQRISVARALYQHA 869
Cdd:cd03267 102 qkTQLWWDLPVIDSFYLlaaIYDLP--PARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438336 870 NVVFLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:cd03267 173 EILFLDEPTIGLDVV-AQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
851-938 |
6.05e-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: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 851 LSGGQRQRISVARALyqhAN---VVFLDDPFSALDIHLsdhlmQAGILELLRDDKRT----VVLVTHKL----QYlphAD 919
Cdd:COG4172 157 LSGGQRQRVMIAMAL---ANepdLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLgvvrRF---AD 225
|
90
....*....|....*....
gi 1189438336 920 WIIAMKDGTIQREGTLKDF 938
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAEL 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
713-927 |
6.33e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqKVSGAVFWSSLPDSEIGEDPSPERETatdlDIR--KRGP 790
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLM--------KVLSGVYPHGTYEGEIIFEGEELQAS----NIRdtERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 791 VAYASQKPWLL-NATVEENIIFES---PFNKQRY-KMVIEACSL--QPDIDILPHgdqTQIGergiNLSGGQRQRISVAR 863
Cdd:PRK13549 84 IAIIHQELALVkELSVLENIFLGNeitPGGIMDYdAMYLRAQKLlaQLKLDINPA---TPVG----NLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 864 ALYQHANVVFLDDPFSALDIHLSDHLmqagiLELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 927
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVL-----LDIIRDLKAhgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
714-942 |
6.55e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllaalgeMQKVSGAVfwssLPDS---EIGEDP----SPERetATDLDIr 786
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTL-------MKIIAGIV----PPDSgtlEIGGNPcarlTPAK--AHQLGI- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 787 krgpvaY-ASQKPWLL-NATVEENIIFESPFNKQRYKMVIE-----ACSLQPDIdilphgdqtQIGergiNLSGGQRQRI 859
Cdd:PRK15439 89 ------YlVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDS---------SAG----SLEVADRQIV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 860 SVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 938
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
....
gi 1189438336 939 QRSE 942
Cdd:PRK15439 228 STDD 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1366-1590 |
7.25e-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: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFsLAFFRMVDTFEGHIIIDGIDIAKLP---------- 1435
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEPTSGRIIYHVALCEkcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 --------------------------LHTLRSRLSIILQDPvlfsgtirFNLDPERKCSDSTLwEALEIAQLKlVVKALP 1489
Cdd:TIGR03269 78 vgepcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRT--------FALYGDDTVLDNVL-EALEEIGYE-GKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1490 GGLDAI--------ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH 1559
Cdd:TIGR03269 148 RAVDLIemvqlshrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSH 227
|
250 260 270
....*....|....*....|....*....|..
gi 1189438336 1560 RVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:TIGR03269 228 WPEVIEDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1113-1247 |
8.67e-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: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1113 KVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVF-LVALL- 1190
Cdd:cd18547 75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtLIVLVt 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1191 -PLAIVC-YFI----QKYFRVASRDLQQLDdttqlpllSHFAETVEGLTTIRAFRYEARFQQK 1247
Cdd:cd18547 155 vPLSLLVtKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEE 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
701-939 |
9.75e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.16 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 701 VQIMGGYFTWTPDGIptLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGED-PSPERET 779
Cdd:PRK11831 8 VDMRGVSFTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD-------GENiPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 780 AtdLDIRKRGPVAYASqKPWLLNATVEENIIF--------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNL 851
Cdd:PRK11831 79 L--YTVRKRMSMLFQS-GALFTDMNVFDNVAYplrehtqlPAPLLHSTVMMKLEAVGLRGAAKLMPS-----------EL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 852 SGGQRQRISVARALYQHANVVFLDDPFSALD-------IHLSDHLMQA-GIlellrddkrTVVLVTHKL-QYLPHAD--W 920
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDpitmgvlVKLISELNSAlGV---------TCVVVSHDVpEVLSIADhaY 215
|
250
....*....|....*....
gi 1189438336 921 IIAmkDGTIQREGTLKDFQ 939
Cdd:PRK11831 216 IVA--DKKIVAHGSAQALQ 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1366-1581 |
1.15e-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: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQkIGICGRTGSGKSSFslafFRMVDTF----EGHIIIDGIDIAKLPlHTLRS 1441
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTL----MRILATLtppsSGTIRIDGQDVLKQP-QKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDPVLFSG-TIRFNLD--------PERKCsDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1512
Cdd:cd03264 73 RIGYLPQEFGVYPNfTVREFLDyiawlkgiPSKEV-KARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1513 LARAFVRKTSIFIMDEATASID----MATENILQKVVmtafADRTVVTIAHRVHTILS-ADLVIVLKRGAILEF 1581
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG----EDRIVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
713-927 |
1.16e-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: 56.37 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqKVSGAVFWSSLPDSEIGEDPSPERetATDLDIRKRGPVA 792
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLM--------KILSGVYPHGTWDGEIYWSGSPLK--ASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 793 YASQKPWLL-NATVEENIIFES----PFNKQRYKMVIEACS---LQPDIDILPhgDQTQIGERGinlsGGQRQRISVARA 864
Cdd:TIGR02633 82 IIHQELTLVpELSVAENIFLGNeitlPGGRMAYNAMYLRAKnllRELQLDADN--VTRPVGDYG----GGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 865 LYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 927
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETE-----ILLDIIRDLKAhgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1366-1592 |
1.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVD-TFEGHIIIDGIDIAKLPLHT---LR 1440
Cdd:PRK13650 5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDgLLEAESGQIIIDGDLLTEENvwdIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 SRLSIILQDP-VLFSGT-----IRFNLDP---ERKCSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLF 1511
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGAtveddVAFGLENkgiPHEEMKERVNEALELV-----------GMQDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1512 CLARAFVRKTSIFIMDEATASID--------MATENILQKVVMTafadrtVVTIAHRVHTILSADLVIVLKRGAILEFDK 1583
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQMT------VISITHDLDEVALSDRVLVMKNGQVESTST 223
|
....*....
gi 1189438336 1584 PEKLLSRKD 1592
Cdd:PRK13650 224 PRELFSRGN 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
850-912 |
1.47e-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: 1.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 850 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKL 912
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKL 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
718-942 |
1.47e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQ--------KVSGAVFWSSLPDSEIgedpsPERETAtdldiRKRG 789
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAI-----DAPRLA-----RLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 790 PVAYASQKPWLLnaTVEENIIFespfnkQRYKMVIEACSL-QPDIDILPH-----GDQTQIGERGINLSGGQRQRISVAR 863
Cdd:PRK13547 87 VLPQAAQPAFAF--SAREIVLL------GRYPHARRAGALtHRDGEIAWQalalaGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 864 ALYQ----HANVV-----FLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 933
Cdd:PRK13547 159 VLAQlwppHDAAQpprylLLDEPTAALDLA-HQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVAHG 237
|
....*....
gi 1189438336 934 TLKDFQRSE 942
Cdd:PRK13547 238 APADVLTPA 246
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
725-921 |
1.65e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 725 IPR-GQLTMIVGQVGCGKSSLLLAALGEMQ----KVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQKPW 799
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKpnlgKFDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 800 LLNATVEENIIFESPFNKQRYkmVIEACSLQPdidilphgdqtqIGERGI-NLSGGQRQRISVARALYQHANVVFLDDPF 878
Cdd:cd03236 102 AVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438336 879 SALDIHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWI 921
Cdd:cd03236 168 SYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1366-1580 |
1.72e-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: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM---------VDTFEghiiIDGIDIAKLPL 1436
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEerptsgqvlVNGQD----LSRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1437 htLRSRLSIILQDpvlfsgtirFNLDPERkcsdsTLWE----ALEIAQ-------------LKLV-----VKALPGGLda 1494
Cdd:COG2884 77 --LRRRIGVVFQD---------FRLLPDR-----TVYEnvalPLRVTGksrkeirrrvrevLDLVglsdkAKALPHEL-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1495 iiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFADR--TVVtIA-HRVHTILSADL- 1569
Cdd:COG2884 139 ---------SGGEQQRVAIARALVNRPELLLADEPTGNLDPETsWEIME--LLEEINRRgtTVL-IAtHDLELVDRMPKr 206
|
250
....*....|.
