|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
100-1424 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 909.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 100 PVDNAGLFSYMTFSWLSPLAQVVHKKgELLMEDVWPLSKYESSDVNCRRLERLWQEELNEVGP-DAASLRRVVWifcrTR 178
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKR-PLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKPwLLRALNNSLG----GR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 179 LILSIVCLMITQLAGFSGPaFVVKHLLEYTQATESNLQ---YSLLlvlglllteVVRSWSLALTWALNY-----RTGVRL 250
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVGP-LLLNLLLESMQNGEPAWIgyiYAFS---------IFVGVVLGVLCEAQYfqnvmRVGFRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 251 RGAVLTMAFKKILKLKNIKEKSL--GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFIL 328
Cdd:PLN03130 373 RSTLVAAVFRKSLRLTHEGRKKFtsGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 329 FYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPI 408
Cdd:PLN03130 453 MFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 409 VVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIKNKPASPHI 488
Cdd:PLN03130 533 IPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 489 -KIEMKNATLAWDsshsstqsspkltpkvkkdkraPKGkkeksrqlqhtehqavlaeqkghllldsdERPspeeeegkqi 567
Cdd:PLN03130 613 pAISIKNGYFSWD----------------------SKA-----------------------------ERP---------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 568 hagsmrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQM-TLLEGSIAVSGTFAYVAQQAWILNATLRDNILFG 646
Cdd:PLN03130 632 ---------TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFG 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 647 KEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNS 726
Cdd:PLN03130 703 SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 727 AIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLL-----LGET--PPVEINSKKE 799
Cdd:PLN03130 783 CIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG---PLFQKLMenagkMEEYveENGEEEDDQT 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 800 ASGSQKSQDKGPKPGSVKKEKAVKSEEGQLVQVEEKGQGSVPWSVYWVYIQAAGGplaFLVIMVLFMLNVGSTAF---ST 876
Cdd:PLN03130 859 SSKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGG---AWVVMILFLCYVLTEVFrvsSS 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 877 WWLSYWIKQGSGNStvfegnrssvsdsmrDNPFlqYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILR 956
Cdd:PLN03130 936 TWLSEWTDQGTPKT---------------HGPL--FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILR 998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 957 SPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNV---ILVFFCVGMIAGVFPWflvAVGPLLILFSVLHIVSRV 1033
Cdd:PLN03130 999 APMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIfqlLSTFVLIGIVSTISLW---AIMPLLVLFYGAYLYYQS 1075
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1034 LIRELKRLDNITQSPFLSHITSSIQGLATIHAYnKRQEFLHRYQELLDDNQAPFFLFT-CAMRWLAVRLDLISIALITTT 1112
Cdd:PLN03130 1076 TAREVKRLDSITRSPVYAQFGEALNGLSTIRAY-KAYDRMAEINGRSMDNNIRFTLVNmSSNRWLAIRLETLGGLMIWLT 1154
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1113 GLMIVLMHGQI--PSAYA---GLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKAPPHDWP 1187
Cdd:PLN03130 1155 ASFAVMQNGRAenQAAFAstmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYID-LPSEAPLVIENNRPPPGWP 1233
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1188 QEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS 1267
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1268 KLTIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHC 1347
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1348 KILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 1424
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
90-1428 |
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: 885.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 90 PFRTTTKHQ---HPVDNAGLFSYMTFSWLSPLAqVVHKKGELLMEDVWPLSKYESSDVNCRRLERLWQEE---------- 156
Cdd:TIGR00957 190 PLFSETNHDpnpCPESSASFLSRITFWWITGMA-VYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKEckktrkqpvs 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 157 ----------------LNEVGPDAA------------SLRRVVWIFCRTRLILSIVCLMITQLAGFSGPAfVVKHLLEYT 208
Cdd:TIGR00957 269 avygkkdpskpkgssqLDANEEVEAlivksphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQ-ILSLLIRFV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 209 QATESNLQYSLLLVLGLLLTEVVRSWSLALTWALNYRTGVRLRGAVLTMAFKKILKLKNIKEKS--LGELINICSNDGQR 286
Cdd:TIGR00957 348 NDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSstVGEIVNLMSVDAQR 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 287 MFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIK 366
Cdd:TIGR00957 428 FMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIK 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 367 FIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMT 444
Cdd:TIGR00957 508 VLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILR 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 445 FALKVTPFSVKSLSEASVAVDRFKSLFLMEEV--HMIKNKPASP--HIKIEMKNATLAWDsshsstqsspkltpkvkkdk 520
Cdd:TIGR00957 588 FPLNILPMVISSIVQASVSLKRLRIFLSHEELepDSIERRTIKPgeGNSITVHNATFTWA-------------------- 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 521 rapkgkkeksrqlqhtehqavlaeqkghllldSDERPspeeeegkqihagsmrlqrTLYNIDLEIEEGKLVGICGSVGSG 600
Cdd:TIGR00957 648 --------------------------------RDLPP-------------------TLNGITFSIPEGALVAVVGQVGCG 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 601 KTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGE 680
Cdd:TIGR00957 677 KSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGE 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 681 RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKR--LKSKTVLFVTHQLQYLVDCDEVIFMKE 758
Cdd:TIGR00957 757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvLKNKTRILVTHGISYLPQVDVIIVMSG 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 759 GCITERGTHEELMNLNGDYATIFNNLLLGET--------PPVEINSKKEA----------------------SGSQKSQD 808
Cdd:TIGR00957 837 GKISEMGSYQELLQRDGAFAEFLRTYAPDEQqghledswTALVSGEGKEAkliengmlvtdvvgkqlqrqlsASSSDSGD 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 809 KGPKPGSVKK-EKA-VKSEEGQLVQVEEKGQGSVPWSVYWVYIQAAGGPLAFLVIMvLFMLNVGSTAFSTWWLSYWIKQG 886
Cdd:TIGR00957 917 QSRHHGSSAElQKAeAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIF-LFVCNHVSALASNYWLSLWTDDP 995
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 887 SGNSTVFEGN-RSSVSDSMrdnPFLQYYAsIYALSMAVMLilkairgvvfvkGTLRASSRLHDELFRRILRSPMKFFDTT 965
Cdd:TIGR00957 996 MVNGTQNNTSlRLSVYGAL---GILQGFA-VFGYSMAVSI------------GGIQASRVLHQDLLHNKLRSPMSFFERT 1059
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 966 PTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLLILFSVLHIVSRVLIRELKRLDNIT 1045
Cdd:TIGR00957 1060 PSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVS 1139
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1046 QSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPS 1125
Cdd:TIGR00957 1140 RSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSA 1219
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1126 AYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKTlSLEAPARIKNKAPPHDWPQEGEITFENAEMRYRENL 1205
Cdd:TIGR00957 1220 GLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDL 1298
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1206 PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRS 1285
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRM 1378
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 NLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDL 1365
Cdd:TIGR00957 1379 NLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1366 LIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNdSSRFYAMCAAA 1428
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ-RGIFYSMAKDA 1520
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
100-1424 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 850.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 100 PVDNAGLFSYMTFSWLSPLAQVVHKKgELLMEDVWPLSKYESSDVNCRRLERLWQEELNEVGPdaaSLRRVVWIFCRTRL 179
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRK-PITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKP---WLLRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 180 ILSIVCLMITQLAGFSGPAfVVKHLLEYTQATES---NLQYSLLLVLGLLLTEVVRSWSLALTWalnyRTGVRLRGAVLT 256
Cdd:PLN03232 304 WLGGIFKIGHDLSQFVGPV-ILSHLLQSMQEGDPawvGYVYAFLIFFGVTFGVLCESQYFQNVG----RVGFRLRSTLVA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 257 MAFKKILKLKNIKEKSL--GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMM 334
Cdd:PLN03232 379 AIFHKSLRLTHEARKNFasGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 335 FVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKA---GYFQSITVGVAPIVVv 411
Cdd:PLN03232 459 LIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAqllSAFNSFILNSIPVVV- 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 412 iaSVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIKNKPASPHI-KI 490
Cdd:PLN03232 538 --TLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGApAI 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 491 EMKNATLAWDSSHsstqsspkltpkvkkdkrapkgkkeksrqlqhtehqavlaeqkghllldsdERPspeeeegkqihag 570
Cdd:PLN03232 616 SIKNGYFSWDSKT---------------------------------------------------SKP------------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 571 smrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLE-GSIAVSGTFAYVAQQAWILNATLRDNILFGKEF 649
Cdd:PLN03232 632 ------TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDF 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 650 DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR 729
Cdd:PLN03232 706 ESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 730 KRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLLlgetppvEINSKKEASGSQKSQD- 808
Cdd:PLN03232 786 DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SG---SLFKKLM-------ENAGKMDATQEVNTNDe 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 809 ----KGPKP---------GSVKKEKAVKSeegQLVQVEEKGQGSVPWSVYWVYIQAAGGplaFLVIMVLFMLNVGSTAF- 874
Cdd:PLN03232 855 nilkLGPTVtidvsernlGSTKQGKRGRS---VLVKQEERETGIISWNVLMRYNKAVGG---LWVVMILLVCYLTTEVLr 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 875 --STWWLSYWIKQgsgnstvfegnrsSVSDSMRDNpflqYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFR 952
Cdd:PLN03232 929 vsSSTWLSIWTDQ-------------STPKSYSPG----FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 953 RILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ---NVILVFFCVGMIAGVFPWflvAVGPLLILFSVLHI 1029
Cdd:PLN03232 992 SILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNqlwQLLSTFALIGTVSTISLW---AIMPLLILFYAAYL 1068
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1030 VSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYnKRQEFLHRYQELLDDNQAPFFLFTCAM-RWLAVRLDLISIAL 1108
Cdd:PLN03232 1069 YYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRMAKINGKSMDNNIRFTLANTSSnRWLTIRLETLGGVM 1147
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1109 ITTTGLMIVLMHGQIP-----SAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKAPP 1183
Cdd:PLN03232 1148 IWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID-LPSEATAIIENNRPV 1226
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1184 HDWPQEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLA 1263
Cdd:PLN03232 1227 SGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLT 1306
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1264 DLRSKLTIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARAL 1343
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1344 LRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYA 1423
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
.