gi 1189438336 1570 VIVLKRGAILE 1580
Cdd:COG2884 207 VLELEDGRLVR 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
850-979 |
1.72e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 850 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 924
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVI 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 925 KDGTIQREGTLKDfqrsecqLFEHWKTLMNRQ------DQELEkETVTERKATEPPQGLSR 979
Cdd:PRK11153 215 DAGRLVEQGTVSE-------VFSHPKHPLTREfiqstlHLDLP-EDYLARLQAEPTTGSGP 267
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
714-937 |
2.53e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIgedPSPERETATDLDIrkrgPVAY 793
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI---TINNINY---NKLDHKLAAQLGI----GIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 asQKPWLLNA-TVEENI--------------IFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQR 858
Cdd:PRK09700 87 --QELSVIDElTVLENLyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 859 ISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSD 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
721-933 |
2.70e-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: 53.14 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 721 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdsEI-GEDPSPERetatdLDIRKRGPVAYASQK-- 797
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--------TVdGFDVVKEP-----AEARRRLGFVSDSTGly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLlnaTVEENIIFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARALYQHAN 870
Cdd:cd03266 91 DRL---TARENLEYFAGLYglkgdelTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 871 VVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
712-934 |
2.78e-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: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgemQKVSGAvfwsslpDSEIGEDPSPERETAtDLDIRK-- 787
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLrmVAGL---ERITSG-------EIWIGGRVVNELEPA-DRDIAMvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 788 -----------RGPVAYAsqkpwLLNATVEENIIfespfnKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 856
Cdd:PRK11650 83 qnyalyphmsvRENMAYG-----LKIRGMPKAEI------EERVAEAARILELEPLLDRKPR-----------ELSGGQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 857 QRISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
712-912 |
2.81e-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: 55.79 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseIGEdpspeRETATDLDIRKRGPV 791
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL--------VGG-----KDIETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 792 AYASQKPWLLNATVEENIIFESPFNKQRYkmviEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANV 871
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1189438336 872 VFLDDPFSALDIHlsdhlMQAGILELLRDDK--RTVVLVTHKL 912
Cdd:TIGR01257 1083 VVLDEPTSGVDPY-----SRRSIWDLLLKYRsgRTIIMSTHHM 1120
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1079-1267 |
2.86e-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: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 TLDQTVYAMVFTVLCSLGIVLCL------VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNT 1152
Cdd:cd18554 36 TLDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1153 IDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVA---LLPLAIVC-YFIQKYFRVASRDLQQLDDTTQlpllSHFAET 1228
Cdd:cd18554 116 TKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFYILAvKYFFGRLRKLTKERSQALAEVQ----GFLHER 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 1189438336 1229 VEGLTTIRAFRYEARFQQkllEYTDSNNiasLFLTAANR 1267
Cdd:cd18554 192 IQGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1366-1601 |
2.88e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.97 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDP--VLFSGTI-------RFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARA 1516
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1517 FVRKTSIFIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEkLLSR 1590
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTD 227
|
250
....*....|.
gi 1189438336 1591 KDSVFASFVRA 1601
Cdd:PRK13647 228 EDIVEQAGLRL 238
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
718-929 |
2.92e-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: 52.43 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETatdlDIRKRGpVAYAS-- 795
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-------GKPVTRRSPR----DAIRAG-IAYVPed 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 --QKPWLLNATVEENIIFespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQHANVVF 873
Cdd:cd03215 84 rkREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 874 LDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
710-931 |
3.04e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.70 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 710 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAAL------GEMQkVSGaVFWSSLPDSEIgedpsperetatdl 783
Cdd:cd03289 12 YTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQ-IDG-VSWNSVPLQKW-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 784 dirkRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 863
Cdd:cd03289 76 ----RKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 864 ALYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQR 931
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1383-1589 |
3.90e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.27 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1383 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRS----RLSIILQDpvlfsgtir 1458
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1459 FNLDPERKCSDSTLWeALEIAQLKLVVKAlPGGLDAIITEGGENF--------SQGQRQLFCLARAFVRKTSIFIMDEAT 1530
Cdd:PRK10070 115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1531 ASID--MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK10070 193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1029-1594 |
4.06e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1029 AGILLLSLLvfSQLLKHMVLVAIDYWLAKWTDSALTLTPAarncslsqectldqtvyamvFTVLCSLGIVLCLVTSVTVE 1108
Cdd:PRK10522 16 ISVMALSLA--SAALGIGLIAFINQRLIETADTSLLVLPE--------------------FLGLLLLLMAVTLGSQLALT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1109 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID---QHIPStlecLSRSTLLCVSALAVISYVTP-V 1184
Cdd:PRK10522 74 TLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITiafVRLPE----LVQGIILTLGSAAYLAWLSPkM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1185 FLVALLPLAIVcyFIQKYFRVAS-----RDLQQLDDTtqlpLLSHFAETVEG-----LTTIRA-FRYEARFQQKLLEYTD 1253
Cdd:PRK10522 150 LLVTAIWMAVT--IWGGFVLVARvykhmATLRETEDK----LYNDYQTVLEGrkeltLNRERAeYVFENEYEPDAQEYRH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1254 SNNIASLFLTAANRWLEVRMeyIGAcvvlIAAVTSISNSLhrelsaGLVGLGL--TYALMVSNYLNWMVRNLADMELQLG 1331
Cdd:PRK10522 224 HIIRADTFHLSAVNWSNIMM--LGA----IGLVFYMANSL------GWADTNVaaTYSLTLLFLRTPLLSAVGALPTLLS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1332 AVKRIHGLLKTEAESYEGLLAPSLIPKNWPdqgKIQIQNLSVRYDS---SLKPVlkhvNALIAPGQKIGICGRTGSGKSS 1408
Cdd:PRK10522 292 AQVAFNKLNKLALAPYKAEFPRPQAFPDWQ---TLELRNVTFAYQDngfSVGPI----NLTIKRGELLFLIGGNGSGKST 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1409 FSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTirfnLDPERKCSDSTLWEA-LEIAQLKlvvka 1487
Cdd:PRK10522 365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMA----- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1488 lpgglDAIITEGGE----NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRV 1561
Cdd:PRK10522 436 -----HKLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDD 510
|
570 580 590
....*....|....*....|....*....|...
gi 1189438336 1562 HTILSADLVIVLKRGAILEFDKPEKLLSRKDSV 1594
Cdd:PRK10522 511 HYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
711-929 |
4.34e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.17 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFW-----SSLPDSE----IG---EDPSpeRE 778
Cdd:COG1101 15 TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdgkdvTKLPEYKrakyIGrvfQDPM--MG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 779 TATDLdirkrgpvayasqkpwllnaTVEENII----------FESPFNKQRYKMVIEACSlqpDIDI-LPHGDQTQIGer 847
Cdd:COG1101 93 TAPSM--------------------TIEENLAlayrrgkrrgLRRGLTKKRRELFRELLA---TLGLgLENRLDTKVG-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 848 giNLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagiL--ELLRDDKRTVVLVTHKLQY-LPHADWIIAM 924
Cdd:COG1101 148 --LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRLIMM 222
|
....*
gi 1189438336 925 KDGTI 929
Cdd:COG1101 223 HEGRI 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
847-933 |
4.83e-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: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 847 RGIN--LSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADWI 921
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRV 175
|
90
....*....|..
gi 1189438336 922 IAMKDGTIQREG 933
Cdd:cd03217 176 HVLYDGRIVKSG 187
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
718-927 |
4.84e-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: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPdseigedpsperetatdLDIRKRGPVAYASQK 797
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP-----------------LDIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWL-LNATVEENIIFESpfnkQRYKMVIEACSLQPD-----IDILPHGDQtQIGErginLSGGQRQRISVARALYQHANV 871
Cdd:cd03269 79 RGLyPKMKVIDQLVYLA----QLKGLKKEEARRRIDewlerLELSEYANK-RVEE----LSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 872 VFLDDPFSALDIHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 927
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDV-IRE-LARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1380-1591 |
7.92e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1380 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIA------KLPLHTLRSRLSIILQDPVLF 1453
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1454 SG-TIRFNLD-PERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1531
Cdd:PRK14246 103 PHlSIYDNIAyPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1532 SIDMATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILE-------FDKPEKLLSRK 1591
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKNELTEK 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
852-915 |
9.70e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 9.70e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 852 SGGQRQRISVARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKRtvvlvTHKLQYL 915
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSL-----DKTVQAQILALLKSLQQ-----KHQLAYL 480
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1365-1587 |
9.78e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.09 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1365 KIQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIdgidiAKLPLH------- 1437
Cdd:PRK14243 10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVE-----GKVTFHgknlyap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 -----TLRSRLSIILQDPVLFSGTI-------------RFNLDP--ERKCSDSTLWEALEiAQLKlvvkalpggldaiit 1497
Cdd:PRK14243 83 dvdpvEVRRRIGMVFQKPNPFPKSIydniaygaringyKGDMDElvERSLRQAALWDEVK-DKLK--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1498 EGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVHTI---LSAD 1568
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMtafFNVE 226
|
250 260
....*....|....*....|
gi 1189438336 1569 LVIVLKR-GAILEFDKPEKL 1587
Cdd:PRK14243 227 LTEGGGRyGYLVEFDRTEKI 246
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1501-1599 |
1.11e-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: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:cd03299 128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNG 206
|
90 100
....*....|....*....|....
gi 1189438336 1577 AILEFDKPEKLLSRKDSVF-ASFV 1599
Cdd:cd03299 207 KLIQVGKPEEVFKKPKNEFvAEFL 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1366-1594 |
1.14e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYD-SSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:PRK13642 5 LEVENLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDP------VLFSGTIRFNLDPE---RKCSDSTLWEALeiaqlkLVVKALPggldaIITEGGENFSQGQRQLFCLAR 1515
Cdd:PRK13642 85 MVFQNPdnqfvgATVEDDVAFGMENQgipREEMIKRVDEAL------LAVNMLD-----FKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1516 AFVRKTSIFIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
..
gi 1189438336 1593 SV 1594
Cdd:PRK13642 233 DM 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
715-934 |
1.22e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.42 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpDSEIGEDPSpERETATDLDIRKRGPVAYA 794
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFD---GKDITDWQT-AKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 SQkpwllnaTVEENIIFESPF-NKQRYKMVIEACslqpdIDILPHGDQTQIgERGINLSGGQRQRISVARALYQHANVVF 873
Cdd:PRK11614 94 RM-------TVEENLAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 874 LDDPfsalDIHLSDHLMQA--GILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK11614 161 LDEP----SLGLAPIIIQQifDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
716-940 |
1.32e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.62 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMqkvsgavfwsslpdseigedPSPERETATDLDIRKRgPVAyAS 795
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIL--------------------PAGVRQTAGRVLLDGK-PVA-PC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QKPWLLNATVEENIifESPFNKQRyKM---VIEAC---SLQPDIDILPH-------GDQTQIGER-GINLSGGQRQRISV 861
Cdd:PRK10418 75 ALRGRKIATIMQNP--RSAFNPLH-TMhthARETClalGKPADDATLTAaleavglENAARVLKLyPFEMSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 862 ARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKRT----VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 936
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDV-----VAQARILDLLESIVQKralgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVE 226
|
....*
gi 1189438336 937 D-FQR 940
Cdd:PRK10418 227 TlFNA 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
720-941 |
1.36e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGeMQKVSGAVFWSSLP--DSEIGEDPSPERETATDLDirkrgpVAYASQK 797
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMAEKLEfnGQDLQRISEKERRNLVGAE------VAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWL-LNA--TVEENII-----FESPFNKQRYKMVIEACSLQ--PD----IDILPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:PRK11022 98 PMTsLNPcyTVGFQIMeaikvHQGGNKKTRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 864 ALYQHANVVFLDDPFSALDIhlsdhLMQAGILELL----RDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 938
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDV-----TIQAQIIELLlelqQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
...
gi 1189438336 939 QRS 941
Cdd:PRK11022 242 FRA 244
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
718-894 |
1.43e-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: 51.00 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPsperetatdLDIRKRGPVAYASQK 797
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL---LDGQDITKLP---------MHKRARLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLL-NATVEENI--IFESpFNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHANVVFL 874
Cdd:cd03218 84 ASIFrKLTVEENIlaVLEI-RGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180
....*....|....*....|....*..
gi 1189438336 875 DDPFSALD-IHLSD------HLMQAGI 894
Cdd:cd03218 158 DEPFAGVDpIAVQDiqkiikILKDRGI 184
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1364-1599 |
1.65e-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: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdtfeghiiidgidiaklplhTLRsrl 1443
Cdd:COG3839 2 ASLELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKST-----------------------------LLR--- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 sII--LQDPVlfSGTIRFN------LDP-ERKCS----DSTLW----------------------------EALEIAQLK 1482
Cdd:COG3839 48 -MIagLEDPT--SGEILIGgrdvtdLPPkDRNIAmvfqSYALYphmtvyeniafplklrkvpkaeidrrvrEAAELLGLE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1483 LVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVVMTafadrTV 1554
Cdd:COG3839 125 DLLDRKPKQL-----------SGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRRLGTT-----TI 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1555 -VTiahrvH------TIlsADLVIVLKRGAILEFDKPEKLLSRKDSVF-ASFV 1599
Cdd:COG3839 189 yVT-----HdqveamTL--ADRIAVMNDGRIQQVGTPEELYDRPANLFvAGFI 234
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1083-1324 |
1.68e-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: 51.70 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLE 1162
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAVISYVTPVF-LVAL--LP-LAIVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAF 1238
Cdd:cd18545 120 NLIPDLLTLVGIVIIMFSLNVRLaLVTLavLPlLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 RYE----ARFQQKLLEYTDSNNIASLFLTAANRWLEVrMEYIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYA----- 1309
Cdd:cd18545 196 AREdeneEIFDELNRENRKANMRAVRLNALFWPLVEL-ISALGTALVYWYGGKLV---LGGAITVGVLVAFIGYVgrfwq 271
|
250
....*....|....*..
gi 1189438336 1310 --LMVSNYLNWMVRNLA 1324
Cdd:cd18545 272 piRNLSNFYNQLQSAMA 288
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1380-1589 |
1.94e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.25 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1380 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHT------LRSRLSIILQDPVLF 1453
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyrdvleFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1454 SGTIRFN-LDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATAS 1532
Cdd:PRK14271 114 PMSIMDNvLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1533 IDMATENILQKVVMTaFADR-TVVTIAHRV-HTILSADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK14271 194 LDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1368-1409 |
2.36e-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: 2.36e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1189438336 1368 IQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1409
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTL 40
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
720-910 |
2.40e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 51.34 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdSEIGEdPSPERETatdldiRKRGPVAYASQKPW 799
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-------SLCGE-PVPSRAR------HARQRVGVVPQFDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 800 L-LNATVEENI-IFESPFN------KQRYKMVIEACSLQPDIDilphgdqTQIGErginLSGGQRQRISVARALYQHANV 871
Cdd:PRK13537 91 LdPDFTVRENLlVFGRYFGlsaaaaRALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVNDPDV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1189438336 872 VFLDDPFSALDIHlSDHLMQAGILELLRDDKrTVVLVTH 910
Cdd:PRK13537 160 LVLDEPTTGLDPQ-ARHLMWERLRSLLARGK-TILLTTH 196
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1366-1589 |
2.51e-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: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTlRSRLSI 1445
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 IL--QDPVLFSG-TIRFNLD-PERKCSDSTLWEALEIaqlklVVKALPgGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:cd03224 78 GYvpEGRRIFPElTVEENLLlGAYARRRAKRKARLER-----VYELFP-RLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1522 SIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:cd03224 152 KLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
728-937 |
2.54e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 728 GQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVF------------WSSLPDSEIGEDPSperetaTDLDIRKRgpvayAS 795
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhfgdysYRSQRIRMIFQDPS------TSLNPRQR-----IS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 796 QkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQRQRISVARALYQHANVVFL 874
Cdd:PRK15112 108 Q---ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 875 DDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:PRK15112 174 DEALASLDMSMRSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
715-941 |
2.82e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.17 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGP-VAY 793
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRGAdMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWL-LNA--TVEENIIfESPFNKQ---RYKMVIEACSLQPDIDIlPHGdQTQIGERGINLSGGQRQRISVARALYQ 867
Cdd:PRK10261 109 IFQEPMTsLNPvfTVGEQIA-ESIRLHQgasREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 868 HANVVFLDDPFSALDIhlsdhLMQAGILELLR----DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:PRK10261 186 RPAVLIADEPTTALDV-----TIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1366-1593 |
3.11e-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: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslkpVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVDT---FEGHIIIDGIDIAKLPLhtlr 1440
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLnlIAGFLPPDSgriLWNGQDLTALPPAERPV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 srlSIILQDPVLFSG-TIRFN----LDPERKCSD---STLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1512
Cdd:COG3840 74 ---SMLFQENNLFPHlTVAQNiglgLRPGLKLTAeqrAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPAlRQEMLDLVDeLCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
....
gi 1189438336 1590 RKDS 1593
Cdd:COG3840 220 GEPP 223
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
843-934 |
4.08e-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: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 843 QIGERGINLSGGQRQRISVARALYQHAN---VVFLDDPFSALdiHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPH 917
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKT 897
|
90 100
....*....|....*....|...