gi 16758936 1424 M 1424
Cdd:PLN03232 1467 M 1467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
164-1433 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 663.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 164 AASLRRVVWIFCRTRLILSIVCLMItqlagfsgpAFVVKHLLEYTQATESNLQYSLLLVLGLLLTEVVRSWSLALTWALN 243
Cdd:PTZ00243 239 FAALPYYVWWQIPFKLLSDVCTLTL---------PVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYIS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 244 YRTGVRLRGAVLTM----AFKKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTG 319
Cdd:PTZ00243 310 IRCGLQYRSALNALifekCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 320 FLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQ 399
Cdd:PTZ00243 390 LMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLAR 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 400 SIT--VGVAPIVVVIASVvtFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFkSLFL----- 472
Cdd:PTZ00243 470 VATsfVNNATPTLMIAVV--FTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRI-STFLecdna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 473 -------MEE-VHMIKNKPASPHIKIEMKNAtlawDSSHSSTQSSPkLTPKVKKD--KRA----------PKGKKEKSRQ 532
Cdd:PTZ00243 547 tcstvqdMEEyWREQREHSTACQLAAVLENV----DVTAFVPVKLP-RAPKVKTSllSRAlrmlcceqcrPTKRHPSPSV 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 533 LQHTEHQAVLAEQKGHLLLD-----SDERPSPEEEEGKQIHAGSMRLQ----RTLYNIDLEIEEGKLVGICGSVGSGKTS 603
Cdd:PTZ00243 622 VVEDTDYGSPSSASRHIVEGgtgggHEATPTSERSAKTPKMKTDDFFElepkVLLRDVSVSVPRGKLTVVLGATGSGKST 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 604 LISAILGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGA 683
Cdd:PTZ00243 702 LLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGV 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 684 NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:PTZ00243 782 NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEF 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 764 RGTHEELMNlngdyATIFNNLLLGET---PPVEINSKKEASGSQKSQDKG--PKPGSVKKEKAVKSEE--------GQLV 830
Cdd:PTZ00243 862 SGSSADFMR-----TSLYATLAAELKenkDSKEGDADAEVAEVDAAPGGAvdHEPPVAKQEGNAEGGDgaaldaaaGRLM 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 831 QVEEKGQGSVPWSVYWVYIQAAGGPLAFLVIMVLFMLNVGSTAFSTWWLSYWikqgsgnSTvfegNRSSVSDSMrdnpfl 910
Cdd:PTZ00243 937 TREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMW-------ST----RSFKLSAAT------ 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 911 qyYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPfqae 990
Cdd:PTZ00243 1000 --YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLP---- 1073
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 991 MFIQNVILVFF--CVGMIAGVF--PWFLVAVGPLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAY 1066
Cdd:PTZ00243 1074 MSYLYLLQCLFsiCSSILVTSAsqPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAY 1153
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1067 NKR----QEFLHRyqelLDDNQAPFFLFTCAMRWLAVRLDLIS------IALITTTGLMIVLMHGQIpsAYAGLAISYAV 1136
Cdd:PTZ00243 1154 GKAhlvmQEALRR----LDVVYSCSYLENVANRWLGVRVEFLSnivvtvIALIGVIGTMLRATSQEI--GLVSLSLTMAM 1227
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1137 QLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEA-----------------------PARIKNKAPPHDWP---QEG 1190
Cdd:PTZ00243 1228 QTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDmpeldeevdalerrtgmaadvtgTVVIEPASPTSAAPhpvQAG 1307
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1191 EITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLT 1270
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1271 IIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKIL 1350
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGF 1467
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1351 IL-DEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMCAAAE 1429
Cdd:PTZ00243 1468 ILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALG 1547
|
....
gi 16758936 1430 NKVA 1433
Cdd:PTZ00243 1548 RSEA 1551
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
854-1166 |
1.96e-179 |
|
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: 535.22 E-value: 1.96e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 854 GPLAFLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVFEGNRSSVSDSMRDNPFLQYYASIYALSMAVMLILKAIRGV 933
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 934 VFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWF 1013
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1014 LVAVGPLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCA 1093
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1094 MRWLAVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1166
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
100-1429 |
2.59e-157 |
|
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: 514.84 E-value: 2.59e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 100 PVDNAGLFSYMTFSWLSPLAQVVHKKgELLMEDVWPLSKYESSDVNCRRLERLWQEELNEVGPDAA---SLRRV-VWIFC 175
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQ-KLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKllnALRRCfFWRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 176 RTRLILSIVCLMIT---QLAGFSGPAFVVKHLLEYTQATESNLQYSLLLvlglllteVVRSWSLALTWALNYRTGVRLRG 252
Cdd:TIGR01271 84 FYGILLYFGEATKAvqpLLLGRIIASYDPFNAPEREIAYYLALGLCLLF--------IVRTLLLHPAIFGLHHLGMQMRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 253 AVLTMAFKKILKLKNIK--EKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAIL--GMIYNviILGPTGFLGSAVFIL 328
Cdd:TIGR01271 156 ALFSLIYKKTLKLSSRVldKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILlmGLIWE--LLEVNGFCGLGFLIL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 329 FYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAG---YFQSITVGV 405
Cdd:TIGR01271 234 LALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAylrYFYSSAFFF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 406 APIVVVIASVVTFSVHMTLgfdlTAAQAFTvvTVFNSMTFALKVT---PFSVKSLSEASVAVDRFKSLFLMEEVHMIKNK 482
Cdd:TIGR01271 314 SGFFVVFLSVVPYALIKGI----ILRRIFT--TISYCIVLRMTVTrqfPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 483 PASPhiKIEMKNATLAWDSSHSstqsspKLTPKVKKDkrapkgkkeksrqlqhtehqavlaeqkghllldSDERPSPEEE 562
Cdd:TIGR01271 388 LTTT--EVEMVNVTASWDEGIG------ELFEKIKQN---------------------------------NKARKQPNGD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 563 EGKQIHAGSMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDN 642
Cdd:TIGR01271 427 DGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDN 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 723 IFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF-------------NNLLLGET 789
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerRNSILTET 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 790 -------------------------PPVEINSKKEAS-----------------GSQKSQ-----DKGPKPGSVKKEKAV 822
Cdd:TIGR01271 667 lrrvsidgdstvfsgpetikqsfkqPPPEFAEKRKQSiilnpiasarkfsfvqmGPQKAQattieDAVREPSERKFSLVP 746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 823 KSEEG-------------------------QLVQVEEKGQG--------------------------------------- 838
Cdd:TIGR01271 747 EDEQGeeslprgnqyhhglqhqaqrrqsvlQLMTHSNRGENrreqlqtsfrkkssitqqnelaseldiysrrlskdsvye 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 839 -------------------SVP----WSVYWVYIqAAGGPLAFLVI--MVLFMLNVGSTAFSTWWLSywikqGSGNSTVF 893
Cdd:TIGR01271 827 iseeineedlkecfadereNVFetttWNTYLRYI-TTNRNLVFVLIfcLVIFLAEVAASLLGLWLIT-----DNPSAPNY 900
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 894 EGNRSSVSDSMRD------NPFLQYYA-SIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTP 966
Cdd:TIGR01271 901 VDQQHANASSPDVqkpviiTPTSAYYIfYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMK 980
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 967 TGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLLILFSVLHIVSRVLIRELKRLDNITQ 1046
Cdd:TIGR01271 981 AGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEAR 1060
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1047 SPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPSA 1126
Cdd:TIGR01271 1061 SPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGE 1140
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1127 yAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI-------------KTLSLEAPARIKNKAPPHDWPQEGEIT 1193
Cdd:TIGR01271 1141 -VGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIdlpqeeprpsgggGKYQLSTVLVIENPHAQKCWPSGGQMD 1219
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1194 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKLTIIP 1273
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE-IQIDGVSWNSVTLQTWRKAFGVIP 1298
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1274 QEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILD 1353
Cdd:TIGR01271 1299 QKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1354 EATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMCAAAE 1429
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAMSAAD 1453
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1190-1410 |
2.06e-136 |
|
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: 417.67 E-value: 2.06e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1190 GEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1269
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1349
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1350 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 1410
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
181-467 |
1.36e-134 |
|
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: 415.42 E-value: 1.36e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 181 LSIVCLMITQLAGFSGPAFVVKHLLEYTQATESNLQYSLLLVLGLLLTEVVRSWSLALTWALNYRTGVRLRGAVLTMAFK 260
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 261 KILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLT 340
Cdd:cd18592 81 KILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 341 AYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSV 420
Cdd:cd18592 161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16758936 421 HMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRF 467
Cdd:cd18592 241 HVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
905-1427 |
1.43e-114 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 372.58 E-value: 1.43e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 905 RDNPFLQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVR 984
Cdd:COG1132 55 GDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 985 LPFQAEMFIQNVILVFFCVGMIAGVFPWF-LVAVGPLLILFSVLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLATI 1063
Cdd:COG1132 135 LAHGLPQLVRSVVTLIGALVVLFVIDWRLaLIVLLVLPLLLLVLRLFGR-RLRKLFRRVQEALAELNGRLQESLSGIRVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1064 HAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLI---SIALITTTGLMIVLmHGQIPSAYAGLAISYAVQLTG 1140
Cdd:COG1132 214 KAFGREERELERFREANEELRRANLRAARLSALFFPLMELLgnlGLALVLLVGGLLVL-SGSLTVGDLVAFILYLLRLFG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1141 LFQFTVRLASETEARFTSVERINHYiktlsLEAPARIKNKAPPHD-WPQEGEITFENAEMRYRENLPlVLKKVSFTIKPK 1219
Cdd:COG1132 293 PLRQLANVLNQLQRALASAERIFEL-----LDEPPEIPDPPGAVPlPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1220 EKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL---DPfnQYTEE 1296
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1297 QIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFA 1376
Cdd:COG1132 445 EVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK 524
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1377 DCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMCAA 1427
Cdd:COG1132 525 GRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG-GLYARLYRL 574
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
577-759 |
7.93e-109 |
|
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: 342.53 E-value: 7.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNS 656
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 657 VLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLK-SK 735
Cdd:cd03250 100 VIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLnNK 179
|
170 180
....*....|....*....|....
gi 16758936 736 TVLFVTHQLQYLVDCDEVIFMKEG 759
Cdd:cd03250 180 TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
858-1166 |
9.45e-104 |
|
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: 332.16 E-value: 9.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVFEGnrssvsdsmrdnpflQYYASIYALSMAVMLILKAIRGVVFVK 937
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG---------------YYLGVYAALLVLASVLLVLLRWLLFVL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 938 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1017
Cdd:cd18580 66 AGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1018 GPLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWL 1097
Cdd:cd18580 146 PPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1098 AVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1166
Cdd:cd18580 226 GLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
911-1417 |
8.35e-100 |
|
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: 336.04 E-value: 8.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 911 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVR 984
Cdd:COG2274 190 QDLSTLWVLAIGLLLallfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 985 LPFQAEMFIQNVILVFFCVGMIAgVFPWFLVAVGPLLILFSVLhiVSRVLIRELKRLDNIT---QSPFLSHITSSIQGLA 1061
Cdd:COG2274 269 LTGSLLTALLDLLFVLIFLIVLF-FYSPPLALVVLLLIPLYVL--LGLLFQPRLRRLSREEseaSAKRQSLLVETLRGIE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1062 TIHAYNKRQEFLHRYQELLDDNQAPFFlftcAMRWLAVRLDLISIAL--ITTTGLMIV----LMHGQIP-------SAYA 1128
Cdd:COG2274 346 TIKALGAESRFRRRWENLLAKYLNARF----KLRRLSNLLSTLSGLLqqLATVALLWLgaylVIDGQLTlgqliafNILS 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1129 GLAISYAVQLTGLFQftvRLAsetEARfTSVERINHYIKtLSLEAPARIKNKAPPHdwpQEGEITFENAEMRYRENLPLV 1208
Cdd:COG2274 422 GRFLAPVAQLIGLLQ---RFQ---DAK-IALERLDDILD-LPPEREEGRSKLSLPR---LKGDIELENVSFRYPGDSPPV 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL- 1287
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENIt 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1288 --DPfnQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDL 1365
Cdd:COG2274 571 lgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1366 LIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1417
Cdd:COG2274 649 IILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1186-1410 |
7.59e-99 |
|
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: 315.12 E-value: 7.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1186 WPQEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL 1265
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1266 RSKLTIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALerthmkeciaqlplklesEVMENGDNFSVGERQLLCIARALLR 1345
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1346 HCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 1410
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
858-1165 |
2.16e-86 |
|
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: 283.60 E-value: 2.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVFEGNRSsvsdsmrdnpflqYYASIYALSMAVMLILKAIRGVVFVK 937
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRD-------------YRLGVYGALGLGQAIFVFLGSLALAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 938 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1017
Cdd:cd18603 68 GCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1018 GPLLILFsvlHIVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAM 1094
Cdd:cd18603 148 IPLAILY---FFIQRFYVatsRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSN 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1095 RWLAVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1165
Cdd:cd18603 225 RWLAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
858-1165 |
4.38e-86 |
|
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: 282.83 E-value: 4.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVFegnrssvsdsmrdnpflqyYASIYALSMAVMLILKAIRGVVFVK 937