gi 1189438336 918 ADWII------AMKDGTIQREGT 934
Cdd:TIGR00630 898 ADYIIdlgpegGDGGGTVVASGT 920
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1366-1589 |
5.06e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 50.61 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVL---FSG--TIRFNLDPERK---CSDSTLWEALEIAQLKLVVKALpggLDAIITEggenFSQGQRQLFCLARAF 1517
Cdd:PRK09536 82 VPQDTSLsfeFDVrqVVEMGRTPHRSrfdTWTETDRAAVERAMERTGVAQF---ADRPVTS----LSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1518 VRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLSA---DLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPPADVLT 228
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1079-1261 |
5.39e-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: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 TLDQTVYAMVFTVLCSLGIVLCLVTS-VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHI 1157
Cdd:cd18541 35 TASQLLRYALLILLLALLIGIFRFLWrYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1158 PSTLECLSRSTLLCVSALAVISYVTPVF-LVALLPL---AIVCYFIQKYFRVASRDLQQ----LDDTTQlpllshfaETV 1229
Cdd:cd18541 115 GPGILYLVDALFLGVLVLVMMFTISPKLtLIALLPLpllALLVYRLGKKIHKRFRKVQEafsdLSDRVQ--------ESF 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438336 1230 EGLTTIRAF----RYEARFQQKLLEYTDSNN----IASLF 1261
Cdd:cd18541 187 SGIRVIKAFvqeeAEIERFDKLNEEYVEKNLrlarVDALF 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1366-1580 |
5.68e-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: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDS--SLKPVLKHVNALIAPGQKIGICGRTGSGKSSF----------------------------SLAFFR 1415
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnilggldrptsgevlidgqdisslserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1416 mvdtfeghiiidgidiaklplhtlRSRLSIILQDpvlfsgtirFNLDPE-----------------RKCSDSTLWEALEI 1478
Cdd:COG1136 85 ------------------------RRHIGFVFQF---------FNLLPEltalenvalplllagvsRKERRERARELLER 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1479 AQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQkvVMTAFAD---RTV 1554
Cdd:COG1136 132 VGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgEEVLE--LLRELNRelgTTI 198
|
250 260
....*....|....*....|....*.
gi 1189438336 1555 VTIAHRVHTILSADLVIVLKRGAILE 1580
Cdd:COG1136 199 VMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1082-1254 |
5.82e-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: 50.12 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1082 QTVYAMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1161
Cdd:cd18551 37 GLLALLVALFL--LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1162 -ECLSRSTLLCVS--ALAVISYVTPVFLVALLPLAIVC-YFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1236
Cdd:cd18551 115 pQLVTGVLTVVGAvvLMFLLDWVLTLVTLAVVPLAFLIiLPLGRRIRKASKRAQD-----ALGELSAALErALSAIRTVK 189
|
170
....*....|....*...
gi 1189438336 1237 AFRYEARFQQKLLEYTDS 1254
Cdd:cd18551 190 ASNAEERETKRGGEAAER 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
727-910 |
6.32e-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: 47.75 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 727 RGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseigedpsperetatdldirkrgpvayasqkpwLLNATVE 806
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------YIDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 807 ENIIFESPFNkqrykmvieacslqpdidilphgdqTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLS 886
Cdd:smart00382 42 LEEVLDQLLL-------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
170 180
....*....|....*....|....*...
gi 1189438336 887 DHLMQAGILELL----RDDKRTVVLVTH 910
Cdd:smart00382 97 ALLLLLEELRLLlllkSEKNLTVILTTN 124
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1091-1264 |
6.58e-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: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1091 VLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILA--------PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLE 1162
Cdd:cd18546 39 LLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRvfahlqrlSLDFHERETSGRIMTRMTSDIDALSELLQTGLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAVISYVTP----VFLVALLPLAIVCYFiqkyFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF 1238
Cdd:cd18546 119 QLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRW----FRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAF 194
|
170 180
....*....|....*....|....*....
gi 1189438336 1239 RYEARFQQKLLEYTDSN---NIASLFLTA 1264
Cdd:cd18546 195 RRERRNAERFAELSDDYrdaRLRAQRLVA 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
714-910 |
7.60e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDLDIRKRGPVAy 793
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS-------GHDITRLKNREVPFLRRQIGMIF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 aSQKPWLLNATVEENIIFespfnkqryKMVIEACSLQpDIDILPHGDQTQIG------ERGINLSGGQRQRISVARALYQ 867
Cdd:PRK10908 86 -QDHHLLMDRTVYDNVAI---------PLIIAGASGD-DIRRRVSAALDKVGlldkakNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438336 868 HANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR---TVVLVTH 910
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSE-----GILRLFEEFNRvgvTVLMATH 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
851-927 |
8.05e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.47 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 851 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 925
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 1189438336 926 DG 927
Cdd:PRK15134 232 NG 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
720-903 |
8.55e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWS-----SLPDSE----------IGEDPSperetaTDLD 784
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridTLSPGKlqalrrdiqfIFQDPY------ASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 785 IRKrgPVAYASQKPWLLNAtveeniIFESPFNKQRYKMVIEACSLQPDIDI-LPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:PRK10261 416 PRQ--TVGDSIMEPLRVHG------LLPGKAAAARVAWLLERVGLLPEHAWrYPH-----------EFSGGQRQRICIAR 476
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1189438336 864 ALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR 903
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVSI-----RGQIINLLLDLQR 511
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1366-1544 |
1.04e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.32 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYD------------SSLKPVlKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAK 1433
Cdd:PRK15079 9 LEVADLKVHFDikdgkqwfwqppKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 L---PLHTLRSRLSIILQDPvLFSgtirfnLDPERKCSD------STLWEALEIAQLKLVVKAL---PGGLDAIITEGGE 1501
Cdd:PRK15079 88 MkddEWRAVRSDIQMIFQDP-LAS------LNPRMTIGEiiaeplRTYHPKLSRQEVKDRVKAMmlkVGLLPNLINRYPH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1189438336 1502 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKV 1544
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNLLQQL 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
718-914 |
1.22e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdseigedpsperETATDLDirkrgpVAYASQK 797
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------------HCGTKLE------VAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLLNA--TVEENIifesPFNKQ------RYKMVIEacSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQHA 869
Cdd:PRK11147 391 RAELDPekTVMDNL----AEGKQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1189438336 870 NVVFLDDPFSALDIHLSDHLMqagilELLRDDKRTVVLVTHKLQY 914
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLE-----ELLDSYQGTVLLVSHDRQF 499
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1086-1336 |
1.25e-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: 49.05 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1086 AMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1165
Cdd:cd18563 48 GLAGAYV--LSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1166 RSTLLCVSALAVISYVTPVF-LVALLPLAIVCYFIQKYFRVASRDLQQL----DDTTqlpllSHFAETVEGLTTIRAF-- 1238
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLaLLVLIPVPLVVWGSYFFWKKIRRLFHRQwrrwSRLN-----SVLNDTLPGIRVVKAFgq 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 -RYE-ARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEyIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYALMVSNYL 1316
Cdd:cd18563 201 eKREiKRFDEANQELLDANIRAEKLWATFFPLLTFLTS-LGTLIVWYFGGRQV---LSGTMTLGTLVAFLSYLGMFYGPL 276
|
250 260
....*....|....*....|
gi 1189438336 1317 NWMVRNLADMELQLGAVKRI 1336
Cdd:cd18563 277 QWLSRLNNWITRALTSAERI 296
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1366-1409 |
1.28e-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: 1.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1409
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1083-1293 |
1.36e-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: 49.00 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLE 1162
Cdd:cd18567 42 TVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAVI-SYVTPVFLVALLPLAIVC---YFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAF 1238
Cdd:cd18567 121 EALLDGLMAILTLVMMfLYSPKLALIVLAAVALYAllrLALYPPLRRATEEQIVASAKEQ----SHFLETIRGIQTIKLF 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1239 RYEARFQQKLLE-YTDSNN------IASLFLTAANRWLeVRMEYIGacVVLIAAVTSISNSL 1293
Cdd:cd18567 197 GREAEREARWLNlLVDAINadirlqRLQILFSAANGLL-FGLENIL--VIYLGALLVLDGEF 255
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
718-910 |
1.42e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.66 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqkvsGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGpvAYASQK 797
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLM-----------NALAFRSPKGVKGSGSVLLNGMPIDAKEMRAIS--AYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLLNA-TVEENIIFESPF----------NKQRYKMVIEACSLQPDIDILphgdqTQIGERGINLSGGQRQRISVARALY 866
Cdd:TIGR00955 108 DLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCANTR-----IGVPGRVKGLSGGERKRLAFASELL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1189438336 867 QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTH 910
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
714-933 |
1.55e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSeiGEDPSPERETatdLDIRKRgpVAY 793
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG--GRSIFNYRDV---LEFRRR--VGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLLNATVEENIIFESPFNK----QRYKMVIEACSLQPDidiLPHGDQTQIGERGINLSGGQRQRISVARALYQHA 869
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVG---LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 870 NVVFLDDPFSALDIHLSDHlmqagILELLRD--DKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREG 933
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEK-----IEEFIRSlaDRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
718-882 |
1.56e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpDSEIGEDP-SPEretatDLDIRKRGPVAYASQ 796
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGV------EGVITYDGiTPE-----EIKKHYRGDVVYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 797 K----PWLlnaTVEENIIF----ESPFNkqRYKMVIEACSLQPDIDI------LPHGDQTQIGE---RGInlSGGQRQRI 859
Cdd:TIGR00956 146 TdvhfPHL---TVGETLDFaarcKTPQN--RPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRGV--SGGERKRV 218
|
170 180
....*....|....*....|...