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQGF-------------------YIGIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 938 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1017
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1018 GPLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWL 1097
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1098 AVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1165
Cdd:cd18606 222 AIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
858-1166 |
1.11e-83 |
|
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: 276.33 E-value: 1.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVFEgnrssvsdsmrdNPFLQYYASIYALSMAVMLILKAIRGVVFVK 937
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFI------------NDSFNFFLTVYGFLAGLNSLFTLLRAFLFAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 938 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVilvFFCVGMIAGV---FPWFL 1014
Cdd:cd18605 69 GGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL---FGLLGYLVVIcyqLPWLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1015 VAVGPLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAM 1094
Cdd:cd18605 146 LLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1095 RWLAVRLDLISIALITTTGLMIVLMH---GQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1166
Cdd:cd18605 226 QWLSIRLQLLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
858-1166 |
3.27e-83 |
|
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: 274.73 E-value: 3.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWikqGSGNSTVFEGNRSSVSdsmrdnpfLQYYASIYALSMAVMLILKAIRGVVFVK 937
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIW---ASAYETSSALPPSEVS--------VLYYLGIYALISLLSVLLGTLRYLLFFF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 938 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1017
Cdd:cd18604 70 GSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1018 GPLLILFSVlhiVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAM 1094
Cdd:cd18604 150 VVLAALYVY---IGRLYLrasRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1095 RWLAVRLDLISIALITTTGLMIVLMHGqIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1166
Cdd:cd18604 227 RWLSVRIDLLGALFSFATAALLVYGPG-IDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
854-1165 |
3.82e-79 |
|
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: 263.80 E-value: 3.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 854 GPLAFLVIMVLFMLNVGSTAFSTWWLSYWI----KQGSGNSTVFEGNRSSVSDSMRDNpflQYYASIYALSMAVMLILKA 929
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWAnleeKLNDTTDRVQGENSTNVDIEDLDR---DFNLGIYAGLTAATFVFGF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 930 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGV 1009
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1010 FPWFLVAVGPLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFL 1089
Cdd:cd18601 158 NPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1090 FTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1165
Cdd:cd18601 238 FLATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1190-1421 |
6.29e-77 |
|
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: 255.22 E-value: 6.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1190 GEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1269
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1349
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1350 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRF 1421
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
848-1417 |
2.00e-74 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 259.30 E-value: 2.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 848 YIQAAGGPLAFLVIMVLfmLNVGSTAFSTWWLSYWIkqgsgnSTVFEGNRSSVSdsmrdnpflqyyASIYALSMAVMLIL 927
Cdd:COG4988 11 LARGARRWLALAVLLGL--LSGLLIIAQAWLLASLL------AGLIIGGAPLSA------------LLPLLGLLLAVLLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 928 KAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV---R-LP--FQAeMFIQNVI 997
Cdd:COG4988 71 RALlawlRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfaRyLPqlFLA-ALVPLLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 998 LVF-FCVGMIAGVFpwfLVAVGPLLILFSVL-HIVSRVLIRelKRLDNITQspfLS-HITSSIQGLATIHAYNKRQEFLH 1074
Cdd:COG4988 150 LVAvFPLDWLSGLI---LLVTAPLIPLFMILvGKGAAKASR--RQWRALAR---LSgHFLDRLRGLTTLKLFGRAKAEAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1075 RYQELLDDnqapfflFTCA-MRWLavRLDLISIA---LITTTGLMIV-------LMHGQIpSAYAGLAIsyavqltgLFq 1143
Cdd:COG4988 222 RIAEASED-------FRKRtMKVL--RVAFLSSAvleFFASLSIALVavyigfrLLGGSL-TLFAALFV--------LL- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1144 ftvrLASE---------------TEARfTSVERInhyIKTLSLEAPARIKNKAPPhDWPQEGEITFENAEMRYRENLPlV 1208
Cdd:COG4988 283 ----LAPEfflplrdlgsfyharANGI-AAAEKI---FALLDAPEPAAPAGTAPL-PAAGPPSIELEDVSFSYPGGRP-A 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNLD 1288
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1289 PFN-QYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLI 1367
Cdd:COG4988 433 LGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI 512
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 16758936 1368 QETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1417
Cdd:COG4988 513 LQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
858-1165 |
4.17e-74 |
|
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: 249.44 E-value: 4.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVfegnRSSVSDSMRDNPFLQYYASIYALSMAVMLILKAIRGVVFVK 937
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASV----VFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 938 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 1017
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1018 GPLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRWL 1097
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1098 AVRLDLISiALITTTGLMIVL---MHGQIPSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1165
Cdd:cd18602 237 GIRLDYLG-AVIVFLAALSSLtaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
939-1426 |
5.45e-71 |
|
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: 249.30 E-value: 5.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 939 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD-----VRLPFqaemfIQNVILVFFCVGMIAGVFPWF 1013
Cdd:COG4987 83 TLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrVLLPL-----LVALLVILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1014 LVAVGPLLILFSVL-----HIVSRVLIRELKRLdnitQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQApff 1088
Cdd:COG4987 158 ALVLALGLLLAGLLlpllaARLGRRAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA--- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1089 lftcAMRWLAvRLDLISIALIT-TTGLMIVLM---------HGQIPSAYAG------LAISYAVQ-LTGLFQFTVRLASe 1151
Cdd:COG4987 231 ----AQRRLA-RLSALAQALLQlAAGLAVVAVlwlaaplvaAGALSGPLLAllvlaaLALFEALApLPAAAQHLGRVRA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1152 tearftSVERINHyiktlSLEAPARIKNKAPPHDWPQEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSG 1231
Cdd:COG4987 305 ------AARRLNE-----LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1232 KSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL---DPfnQYTEEQIWDALERTHMK 1308
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1309 ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLH 1388
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
490 500 510
....*....|....*....|....*....|....*...
gi 16758936 1389 TVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMCA 1426
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1190-1414 |
1.58e-69 |
|
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: 232.89 E-value: 1.58e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1190 GEITFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1269
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSGTVRSNLDPFNQY-TEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1348
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1349 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLL 1414
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
913-1424 |
1.70e-63 |
|
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: 227.29 E-value: 1.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 913 YASIYALSMAVMLILKAIRGvvfvkgtlrassrlhdELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 992
Cdd:TIGR02203 72 FVSTYLLSWVSNKVVRDIRV----------------RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 993 IQNVILVFFCVGMIAgVFPWFLVAVgpLLILFSVLHIVSRVLIRELKRLDNITQSPF--LSHITS-SIQGLATIHAYNKR 1069
Cdd:TIGR02203 136 VRETLTVIGLFIVLL-YYSWQLTLI--VVVMLPVLSILMRRVSKRLRRISKEIQNSMgqVTTVAEeTLQGYRVVKLFGGQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1070 QEFLHRYQELlddnqapfflfTCAMRWLAVRLD------------LISIALITTtgLMIVLMHGQIPSAYAGLAISYAVQ 1137
Cdd:TIGR02203 213 AYETRRFDAV-----------SNRNRRLAMKMTsagsisspitqlIASLALAVV--LFIALFQAQAGSLTAGDFTAFITA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1138 LTGLFQFTVRLA---SETEARFTSVERINHYIKT-LSLEAPARIKNKApphdwpqEGEITFENAEMRYRENLPLVLKKVS 1213
Cdd:TIGR02203 280 MIALIRPLKSLTnvnAPMQRGLAAAESLFTLLDSpPEKDTGTRAIERA-------RGDVEFRNVTFRYPGRDRPALDSIS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1214 FTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL---DPf 1290
Cdd:TIGR02203 353 LVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1291 NQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQET 1370
Cdd:TIGR02203 432 EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 16758936 1371 IREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAM 1424
Cdd:TIGR02203 512 LERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG--LYAQ 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1192-1424 |
4.23e-63 |
|
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: 214.79 E-value: 4.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVRSNLdpfnQY-----TEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1346
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1347 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAM 1424
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEM 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
163-782 |
7.63e-63 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 225.81 E-value: 7.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 163 DAASLRRVVWIF--CRTRLILSIVCLMITQLAGFSGPAFVVKHLLEYTQATESN--LQYSLLLVLGLLLTEVVRSWSLAL 238
Cdd:COG1132 5 PRKLLRRLLRYLrpYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSalLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 239 TWALNYRTGVRLRGAV------LTMAFKKilklknikEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNV 312
Cdd:COG1132 85 LARLAQRVVADLRRDLfehllrLPLSFFD--------RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 313 IILGPTgfLGSAVFILFyPAMMFVSRLTAYFRRKCVAATDDRVQKMN----EVLTYIKFIKMYA----WVKAFSQCVQKI 384
Cdd:COG1132 157 FVIDWR--LALIVLLVL-PLLLLVLRLFGRRLRKLFRRVQEALAELNgrlqESLSGIRVVKAFGreerELERFREANEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 385 REEERRILEKAGYFQSITVGVAPIVVVIasVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAV 464
Cdd:COG1132 234 RRANLRAARLSALFFPLMELLGNLGLAL--VLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 465 DRFKSLflMEEVHMIKNKPASPHIK-----IEMKNATLAWDsshsstqsspkltpkvkkdkrapkgkkeksrqlqhtehq 539
Cdd:COG1132 312 ERIFEL--LDEPPEIPDPPGAVPLPpvrgeIEFENVSFSYP--------------------------------------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 540 avlaeqkghllldsDERPspeeeegkqihagsmrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI 619
Cdd:COG1132 351 --------------GDRP-------------------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 620 AVSGT-------------FAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANL 685
Cdd:COG1132 398 LIDGVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNL 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 686 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERG 765
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
650
....*....|....*..