gi 1189438336 860 SVARALYQHANVVFLDDPFSALD 882
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1366-1559 |
2.01e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.85 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD-------TFEGHIIIDGIDIAKLPLHT 1438
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevtiTGSIVYNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDPVLFSGTI--------RFNLDPERKCSDSTLWEALEIAQLKLVVKAlpggldaIITEGGENFSQGQRQL 1510
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1559
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
714-913 |
2.07e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.97 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPsperetatdLDIRKRGPVAY 793
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI---IIDDEDISLLP---------LHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLLNA-TVEENI-----IFESPFNKQRYKMVIEacsLQPDIDILPHGDQTqigerGINLSGGQRQRISVARALYQ 867
Cdd:PRK10895 83 LPQEASIFRRlSVYDNLmavlqIRDDLSAEQREDRANE---LMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1189438336 868 HANVVFLDDPFSALD-IHLSDhlmQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:PRK10895 155 NPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1383-1592 |
2.70e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.90 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1383 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV----DTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGT 1456
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpssGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1457 IRFNLDPERKCSDSTLWEALEIAqLKLVVKAlpGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-M 1535
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKA-LKWLKKV--GLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1536 ATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1370-1594 |
2.77e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.69 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1370 NLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIIL 1447
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLfmNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1448 QDP---VLFS---GTIRFNLD----PE----RKCSDS-TLWEALEIAQLKLvvkalpggldaiiteggENFSQGQRQLFC 1512
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRnlgvPEaeitRRVDEAlTLVDAQHFRHQPI-----------------QCLSHGQKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKL 1587
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEV 223
|
....*..
gi 1189438336 1588 LSRKDSV 1594
Cdd:PRK13638 224 FACTEAM 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
804-894 |
2.81e-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: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 804 TVEENI--IFE-SPFNKQRYKMVIEacSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHANVVFLDDPFSA 880
Cdd:COG1137 94 TVEDNIlaVLElRKLSKKEREERLE--ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
90 100
....*....|....*....|.
gi 1189438336 881 LD-IHLSD------HLMQAGI 894
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 ... |
849-912 |
2.83e-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: 2.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 849 INLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL 912
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA-IRRLSEEGKKTALVVEHDL 132
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1084-1247 |
2.91e-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: 48.01 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1084 VYAMVFTVLC--SLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1161
Cdd:cd18780 41 LNQAVLILLGvvLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1162 ECLSRSTLLCVSALAVISYVTP----VFLVALLPLAIVCYFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1236
Cdd:cd18780 121 SMLLRYLVQIIGGLVFMFTTSWkltlVMLSVVPPLSIGAVIYGKYVRKLSKKFQD-----ALAAASTVAEeSISNIRTVR 195
|
170
....*....|.
gi 1189438336 1237 AFRYEARFQQK 1247
Cdd:cd18780 196 SFAKETKEVSR 206
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1474-1599 |
3.43e-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: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1474 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVV 1545
Cdd:TIGR01187 83 EALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkTIQEQLG 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1546 MtafadrTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKDSVF-ASFV 1599
Cdd:TIGR01187 152 I------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1366-1578 |
3.47e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVDTFEGHIIIDGIDIAKlPLHTLRSRL 1443
Cdd:PRK15439 12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSG-TIRFNL--------DPERKCSDstLWEALEiAQLKLVVKAlpGGLDAiiteggenfsqGQRQLFCLA 1514
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENIlfglpkrqASMQKMKQ--LLAALG-CQLDLDSSA--GSLEV-----------ADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1515 RAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
720-935 |
4.50e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQK----VSGAVfwssLPDSEIGEDPSPERetatdldiRKRGpvaY 793
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLinAISGLTRPQKgrivLNGRV----LFDAEKGICLPPEK--------RRIG---Y 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLL-NATVEENIIFE-SPFNKQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQRQRISVARALYQHANV 871
Cdd:PRK11144 81 VFQDARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 872 VFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVL-VTHKLQYLPH-ADWIIAMKDGTIQREGTL 935
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPL 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
852-912 |
4.98e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.41 E-value: 4.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 852 SGGQRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTHKL 912
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 222
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1097-1311 |
6.27e-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: 46.92 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1097 IVLCLVTSVTVEWTGLK------VAKRLH---RSLLNR-IILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSR 1166
Cdd:cd18784 40 IIMGLLAIASSVAAGIRgglftlAMARLNiriRNLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1167 STLLCVSALAVI---SYVTPVFLVALLPL-AIVCYFIQKYFRVASRDLQqlddtTQLPLLSHFA-ETVEGLTTIRAF--- 1238
Cdd:cd18784 120 SLVKAIGVIVFMfklSWQLSLVTLIGLPLiAIVSKVYGDYYKKLSKAVQ-----DSLAKANEVAeETISSIRTVRSFane 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 -----RYEARFQQ-------KLLEYTDSNNIASLFLTAanrwLEVRMEYIGACVVLIAAVTS---ISNSLHR-ELSAGLV 1302
Cdd:cd18784 195 dgeanRYSEKLKDtyklkikEALAYGGYVWSNELTELA----LTVSTLYYGGHLVITGQISGgnlISFILYQlELGSCLE 270
|
250
....*....|
gi 1189438336 1303 GLGLTYA-LM 1311
Cdd:cd18784 271 SVGSVYTgLM 280
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
391-608 |
6.28e-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: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 391 IQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYI---LGVSALIGAAV 466
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTsALTVLVRDPLTVIGLLGVLFYLdwkLTLIALVVLPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 467 IILlaPVQYFvATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FRTRVETTRRKEMTSLRAFAIYTSI 542
Cdd:cd18552 152 AAL--PIRRI-GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 543 SIFMnTAIPIAAVLItFVGHVSFfkEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18552 229 MELL-GAIAIALVLW-YGGYQVI--SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
714-927 |
8.93e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEdpsperetatdldirkrgPVAY 793
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ-------GK------------------EIDF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWLLNA--------------TVEENIIF-----ESPFNKQRyKMVIEACSL--QPDIDILPHgdqtqigERGINLS 852
Cdd:PRK10982 65 KSSKEALENGismvhqelnlvlqrSVMDNMWLgryptKGMFVDQD-KMYRDTKAIfdELDIDIDPR-------AKVATLS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 853 GGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDG 927
Cdd:PRK10982 137 VSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1376-1600 |
9.45e-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: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1376 DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRS-RLSIILQDpv 1451
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQS-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1452 lfsgtirFNLDPERKCSDSTLWeALEIA-------------QLKLVvkALPGGLDAIITEggenFSQGQRQLFCLARAFV 1518
Cdd:cd03294 111 -------FALLPHRTVLENVAF-GLEVQgvpraereeraaeALELV--GLEGWEHKYPDE----LSGGMQQRVGLARALA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1519 RKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLL-SRKDSV 1594
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILtNPANDY 256
|
....*.
gi 1189438336 1595 FASFVR 1600
Cdd:cd03294 257 VREFFR 262
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1366-1599 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAK----LPLHtlRS 1441
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFETPTSGEILLDGKditnLPPH--KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDPVLF-----SGTIRFNLDpERKCSDSTLWEALEiAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARA 1516
Cdd:cd03300 73 PVNTVFQNYALFphltvFENIAFGLR-LKKLPKAEIKERVA-EALDLV------QLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1517 FVRKTSIFIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILSADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
....*...
gi 1189438336 1593 SVF-ASFV 1599
Cdd:cd03300 224 NRFvADFI 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
850-912 |
1.27e-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: 1.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 850 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIhlSDHLMQAGILELLRDDKRTVVLVTHKL 912
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
846-942 |
1.30e-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: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 846 ERGIN-LSGGQRQRISVARAL-YQHANVVF-LDDPfsALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWII 922
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEP--SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|....*.
gi 1189438336 923 AM------KDGTIQREGTLKDFQRSE 942
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILANP 586
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
714-910 |
1.38e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 45.98 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdSEIGEdPSPERETATdldiRKRgpVAY 793
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-------TVLGV-PVPARARLA----RAR--IGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 794 ASQKPWL-LNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVARALYQHANVV 872
Cdd:PRK13536 119 VPQFDNLdLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLL 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 1189438336 873 FLDDPFSALDIHlSDHLMQAGILELLRDDKrTVVLVTH 910
Cdd:PRK13536 195 ILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1366-1589 |
1.49e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.46 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY----DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM---------VDTFEGHIIIDgidia 1432
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlipsegkvyVDGLDTSDEEN----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1433 klpLHTLRSRLSIILQDP------------VLFsGTIRFNLDPE--RKCSDstlwEALEIAQLKLVVKALPGGLdaiite 1498
Cdd:PRK13633 80 ---LWDIRNKAGMVFQNPdnqivativeedVAF-GPENLGIPPEeiRERVD----ESLKKVGMYEYRRHAPHLL------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1499 ggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILSADLVIV 1572
Cdd:PRK13633 146 -----SGGQKQRVAIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIV 216
|
250
....*....|....*..
gi 1189438336 1573 LKRGAILEFDKPEKLLS 1589
Cdd:PRK13633 217 MDSGKVVMEGTPKEIFK 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
720-937 |
1.66e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPEREtatdLDIRKRGpVAYASQKP- 798
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN-------GKDISPRSP----LDAVKKG-MAYITESRr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 799 ---WLLNATVEENIIFESPFNKQRYKMVI----------EACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVARAL 865
Cdd:PRK09700 349 dngFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 866 YQHANVVFLDDPFSALDIHlsdhlMQAGILELLR---DDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVG-----AKAEIYKVMRqlaDDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1365-1589 |
1.73e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 45.00 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1365 KIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDPVLFSG-TIRfNLDPERKCSDSTLWEALEIAQLKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:PRK11231 80 LLPQHHLTPEGiTVR-ELVAYGRSPWLSLWGRLSAEDNARVNQAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1523 IFIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
718-911 |
1.80e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKvsgavfwSSLPDSEIGEDPSPERETatdldIRKRGpvaYASQK 797
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQG-------NNFTGTILANNRKPTKQI-----LKRTG---FVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLL-NATVEENIIFES----PFNKQRYKMVIEACSLQPDIDiLPHGDQTQIGE---RGInlSGGQRQRISVARALYQHA 869
Cdd:PLN03211 149 DILYpHLTVRETLVFCSllrlPKSLTKQEKILVAESVISELG-LTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1189438336 870 NVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHK 911
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLT--LGSLAQKGKTIVTSMHQ 265
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1366-1589 |
1.85e-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: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNAL---IAPGQKIGICGRTGSGKSSFS--LA----------FFRM----VDTFEghiii 1426
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSkiIAgvleptsgevNVRVgdewVDMTK----- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1427 dgidiaklPLHTLRSR----LSIILQDPVLFsgtirfnldPERKCSDStLWEAL------EIAQLKLVVKALPGGLD--- 1493
Cdd:TIGR03269 355 --------PGPDGRGRakryIGILHQEYDLY---------PHRTVLDN-LTEAIglelpdELARMKAVITLKMVGFDeek 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1494 --AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-AD 1568
Cdd:TIGR03269 417 aeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCD 496
|
250 260
....*....|....*....|.
gi 1189438336 1569 LVIVLKRGAILEFDKPEKLLS 1589
Cdd:TIGR03269 497 RAALMRDGKIVKIGDPEEIVE 517
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
715-933 |
2.43e-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: 45.56 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpdsEIGEDPsperetatdLDIRKRGPVAYA 794
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV------RVGDEW---------VDMTKPGPDGRG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 795 SQKPWL----------LNATVEEN----IIFESPFNKQRYKMVI----------EACSLqpdIDILPHgdqtqigergiN 850
Cdd:TIGR03269 362 RAKRYIgilhqeydlyPHRTVLDNlteaIGLELPDELARMKAVItlkmvgfdeeKAEEI---LDKYPD-----------E 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 851 LSGGQRQRISVARALYQHANVVFLDDPFSALD----IHLSDHLMQAGIlELlrddKRTVVLVTHKLQY-LPHADWIIAMK 925
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKARE-EM----EQTFIIVSHDMDFvLDVCDRAALMR 502
|
....*...
gi 1189438336 926 DGTIQREG 933
Cdd:TIGR03269 503 DGKIVKIG 510
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
733-921 |
2.45e-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: 45.70 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 733 IVGQVGCGKSSLLlaalgemqKVSGAVfwsslpDSEI-GED-PSPeretatdlDIRkrgpVAYASQKPWL-LNATVEENI 809
Cdd:TIGR03719 36 VLGLNGAGKSTLL--------RIMAGV------DKDFnGEArPQP--------GIK----VGYLPQEPQLdPTKTVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 810 I-------------------FESP---FNKQRYKM-----VIEAC---SLQPDIDI------LPHGDQtQIGergiNLSG 853
Cdd:TIGR03719 90 EegvaeikdaldrfneisakYAEPdadFDKLAAEQaelqeIIDAAdawDLDSQLEIamdalrCPPWDA-DVT----KLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 854 GQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWI 921
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPGTVVAVTHDRYFLDNvAGWI 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1356-1599 |
2.78e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.21 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1356 IPKNWPDQGK-----IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGID 1430
Cdd:PRK11607 5 IPRPQAKTRKaltplLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEQPTAGQIML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1431 IAKLPLHT--LRSRLSIILQDPVLF-----SGTIRFNLDPERKCSD---STLWEALEIAQLKLVVKALPGGLdaiitegg 1500
Cdd:PRK11607 79 DGVDLSHVppYQRPINMMFQSYALFphmtvEQNIAFGLKQDKLPKAeiaSRVNEMLGLVHMQEFAKRKPHQL-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 enfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKV----VMTAFADRTVVTIAHRvhtilsad 1568
Cdd:PRK11607 151 ---SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrMQLEvvDILERVgvtcVMVTHDQEEAMTMAGR-------- 219
|
250 260 270
....*....|....*....|....*....|..
gi 1189438336 1569 lVIVLKRGAILEFDKPEKLLSRKDSVF-ASFV 1599
Cdd:PRK11607 220 -IAIMNRGKFVQIGEPEEIYEHPTTRYsAEFI 250
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1108-1255 |
2.80e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 44.73 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1108 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVF-L 1186
Cdd:cd18542 64 EKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLtL 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1187 VALLPLAIVCYFIQKYFRVASRDLQQLDDttQLPLLSHFA-ETVEGLTTIRAF---RYE-ARFQQKLLEYTDSN 1255
Cdd:cd18542 144 ISLAIIPFIALFSYVFFKKVRPAFEEIRE--QEGELNTVLqENLTGVRVVKAFareDYEiEKFDKENEEYRDLN 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
718-884 |
2.83e-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: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdsEIGE--------------DPSPE--RETAT 781
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI--------EIGEtvklayvdqsrdalDPNKTvwEEISG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 782 DLDIRKRGPV-----AYASQkpwllnatveeniifespFNkqrYKmvieacslqpdidilpHGDQTQ-IGErginLSGGQ 855
Cdd:TIGR03719 410 GLDIIKLGKReipsrAYVGR------------------FN---FK----------------GSDQQKkVGQ----LSGGE 448
|
170 180
....*....|....*....|....*....
gi 1189438336 856 RQRISVARALYQHANVVFLDDPFSALDIH 884
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1083-1202 |
3.13e-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: 44.77 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID----QHIP 1158
Cdd:cd18577 47 NKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQdgigEKLG 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1159 STLECLSrstlLCVSALaVISYV---------TPVFLVALLPLAIVCYFIQKY 1202
Cdd:cd18577 127 LLIQSLS----TFIAGF-IIAFIyswkltlvlLATLPLIAIVGGIMGKLLSKY 174
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1366-1578 |
3.31e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 44.65 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSL---KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFR---------MVDTFEGHIIidgidiaK 1433
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkptsgkiIIDGVDITDK-------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPLHTLRSRLSIILQDP--VLFSGT----IRF---NLDPERKCSDSTLWEALEIAQLKlvvkalpggLDAIITEGGENFS 1504
Cdd:PRK13637 76 VKLSDIRKKVGLVFQYPeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1505 QGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
851-925 |
3.91e-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: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 851 LSGGQRQRISVARALyQHANV-----VFLDDPFSALDIHLSDHLMQAgILELLrDDKRTVVLVTHKLQYLPHADWIIAMK 925
Cdd:cd03227 78 LSGGEKELSALALIL-ALASLkprplYILDEIDRGLDPRDGQALAEA-ILEHL-VKGAQVIVITHLPELAELADKLIHIK 154
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1392-1585 |
4.29e-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: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1392 PGQKIGICGRTGSGKSSFSLAFFRMVDtfeghiiidgidiaklplhtlrsrlsiilqdpVLFSGTIRFNLDPERKCSDST 1471
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG--------------------------------PPGGGVIYIDGEDILEEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1472 LWEAleiaqlklvvkalpggldaIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAF-- 1549
Cdd:smart00382 49 LLLI-------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1189438336 1550 -----ADRTVVTIAHRVHTILSADLVIVLKRgaILEFDKPE 1585
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPALLRRRFDR--RIVLLLIL 148
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1366-1592 |
4.46e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDP--VLFS---------GTIRFNLDPErkcsdsTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1514
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEE------TVAHRVSSA-LHML------GLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1515 RAFVRKTSIFIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
...