gi 16758936 766 THEELMNLNGDYATIFN 782
Cdd:COG1132 557 THEELLARGGLYARLYR 573
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1192-1403 |
8.17e-63 |
|
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: 211.47 E-value: 8.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVRSNLdpfnqyteeqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILI 1351
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1352 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQ 1403
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1192-1424 |
1.63e-61 |
|
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: 210.16 E-value: 1.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVRSNLdpfnQY-----TEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1346
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1347 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAM 1424
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGG--VYAK 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
577-759 |
5.26e-61 |
|
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: 208.34 E-value: 5.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVS-----------------GTFAYVAQQAWILNATL 639
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 719
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16758936 720 GNHIFNSAIRKRLK--SKTVLFVTHQLQYLVDCDEVIFMKEG 759
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
917-1406 |
5.32e-60 |
|
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: 218.15 E-value: 5.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 917 YALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTG---RILNRFSKDMDEVdVRlpfqaeMFI 993
Cdd:COG5265 84 YGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGglsRDIERGTKGIEFL-LR------FLL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 994 QNVILVFFCVGMIAGVF-----PWF----LVAVGpLLILFSVLHIVSRV-LIRELKRLDNITQSpflsHITSSIQGLATI 1063
Cdd:COG5265 157 FNILPTLLEIALVAGILlvkydWWFalitLVTVV-LYIAFTVVVTEWRTkFRREMNEADSEANT----RAVDSLLNYETV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1064 HAYNKRQEFLHRYQELLDDnqapfflFTCAMRWLAVRLDLISI--ALITTTGLMIVLMhgqipsaYAGLAIS-------- 1133
Cdd:COG5265 232 KYFGNEAREARRYDEALAR-------YERAAVKSQTSLALLNFgqALIIALGLTAMML-------MAAQGVVagtmtvgd 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1134 ------YAVQLT---GLFQFTVRlasETEARFTSVERInhyiKTLsLEAPARIKNK--APPHDwPQEGEITFENAEMRYR 1202
Cdd:COG5265 298 fvlvnaYLIQLYiplNFLGFVYR---EIRQALADMERM----FDL-LDQPPEVADApdAPPLV-VGGGEVRFENVSFGYD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1203 ENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGT 1282
Cdd:COG5265 369 PERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDT 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1283 VRSNLdpfnQY-----TEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 1357
Cdd:COG5265 448 IAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16758936 1358 AMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1406
Cdd:COG5265 524 ALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
904-1406 |
1.52e-58 |
|
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: 213.02 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 904 MRDNPFLQYYA----SIYALSMAVMLILKAIRGVVFVKGTL---RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSK 976
Cdd:TIGR02204 44 MIDHGFSKDSSgllnRYFAFLLVVALVLALGTAARFYLVTWlgeRVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 977 DMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFP---WFLVAVGPLlILFSVLHIVSRVliRELKRLDNITQSPFLSHI 1053
Cdd:TIGR02204 124 DTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPkltSLVLLAVPL-VLLPILLFGRRV--RKLSRESQDRIADAGSYA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1054 TSSIQGLATIHAYNKRQEFLHRYQELLDDNqapfflFTCAMRWLAVRLDLISIAL-ITTTGLMIVL-------MHGQIPS 1125
Cdd:TIGR02204 201 GETLGAIRTVQAFGHEDAERSRFGGAVEKA------YEAARQRIRTRALLTAIVIvLVFGAIVGVLwvgahdvIAGKMSA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1126 AYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKTLS-LEAPAriKNKAPPHdwPQEGEITFENAEMRY--R 1202
Cdd:TIGR02204 275 GTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdIKAPA--HPKTLPV--PLRGEIEFEQVNFAYpaR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1203 ENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGT 1282
Cdd:TIGR02204 351 PDQP-ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAAS 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1283 VRSNLDPFN-QYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1361
Cdd:TIGR02204 430 VMENIRYGRpDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 16758936 1362 ETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1406
Cdd:TIGR02204 510 ESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVA 554
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
575-775 |
6.49e-57 |
|
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: 207.69 E-value: 6.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRD 641
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:COG4988 430 NLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 721 NHIFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 775
Cdd:COG4988 510 AEILQ-ALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1192-1417 |
2.83e-56 |
|
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: 195.45 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1269
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSGTVRSNL-----DPfnqyTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALL 1344
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1345 RHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1417
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
181-466 |
4.28e-55 |
|
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: 193.86 E-value: 4.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 181 LSIVCLMITQLAGFSGPaFVVKHLLEYTQA-TESNLQYSLLLVLGLLLTEVVRSWSLALTWALNYRTGVRLRGAVLTMAF 259
Cdd:cd18579 1 LAGLLKLLEDLLSLAQP-LLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 260 kkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFI 327
Cdd:cd18579 80 ----------RKALrlsssarqetstGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 328 LFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAP 407
Cdd:cd18579 150 LLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFF 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 408 IVVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18579 230 STPVLVSLATFATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
271-783 |
6.34e-55 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 205.07 E-value: 6.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 271 KSLGELINicsndgqRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGS---AVFILFYPAMMFVSRLTAYFRRKC 347
Cdd:COG2274 250 RSVGDLAS-------RFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPplaLVVLLLIPLYVLLGLLFQPRLRRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 348 VAATDDRVQKMN----EVLTYIKFIKMYA--------WVKAFSQCVqKIREEERRILEKAGYFQSITVGVAPIVVVIASV 415
Cdd:COG2274 323 SREESEASAKRQsllvETLRGIETIKALGaesrfrrrWENLLAKYL-NARFKLRRLSNLLSTLSGLLQQLATVALLWLGA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 416 vtFSV---HMTLGfDLTAAQAFtVVTVFNSMT-FALKVTpfsvkSLSEASVAVDRFKSLFLME-EVHMIKNKPASPHIK- 489
Cdd:COG2274 402 --YLVidgQLTLG-QLIAFNIL-SGRFLAPVAqLIGLLQ-----RFQDAKIALERLDDILDLPpEREEGRSKLSLPRLKg 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 490 -IEMKNATLawdsshsstqsspkltpkvkkdkrapkgkkeksrqlqhtehqavlaeqkghllldsdeRPSPEEEEgkqih 568
Cdd:COG2274 473 dIELENVSF----------------------------------------------------------RYPGDSPP----- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 569 agsmrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWIL 635
Cdd:COG2274 490 --------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpaslrrqIGVVLQDVFLF 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 636 NATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG2274 562 SGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 715 LDAHvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 783
Cdd:COG2274 642 LDAE-TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
915-1416 |
5.03e-54 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 202.64 E-value: 5.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 915 SIYALSM--AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 992
Cdd:TIGR00958 203 AIFFMCLlsIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 993 IQNVILVFFCVGMIAGVFPWF----LVAVGPLLILFSVLHIVSRVLIRELKrlDNITQSPFLSHitSSIQGLATIHAY-N 1067
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1068 KRQEfLHRYQELLDDnqapfflftcaMRWLAVRLDLISIALITTTGLM------IVL-------MHGQIPSayaGLAIS- 1133
Cdd:TIGR00958 359 EEGE-ASRFKEALEE-----------TLQLNKRKALAYAGYLWTTSVLgmliqvLVLyyggqlvLTGKVSS---GNLVSf 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1134 --YAVQLTGLFQFTVRLASETEARFTSVERINHYI-KTLSLEAPARIknkAPPHDwpqEGEITFENAEMRY--RENLPlV 1208
Cdd:TIGR00958 424 llYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdRKPNIPLTGTL---APLNL---EGLIEFQDVSFSYpnRPDVP-V 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNLD 1288