gi 1189438336 1590 RKD 1592
Cdd:PRK13652 228 QPD 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1366-1582 |
5.23e-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: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKL-----PLHtlR 1440
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEPTSGRIYIGGRDvtdlpPKD--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 SrLSIILQDPVLFS-----GTIRFNLD----PERKCSDSTLWEAlEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLF 1511
Cdd:cd03301 73 D-IAMVFQNYALYPhmtvyDNIAFGLKlrkvPKDEIDERVREVA-ELLQIEHLLDRKPKQL-----------SGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1512 CLARAFVRKTSIFIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILSADLVIVLKRGAILEFD 1582
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1390-1572 |
5.34e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.42 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1390 IAPGQKIGICGRTGSGKSSF-SL-AFFRMVDTfeghiiidgidiAKLPL----HTL----RSRLSIILQDPVLFSG-TIR 1458
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLlNLiAGFLTPAS------------GSLTLngqdHTTtppsRRPVSMLFQENNLFSHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1459 FN----LDPERKCSDSTLWEALEIAQ---LKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATA 1531
Cdd:PRK10771 90 QNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1189438336 1532 SIDMATENILQKVVMTAFADR--TVVTIAHRV---HTILSADLVIV 1572
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERqlTLLMVSHSLedaARIAPRSLVVA 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1366-1579 |
5.61e-04 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 43.19 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSsLKpVLKHVNALIAPGQKIGICGRTGSGKSS-FSL-----------AFFRMVDTfeghiiidgidiAK 1433
Cdd:cd03219 1 LEVRGLTKRFGG-LV-ALDDVSFSVRPGEIHGLIGPNGAGKTTlFNLisgflrptsgsVLFDGEDI------------TG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPLHtLRSRLSII--LQDPVLFSG-TIRFNL-------------DPERKCSDSTLWE-ALEIaqLKLVvkalpgGLDAII 1496
Cdd:cd03219 67 LPPH-EIARLGIGrtFQIPRLFPElTVLENVmvaaqartgsgllLARARREEREARErAEEL--LERV------GLADLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1497 TEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLK 1574
Cdd:cd03219 138 DRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLD 217
|
....*
gi 1189438336 1575 RGAIL 1579
Cdd:cd03219 218 QGRVI 222
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
445-561 |
5.93e-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: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 445 IIVGVILLYY--ILGVSALIGAAVIILLApvqYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAW 514
Cdd:cd18555 130 VIYLIYMLYYspLLTLIVLLLGLLIVLLL---LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKslgsekniYKKW 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1189438336 515 ENIFRTRVETTRRKEMTSlrafAIYTSISIFMNTAIPIaavLITFVG 561
Cdd:cd18555 207 ENLFKKQLKAFKKKERLS----NILNSISSSIQFIAPL---LILWIG 246
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
718-912 |
6.07e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.56 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQkvsgavfwsslPDSEIGEDPSPERetatdldirkrgpVAYASQK 797
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA-----------PDEGVIKRNGKLR-------------IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 798 PWLlNATVeeniifesPFNKQRYKMvieacsLQPDI---DILPHGDQTQIGERgIN-----LSGGQRQRISVARALYQHA 869
Cdd:PRK09544 76 LYL-DTTL--------PLTVNRFLR------LRPGTkkeDILPALKRVQAGHL-IDapmqkLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1189438336 870 NVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRT----VVLVTHKL 912
Cdd:PRK09544 140 QLLVLDEPTQGVDVN-----GQVALYDLIDQLRREldcaVLMVSHDL 181
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
712-929 |
8.00e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.86 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGED---PSPERetatdldIRKR 788
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD-------GEDitgLSPRE-------RRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 789 GpVAYASQKPW----LLNATVEENIIFES----PFNK----QRYKMVIEACSLQPDIDILPHGDQTQIGergiNLSGGQR 856
Cdd:COG3845 334 G-VAYIPEDRLgrglVPDMSVAENLILGRyrrpPFSRggflDRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILElLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTI 929
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQR-LLE-LRDAGAAVLLISEDLDeILALSDRIAVMYEGRI 480
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1366-1407 |
9.32e-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: 9.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1366 IQIQNLSVRY------DSSLK--------------PVLKHVNALIAPGQKIGICGRTGSGKS 1407
Cdd:COG1134 5 IEVENVSKSYrlyhepSRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKS 66
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1366-1592 |
1.16e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 42.91 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD--TFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpsSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDP--VLFSGTIRFNLdperkcsdstlweALEIAQLKLVVKALPGGLDAIITEGG---------ENFSQGQRQLFC 1512
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDV-------------SFGAVNLKLPEDEVRKRVDNALKRTGiehlkdkptHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1513 LARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LSADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFA 231
|
...
gi 1189438336 1590 RKD 1592
Cdd:PRK13636 232 EKE 234
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1117-1248 |
1.26e-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: 42.85 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1117 RLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIdQHIPSTLECLSRSTLLCVSALAVISYVTP----VFLVALLPL 1192
Cdd:cd18543 73 DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPplalVALASLPPL 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1193 AIVCYFIQKYFRVASRDLQQL--DDTTqlpllsHFAETVEGLTTIRAFRYEARFQQKL 1248
Cdd:cd18543 152 VLVARRFRRRYFPASRRAQDQagDLAT------VVEESVTGIRVVKAFGRERRELDRF 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1501-1578 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDG 216
|
..
gi 1189438336 1577 AI 1578
Cdd:COG1129 217 RL 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
846-912 |
1.30e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 846 ERGI-NLSGGQRQRISVARALYQHANVVFLDDPFSALDIH--LSdhlMQAGILELLRDdkRTVVLVTHKL 912
Cdd:PRK13409 207 DRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrLN---VARLIRELAEG--KYVLVVEHDL 271
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1366-1409 |
1.40e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 42.45 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1409
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTL 44
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1083-1254 |
1.40e-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: 42.58 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPSTLE 1162
Cdd:cd18782 42 YVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAV-ISYVTPVFLVAL--LPLAIVCYF---------IQKYFRVASRdlqqlddtTQlpllSHFAETVE 1230
Cdd:cd18782 121 TTLLDVLFSVIYIAVlFSYSPLLTLVVLatVPLQLLLTFlfgpilrrqIRRRAEASAK--------TQ----SYLVESLT 188
|
170 180
....*....|....*....|....*
gi 1189438336 1231 GLTTIRAFRYEARFQQKLLE-YTDS 1254
Cdd:cd18782 189 GIQTVKAQNAELKARWRWQNrYARS 213
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
730-910 |
1.60e-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: 41.87 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 730 LTMIVGQVGCGKSSLLLAalgemqkVSGAVFwsslpdseiGEDPSPERETATDLDIrkrgpvayasqkpwllnATVEE-- 807
Cdd:cd03279 30 LFLICGPTGAGKSTILDA-------ITYALY---------GKTPRYGRQENLRSVF-----------------APGEDta 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 808 NIIFESPFNKQRYKmVIEACSLQPD----IDILPHGDQTQIGERGI-NLSGGQRQRISVARAL------YQHANVV---- 872
Cdd:cd03279 77 EVSFTFQLGGKKYR-VERSRGLDYDqftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevlQNRGGARleal 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1189438336 873 FLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTH 910
Cdd:cd03279 156 FIDEGFGTLDPEALEAVATA--LELIRTENRMVGVISH 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1366-1599 |
1.62e-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: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAK-LPLHTLRSR-L 1443
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAGLERPDSGTILFGGEdATDVPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLF-----SGTIRFNLDPERKcsdSTLWEALEIAQ-----LKLVvkalpgGLDAIITEGGENFSQGQRQLFCL 1513
Cdd:cd03296 77 GFVFQHYALFrhmtvFDNVAFGLRVKPR---SERPPEAEIRAkvhelLKLV------QLDWLADRYPAQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1514 ARAFVRKTSIFIMDEATASIDMATENILQKVVmTAFADRTVVT---IAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|.
gi 1189438336 1590 RKDSVF-ASFV 1599
Cdd:cd03296 227 HPASPFvYSFL 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1366-1600 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSsfSLAffRM-------------VDTFEghiiidgid 1430
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS--TLI--RCinllerptsgsvlVDGVD--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1431 IAKLP---LHTLRSRLSIILQDpvlfsgtirFNLDPERkcsdsTLWE----ALEIAQ-------------LKLV-----V 1485
Cdd:COG1135 69 LTALSereLRAARRKIGMIFQH---------FNLLSSR-----TVAEnvalPLEIAGvpkaeirkrvaelLELVglsdkA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1486 KALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENIL---QKVvmtafADR---TVVTIA 1558
Cdd:COG1135 135 DAYPSQL-----------SGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILdllKDI-----NRElglTIVLIT 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1189438336 1559 HRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKDSVFA-SFVR 1600
Cdd:COG1135 199 HEMDVVRRiCDRVAVLENGRIVEQGPVLDVFANPQSELTrRFLP 242
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1380-1594 |
1.87e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.94 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1380 KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKlplHTLRsRLSIILQDPVLFSG-T 1456
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYPHlT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1457 IRFNLdpeRKCSDSTLWEALEiAQLKLVVKalpgglDAIITEGG----EN----------FSQGQRQLFCLARAFVRKTS 1522
Cdd:PLN03211 157 VRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1523 IFIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILsaDLVIVLKRGAILEFDKPEKLLSRKDSV 1594
Cdd:PLN03211 227 LLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1085-1247 |
2.15e-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: 42.05 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1085 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFF---ETTPlGSILNRFSSDCNTI----DQHI 1157
Cdd:cd18578 54 WALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddpENST-GALTSRLSTDASDVrglvGDRL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1158 PSTLECLsrSTLLCVSALAVISY--VTPVfLVALLPLAIVCYFIQKYF--RVASRDLQQLDDTTQLpllshFAETVEGLT 1233
Cdd:cd18578 133 GLILQAI--VTLVAGLIIAFVYGwkLALV-GLATVPLLLLAGYLRMRLlsGFEEKNKKAYEESSKI-----ASEAVSNIR 204
|
170
....*....|....
gi 1189438336 1234 TIRAFRYEARFQQK 1247
Cdd:cd18578 205 TVASLTLEDYFLEK 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
838-957 |
2.22e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 838 HGDQ-TQIGERginLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTHKLQYL- 915
Cdd:PRK10636 420 QGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVSHDRHLLr 491
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1189438336 916 PHADWIIAMKDGTIQR-EGTLKDFQRsecqlfehWKTLMNRQD 957
Cdd:PRK10636 492 STTDDLYLVHDGKVEPfDGDLEDYQQ--------WLSDVQKQE 526
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
851-934 |
2.31e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 851 LSGGQRQRISVARALYQHAN---VVFLDDPFSAL---DIHlsdHLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAM 924
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIR---KLLE--VLHRLVDKGNTVVVIEHNLDVIKTADWIIDL 905
|
90
....*....|....*.
gi 1189438336 925 ------KDGTIQREGT 934
Cdd:PRK00349 906 gpeggdGGGEIVATGT 921
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
844-935 |
2.44e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 844 IGERGINLSGGQRQRISVARALY---QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADW 920
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLV--QLRTLVSLGHSVIYIDHDPALLKQADY 1770
|
90
....*....|....*
gi 1189438336 921 IIAMKDGTIQREGTL 935
Cdd:PRK00635 1771 LIEMGPGSGKTGGKI 1785
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1366-1580 |
2.50e-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: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKlPL------- 1436
Cdd:PRK11264 4 IEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTIRVGDITIDTAR-SLsqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1437 HTLRSRLSIILQDpvlfsgtirFNLDPERKcsdstlweALE-IAQLKLVVKALPGG---------LDAIITEGGEN---- 1502
Cdd:PRK11264 81 RQLRQHVGFVFQN---------FNLFPHRT--------VLEnIIEGPVIVKGEPKEeatararelLAKVGLAGKETsypr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1503 -FSQGQRQLFCLARAFVRKTSIFIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:PRK11264 144 rLSGGQQQRVAIARALAMRPEVILFDEPTSALDpeLVGE-VLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
..
gi 1189438336 1579 LE 1580
Cdd:PRK11264 223 VE 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
852-915 |
2.77e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 852 SGGQRQRISVARALYQHANVVFLDDPFSALDIH----LSDHLMQAgilellrddKRTVVLVTHKLQYL 915
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKW---------PKTFIVVSHAREFL 404
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
849-930 |
2.80e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.27 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 849 INLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
..
gi 1189438336 929 IQ 930
Cdd:PRK10522 527 LS 528
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1373-1573 |
2.91e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 41.24 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1373 VRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVL 1452
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1453 FSGTIRFNL-----------DPERKCSDstlwealeiaqlkLVVKALPgglDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:PRK10247 93 FGDTVYDNLifpwqirnqqpDPAIFLDD-------------LERFALP---DTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1522 SIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVL 1573
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1111-1255 |
3.19e-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: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCntidQHIPSTLE-CLS---RSTLL---CVSALAVISYVTP 1183
Cdd:cd18574 70 GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV----QEFKSSFKqCVSqglRSVTQtvgCVVSLYLISPKLT 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1184 VFLVALLPLAIVC-YFIQKYFRVASRDLQQLDDTTqlplLSHFAETVEGLTTIRAFRYEAR----FQQKLLEYTDSN 1255
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 ... |
1079-1247 |
3.50e-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: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 TLDQTVYAMVFTVLCSlgIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIP 1158
Cdd:cd18566 40 TLQVLVIGVVIAILLE--SLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1159 stleclSRSTLLCVSALAVISYVTPVF----------LVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAET 1228
Cdd:cd18566 117 ------GQALLALLDLPFVLIFLGLIWylggklvlvpLVLLGLFVLVAILLGPILRRALKERSRADERRQ----NFLIET 186
|
170
....*....|....*....
gi 1189438336 1229 VEGLTTIRAFRYEARFQQK 1247
Cdd:cd18566 187 LTGIHTIKAMAMEPQMLRR 205
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
846-922 |
3.84e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 846 ERGIN-LSGGQRQRISVARALYQHANVV--FLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWII 922
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 ... |
1388-1543 |
4.44e-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: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1388 ALIAPGQKIGICGRTGSGKSSF--SLAFFRMVD--TFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL- 1461
Cdd:cd03297 18 DFDLNEEVTGIFGASGAGKSTLlrCIAGLEKPDggTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHlNVRENLa 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1462 -------DPERKCSDSTLWEALEIAQLKlvvKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID 1534
Cdd:cd03297 98 fglkrkrNREDRISVDELLDLLGLDHLL---NRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
....*....
gi 1189438336 1535 MATENILQK 1543
Cdd:cd03297 164 RALRLQLLP 172
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
378-561 |
4.46e-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: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 378 YVAIETGINLRgaiqTKIYNKIMHLSTSNlsMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAM-PVQIIVGVILLYYIL 456
Cdd:cd18548 65 KASQGFGRDLR----KDLFEKIQSFSFAE--IDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRaPIMLIGAIIMAFRIN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 457 GVSALIGAAVIILLAPVQYFVATK---LSQAQRSTLEYSNERLKqtnEMLRGIKLLKLYAWENIFRTRVETTRRKEM-TS 532
Cdd:cd18548 139 PKLALILLVAIPILALVVFLIMKKaipLFKKVQKKLDRLNRVVR---ENLTGIRVIRAFNREDYEEERFDKANDDLTdTS 215
|
170 180
....*....|....*....|....*....
gi 1189438336 533 LRAFAIYTSISIFMNTAIPIAAVLITFVG 561
Cdd:cd18548 216 LKAGRLMALLNPLMMLIMNLAIVAILWFG 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1366-1407 |
6.70e-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: 6.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1189438336 1366 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKS 1407
Cdd:COG4172 7 LSVEDLSVAFgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKS 50
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1366-1535 |
6.87e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 40.44 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY-------DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSfsLAffRMVDTFEGHIIIDGIDIAKlPLHT 1438
Cdd:PRK10419 4 LNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKST--LA--RLLVGLESPSQGNVSWRGE-PLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 L--------RSRLSIILQDP---VLFSGTIRFNLD-PERKCSDstLWEALEIAQLKLVVKALpgGLDA-IITEGGENFSQ 1505
Cdd:PRK10419 79 LnraqrkafRRDIQMVFQDSisaVNPRKTVREIIRePLRHLLS--LDKAERLARASEMLRAV--DLDDsVLDKRPPQLSG 154
|
170 180 190
....*....|....*....|....*....|
gi 1189438336 1506 GQRQLFCLARAFVRKTSIFIMDEATASIDM 1535
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1091-1266 |
6.99e-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: 40.46 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1091 VLCSLGIVLC-LVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTL 1169
Cdd:cd18548 46 LLLALLGLIAgILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI 125
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1170 LCVSALAVISYVTP----VFLVALLPLAIVCYFIQKYFRVASRDLQ-QLDDTTQLpllshFAETVEGLTTIRAF---RYE 1241
Cdd:cd18548 126 MLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKAIPLFKKVQkKLDRLNRV-----VRENLTGIRVIRAFnreDYE 200
|
170 180
....*....|....*....|....*.
gi 1189438336 1242 -ARFQQKLLEYTDsNNIASLFLTAAN 1266
Cdd:cd18548 201 eERFDKANDDLTD-TSLKAGRLMALL 225
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| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
839-927 |
8.58e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 839 GDQTQIGergiNLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHA 918
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGIT 458
|
....*....
gi 1189438336 919 DWIIAMKDG 927
Cdd:PRK10982 459 DRILVMSNG 467
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
846-937 |
8.85e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 39.92 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 846 ERGIN-LSGGQRQRISVARALYQ-------HANVVFLDDPFSALDI-------HLSDHLMQAGIlellrddkrTVVLVTH 910
Cdd:PRK03695 121 GRSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVaqqaaldRLLSELCQQGI---------AVVMSSH 191
|
90 100
....*....|....*....|....*...
gi 1189438336 911 KLQY-LPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK03695 192 DLNHtLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1366-1412 |
9.75e-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: 9.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLA 1412
Cdd:cd03217 1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKT 45
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