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1289 -PFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLI 1367
Cdd:TIGR00958 577 yGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16758936 1368 QETirEAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:TIGR00958 657 QES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1190-1419 |
6.74e-53 |
|
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: 186.98 E-value: 6.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1190 GEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKL 1269
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD-IQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1349
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1350 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSS 1419
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1190-1405 |
8.16e-53 |
|
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: 184.72 E-value: 8.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1190 GEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1269
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSGTVRSNLDPFNQY-TEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1348
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1349 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVV 1405
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
578-787 |
2.00e-52 |
|
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: 185.83 E-value: 2.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSV 657
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 658 LNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLKSKTV 737
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758936 738 LFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDyatiFNNLLLG 787
Cdd:cd03291 213 ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD----FSSKLMG 258
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1192-1418 |
1.58e-51 |
|
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: 181.92 E-value: 1.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVRSNL---DPfnQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1348
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1349 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 1418
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
950-1417 |
1.86e-49 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 186.38 E-value: 1.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 950 LFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD----------VRlpfQAEMFIQNVILVFFcvgmiagvFPWFLVavgp 1019
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAssssgalitvVR---EGASIIGLFIMMFY--------YSWQLS---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1020 lLILFSVLHIVSrVLIREL-KRLDNIT---QSPfLSHITSS----IQGLATIHAYNKRQEFLHRYQELLDDnqapfflft 1091
Cdd:PRK11176 169 -LILIVIAPIVS-IAIRVVsKRFRNISknmQNT-MGQVTTSaeqmLKGHKEVLIFGGQEVETKRFDKVSNR--------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1092 caMRWLAVRL---DLIS---IALITTTGLMIVLMHGQIPSAYAGL-AISYAVQLTGLFQFTVRLASETE--ARFtsvERI 1162
Cdd:PRK11176 237 --MRQQGMKMvsaSSISdpiIQLIASLALAFVLYAASFPSVMDTLtAGTITVVFSSMIALMRPLKSLTNvnAQF---QRG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1163 NHYIKTL----SLEAPariKNKAPPHDWPQEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMA 1238
Cdd:PRK11176 312 MAACQTLfailDLEQE---KDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1239 LFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL--DPFNQYTEEQIWDALERTHMKECIAQLPL 1316
Cdd:PRK11176 389 LTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDN 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1317 KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRI 1396
Cdd:PRK11176 469 GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEI 548
|
490 500
....*....|....*....|.
gi 16758936 1397 MVLAQGQVVEFDTPSVLLSND 1417
Cdd:PRK11176 549 LVVEDGEIVERGTHAELLAQN 569
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
580-778 |
1.04e-48 |
|
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: 183.81 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNILFG 646
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 647 K-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 725
Cdd:COG4987 433 RpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758936 726 sAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:COG4987 513 -DLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
918-1399 |
2.24e-47 |
|
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: 178.63 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 918 ALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDvrlPFQAEMFI 993
Cdd:TIGR02857 47 LGALALVLLLRAllgwLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALD---GYFARYLP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 994 QNVILVFFCVGMIAGVFP--W----FLVAVGPLLILFSVL--HIVSRVLIRELKRLDNITqspflSHITSSIQGLATIHA 1065
Cdd:TIGR02857 124 QLVLAVIVPLAILAAVFPqdWisglILLLTAPLIPIFMILigWAAQAAARKQWAALSRLS-----GHFLDRLRGLPTLKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1066 YNKRqeflHRYQELLDDNQAPF-----------FLFTCAMRWLAVrldlISIALITTT-GLMivLMHGQIPSAYAGLAIS 1133
Cdd:TIGR02857 199 FGRA----KAQAAAIRRSSEEYrertmrvlriaFLSSAVLELFAT----LSVALVAVYiGFR--LLAGDLDLATGLFVLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1134 YAVQltglFQFTVR-LASETEARFTSVERINHyIKTLsLEAPARIKNKAPPHDWPQEGEITFENAEMRYrENLPLVLKKV 1212
Cdd:TIGR02857 269 LAPE----FYLPLRqLGAQYHARADGVAAAEA-LFAV-LDAAPRPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1213 SFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL---DP 1289
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1290 fnQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQE 1369
Cdd:TIGR02857 422 --DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
490 500 510
....*....|....*....|....*....|
gi 16758936 1370 TIREAFADCTMLTIAHRLHTVLGSDRIMVL 1399
Cdd:TIGR02857 500 ALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
949-1427 |
6.74e-47 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 178.62 E-value: 6.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 949 ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV-DVRLPFQAEMFIQNVILVFFCVgmIAGVFPWFLVAVgpLLILFSVL 1027
Cdd:PRK13657 94 EYFERIIQLPLAWHSQRGSGRALHTLLRGTDALfGLWLEFMREHLATLVALVVLLP--LALFMNWRLSLV--LVVLGIVY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1028 HIVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYNKRQ---EFLHRYQELLDDNQAPfflftcAMRWLAVRL 1101
Cdd:PRK13657 170 TLITTLVMRKTKDGQAAVEehyHDLFAHVSDAIGNVSVVQSYNRIEaetQALRDIADNLLAAQMP------VLSWWALAS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1102 DL------ISIALITTTGLMIV----LMHGQIPS--AYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKTL 1169
Cdd:PRK13657 244 VLnraastITMLAILVLGAALVqkgqLRVGEVVAfvGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPP 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1170 SLEAPARIKnkapphdwpqeGEITFENAEMRYrENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC 1249
Cdd:PRK13657 324 GAIDLGRVK-----------GAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1250 IKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL-----DPfnqyTEEQIWDALERTHMKECIAQLPLKLESEVME 1324
Cdd:PRK13657 392 ILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1325 NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1404
Cdd:PRK13657 468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
490 500
....*....|....*....|....*.
gi 16758936 1405 VE---FDTpsvlLSNDSSRFYAMCAA 1427
Cdd:PRK13657 548 VEsgsFDE----LVARGGRFAALLRA 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
955-1424 |
1.74e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 177.60 E-value: 1.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 955 LRSPMKFFDTTPTGRILNRFSKDMdEVdVRlpfqaEMFIQNVILVFFCVGMIAGVfpwfLVAVGPL--------LILFSV 1026
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDT-EV-IR-----DLYVTVVATVLRSAALIGAM----LVAMFSLdwrmalvaIMIFPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1027 LHIV-------SRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYNKRQEFLHRyqeLLDDNQAPFflftcAMR 1095
Cdd:PRK10790 178 VLVVmviyqrySTPIVRRVRA--------YLADINDgfneVINGMSVIQQFRQQARFGER---MGEASRSHY-----MAR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1096 WLAVRLD------LISI--ALITTtGLMivLMHGQIPSAYAGLAISYA-VQLTG-----LFQFTVRLASETEArFTSVER 1161
Cdd:PRK10790 242 MQTLRLDgfllrpLLSLfsALILC-GLL--MLFGFSASGTIEVGVLYAfISYLGrlnepLIELTTQQSMLQQA-VVAGER 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1162 InhyiktlsLEAPARIKNKAPPHDWP-QEGEITFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALF 1240
Cdd:PRK10790 318 V--------FELMDGPRQQYGNDDRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLM 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1241 RLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLES 1320
Cdd:PRK10790 389 GYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYT 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1321 EVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLA 1400
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLH 548
|
490 500
....*....|....*....|....
gi 16758936 1401 QGQVVEFDTPSVLLSNdSSRFYAM 1424
Cdd:PRK10790 549 RGQAVEQGTHQQLLAA-QGRYWQM 571
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1181-1404 |
1.25e-44 |
|
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: 161.48 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1181 APPHdwpQEGEITFENAEMRYReNLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS 1258
Cdd:cd03248 4 APDH---LKGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1259 DIGLADLRSKLTIIPQEPVLFSGTVRSNLD-PFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLL 1337
Cdd:cd03248 80 QYEHKYLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1338 CIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1404
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1209-1427 |
9.55e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 169.26 E-value: 9.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG-----GCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTV 1283
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSL------LNALLGflpyqGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 RSNL---DPfnQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1360
Cdd:PRK11174 440 RDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1361 TETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE---FDTpsvlLSNDSSRFYAMCAA 1427
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
941-1415 |
1.48e-43 |
|
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: 170.14 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 941 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKdMDEVDVRLpfqAEMFIQNVILVFFC----VGMIAGVFPWFLVA 1016
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRIL---SGSTLTTLLSGIFAllnlGLMFYYSWKLALVA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1017 VGPLLILFSVLHIVSRVLIRELKRLDNItQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCAMRW 1096
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRLLEL-SGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1097 LAVrldLISIALITTTGLMIVLMHGQIPSAYAGLA--ISYAVQLTglfQFTVRLASETEARFTSVERINHYIKTLS-LEA 1173
Cdd:TIGR03797 361 LTV---FNAVLPVLTSAALFAAAISLLGGAGLSLGsfLAFNTAFG---SFSGAVTQLSNTLISILAVIPLWERAKPiLEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1174 PARIK-NKAPPHDWpqEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLveLSG----- 1247
Cdd:TIGR03797 435 LPEVDeAKTDPGKL--SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRL--LLGfetpe 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1248 -GCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENG 1326
Cdd:TIGR03797 507 sGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGG 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1327 DNFSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliQETIREAFA--DCTMLTIAHRLHTVLGSDRIMVLAQGQV 1404
Cdd:TIGR03797 587 GTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRV 662
|
490
....*....|.
gi 16758936 1405 VEFDTPSVLLS 1415
Cdd:TIGR03797 663 VQQGTYDELMA 673
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
573-759 |
2.73e-43 |
|
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: 155.62 E-value: 2.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATL 639
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNILfgkefdeerynsvlnscclrpdlailpnsdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 719
Cdd:cd03228 93 RENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16758936 720 GNHIFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEG 759
Cdd:cd03228 132 EALILE-ALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
939-1387 |
1.37e-42 |
|
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: 164.46 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 939 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR--LPfqaemfiqnvILVFFCVGMIA-GVFPW 1012
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyVRviVP----------AGVALVVGAAAvAAIAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1013 FLVAVGPLLIL-----FSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQEL------LD 1081
Cdd:TIGR02868 151 LSVPAALILAAglllaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEAdreltrAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1082 DNQApfflftcamRWLAVRLDLISIALITTTGLMIVL-----MHGQIPSAYagLAISYAVQLT---GLFQFTVRLASETE 1153
Cdd:TIGR02868 231 RRAA---------AATALGAALTLLAAGLAVLGALWAggpavADGRLAPVT--LAVLVLLPLAafeAFAALPAAAQQLTR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1154 ARfTSVERINHyiktlSLEAPARIKNKAPPHDWPQ-EGEITFENAEMRYR-ENLPLVLKKVSFTIKPKEKIGIVGRTGSG 1231
Cdd:TIGR02868 300 VR-AAAERIVE-----VLDAAGPVAEGSAPAAGAVgLGKPTLELRDLSAGyPGAPPVLDGVSLDLPPGERVAILGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1232 KSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL---DPfnQYTEEQIWDALERTHMK 1308
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLA 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1309 ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL 1387
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
578-782 |
2.50e-42 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 155.08 E-value: 2.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNIL 644
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKE--FDEERYNSVLnSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:cd03253 97 YGRPdaTDEEVIEAAK-AAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTERE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 723 IFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 782
Cdd:cd03253 176 IQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
578-778 |
1.36e-41 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 153.16 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHI 723
Cdd:cd03251 98 YGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ESERL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 724 FNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:cd03251 177 VQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
952-1423 |
2.11e-41 |
|
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: 164.14 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 952 RRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemfIQNVIL-VFFCVGMIAGVfPWFLVAVGPLLILFSVLHIV 1030
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDA---------LASTILsLFLDMWILVIV-GLFLVRQNMLLFLLSLLSIP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1031 SRVLI-----RELKRLDN---ITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCA---MRWLAV 1099
Cdd:TIGR01193 307 VYAVIiilfkRTFNKLNHdamQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAdqgQQAIKA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1100 RLDLISIALITTTGLMIVLMH----GQIpSAYAGLaISYavqLTGLFQFTVRLASETEARFTSVERINH-YIKTLSLEAP 1174
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGkltlGQL-ITFNAL-LSY---FLTPLENIINLQPKLQAARVANNRLNEvYLVDSEFINK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1175 ARIKNKAPPHdwpqeGEITFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG 1254
Cdd:TIGR01193 462 KKRTELNNLN-----GDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1255 VRISDIGLADLRSKLTIIPQEPVLFSGTVRSNLDPFNQ--YTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVG 1332
Cdd:TIGR01193 536 FSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGG 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1333 ERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREaFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1412
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
490
....*....|.
gi 16758936 1413 LLsnDSSRFYA 1423
Cdd:TIGR01193 695 LL--DRNGFYA 703
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
577-775 |
1.29e-40 |
|
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: 150.07 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNI 643
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 LFGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:cd03254 98 RLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758936 723 IfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 775
Cdd:cd03254 178 I-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
842-1166 |
1.45e-40 |
|
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: 153.03 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 842 WSVYWVYIQAAGGPLAFLV-IMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTVFEGNRSSVSDSMRDNpflQYYASIYALS 920
Cdd:cd18600 3 WNTYLRYITSHKSLIFVLIlCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSS---YYVFYIYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 921 MAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF 1000
Cdd:cd18600 80 ADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1001 FCVGMIAGVFPWFLVAVGPLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELL 1080
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1081 DDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPSAyAGLAISYAVQLTGLFQFTVRLASETEARFTSVE 1160
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGR-VGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVS 318
|
....*.
gi 16758936 1161 RINHYI 1166
Cdd:cd18600 319 RIFKFI 324
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
968-1425 |
1.55e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 159.22 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 968 GRILNRFSKDMDEVD---VRL--PFQAEMFiqnVILVffcvgmIAGVFPWF-----LVAVGPLLILFSVLHIVSRVLIRE 1037
Cdd:PRK11160 117 GDLLNRLVADVDTLDhlyLRLisPLVAALV---VILV------LTIGLSFFdltlaLTLGGILLLLLLLLPLLFYRLGKK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1038 LKRLDNITQSPFLSHITSSIQGLATIHAYNKrqefLHRYQELLDDNQApfflftcamRWLA-----VRLDLISIAL-ITT 1111
Cdd:PRK11160 188 PGQDLTHLRAQYRVQLTEWLQGQAELTLFGA----EDRYRQQLEQTEQ---------QWLAaqrrqANLTGLSQALmILA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1112 TGLMIVLMhgqipSAYAGLAISYAVQ---LTGLFQFTVRLASET----EARF-------TSVERINHYIktlslEAPARI 1177
Cdd:PRK11160 255 NGLTVVLM-----LWLAAGGVGGNAQpgaLIALFVFAALAAFEAlmpvAGAFqhlgqviASARRINEIT-----EQKPEV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1178 KNKAPPHDWPQEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI 1257
Cdd:PRK11160 325 TFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1258 SDIGLADLRSKLTIIPQEPVLFSGTVRSNL---DPfnQYTEEQIWDALERTHMkECIAQLPLKLESEVMENGDNFSVGER 1334
Cdd:PRK11160 405 ADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQ 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1335 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLL 1414
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
490
....*....|.
gi 16758936 1415 SNDsSRFYAMC 1425
Cdd:PRK11160 562 AQQ-GRYYQLK 571
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
531-756 |
2.50e-40 |
|
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: 157.83 E-value: 2.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 531 RQLQ---HTEHQAVLAEQKGHLLLDSDERPSPEEEEGKQIHAGSMRLQ----------RTLYNIDLEIEEGKLVGICGSV 597
Cdd:TIGR02857 278 RQLGaqyHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSgvsvaypgrrPALRPVSFTVPPGERVALVGPS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 598 GSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCL 663
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGL 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 664 RPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKRLKSKTVLFVTHQ 743
Cdd:TIGR02857 438 DEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTHR 516
|
250
....*....|...
gi 16758936 744 LQYLVDCDEVIFM 756
Cdd:TIGR02857 517 LALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
535-783 |
2.69e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 155.77 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 535 HTEHQAVLAEQKGHLLLDSDERPSPEEE------EGKQIHAG-----SMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTS 603
Cdd:PRK11174 312 HAKAQAVGAAESLVTFLETPLAHPQQGEkelasnDPVTIEAEdleilSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 604 LISAILGQMTLlEGSIAVSGT-------------FAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAI 669
Cdd:PRK11174 392 LLNALLGFLPY-QGSLKINGIelreldpeswrkhLSWVGQNPQLPHGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 670 LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKRLKSKTVLFVTHQLQYLVD 749
Cdd:PRK11174 471 LPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV-MQALNAASRRQTTLMVTHQLEDLAQ 549
|
250 260 270
....*....|....*....|....*....|....
gi 16758936 750 CDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 783
Cdd:PRK11174 550 WDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1192-1404 |
7.23e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.19 E-value: 7.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENaeMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:COG4619 1 LELEG--LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVRSNLD-PFN----QYTEEQIWDALERthmkeciaqlpLKLESEVME-NGDNFSVGERQLLCIARALLR 1345
Cdd:COG4619 79 VPQEPALWGGTVRDNLPfPFQlrerKFDRERALELLER-----------LGLPPDILDkPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1346 HCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAH------RLhtvlgSDRIMVLAQGQV 1404
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
577-761 |
7.27e-39 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 144.65 E-value: 7.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNI 643
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 LFGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:cd03245 99 TLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 16758936 723 IFnSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:cd03245 179 LK-ERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
181-466 |
9.38e-38 |
|
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: 144.13 E-value: 9.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 181 LSIVCLMITQLAGFSGPaFVVKHLLEYtqATESNLQYSLllvlglllTEVVRSWSLAL---------TWALNY------R 245
Cdd:cd18597 1 LAGLLKLLADVLQVLSP-LLLKYLINF--VEDAYLGGPP--------PSIGYGIGYAIglfllqllsSLLLNHffyrsmL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 246 TGVRLRGAVLTMAFkkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVI 313
Cdd:cd18597 70 TGAQVRAALTKAIY----------RKSLrlsgksrhefpnGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 314 ILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILE 393
Cdd:cd18597 140 NLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 394 KAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18597 220 KLQILRSILTAVAFSLPVLASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKR 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
670-1399 |
6.30e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 152.49 E-value: 6.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 670 LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIFNSAIR--KRLKSKTVLFVTHQLQYL 747
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 748 -------------------VDCDEVIFMKEGC----------------------------ITERGTHEELM-NLNGDYAT 779
Cdd:PTZ00265 644 ryantifvlsnrergstvdVDIIGEDPTKDNKennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMkNKNGIYYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 780 IFNNLLLGETPPVEINSKKEA---SGSQKSQDKGPKP----GSVKKEK----AVKSEEGQLVQVEEKGQGSVPWSVYWVY 848
Cdd:PTZ00265 724 MINNQKVSSKKSSNNDNDKDSdmkSSAYKDSERGYDPdemnGNSKHENesasNKKSCKMSDENASENNAGGKLPFLRNLF 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 849 IQAAGGPLAFLVI---MVLFMLNVGSTAFStwwlsywIKQGSGNSTVFEGNRSSVSDSMRDNPFLQYYA---SIYALSMA 922
Cdd:PTZ00265 804 KRKPKAPNNLRIVyreIFSYKKDVTIIALS-------ILVAGGLYPVFALLYAKYVSTLFDFANLEANSnkySLYILVIA 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 923 V-MLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDT---TPtGRILNRFSKDMDEVDVRLPFQAEMFIQNVIL 998
Cdd:PTZ00265 877 IaMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTHFIVL 955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 999 vfFCVGMIAGVFPWFLVA---VGPLLILFSVLHIVSRVLIR---ELKRL------------DNITQSP-FLshITSSIQG 1059
Cdd:PTZ00265 956 --FLVSMVMSFYFCPIVAavlTGTYFIFMRVFAIRARLTANkdvEKKEInqpgtvfaynsdDEIFKDPsFL--IQEAFYN 1031
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1060 LATIHAYNKRQEFLHRYQELLD-------------------DNQAPFFLFTCAMrWLAVRLdlISIALITTTGLMIVLMH 1120
Cdd:PTZ00265 1032 MNTVIIYGLEDYFCNLIEKAIDysnkgqkrktlvnsmlwgfSQSAQLFINSFAY-WFGSFL--IRRGTILVDDFMKSLFT 1108
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1121 GQIPSAYAGLAISyavqltglfqftvrLASETEARFTSVERINHYIKTLSL-----EAPARIKNKAPPhdwpqEGEITFE 1195
Cdd:PTZ00265 1109 FLFTGSYAGKLMS--------------LKGDSENAKLSFEKYYPLIIRKSNidvrdNGGIRIKNKNDI-----KGKIEIM 1169
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1196 NAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL---------------------------- 1245
Cdd:PTZ00265 1170 DVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeq 1248
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1246 --------------------------SGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNLDpFNQ--YTEEQ 1297
Cdd:PTZ00265 1249 nvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATRED 1327
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1298 IWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREA--F 1375
Cdd:PTZ00265 1328 VKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdK 1407
|
890 900
....*....|....*....|....
gi 16758936 1376 ADCTMLTIAHRLHTVLGSDRIMVL 1399
Cdd:PTZ00265 1408 ADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
578-778 |
4.17e-36 |
|
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: 137.29 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKE--FDEERyNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNH 722
Cdd:cd03249 99 YGKPdaTDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES-EK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 723 IFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
566-766 |
5.29e-36 |
|
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: 136.47 E-value: 5.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 566 QIHAGSMR----LQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYV 628
Cdd:cd03244 4 EFKNVSLRyrpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 629 AQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:cd03244 84 PQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 709 DDPLSALDAHVGNHIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 766
Cdd:cd03244 164 DEATASVDPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
230-466 |
5.47e-36 |
|
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: 139.17 E-value: 5.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 230 VVRSWSLALTWALNYRTGVRLRgAVLTMA----------------------FKKILKLKNIKEKSLGELINICSNDGQRM 287
Cdd:cd18596 50 LLSSLLDQQYLWIGRRLSVRLR-AILTQLifekalrrrdksgssksseskkKDKEEDEDEKSSASVGKINNLMSVDANRI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 288 FEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKF 367
Cdd:cd18596 129 SEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRM 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 368 IKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVH-MTLGFDLTAAQAFTVVTVFNSMTFA 446
Cdd:cd18596 209 IKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYtLVMGQELTASVAFTSLALFNMLRGP 288
|
250 260
....*....|....*....|
gi 16758936 447 LKVTPFSVKSLSEASVAVDR 466
Cdd:cd18596 289 LNVLPELITQLLQAKVSLDR 308
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1208-1407 |
7.98e-36 |
|
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: 136.10 E-value: 7.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLTIIPQEPvlfsgtvR 1284
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP-------M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLDPfnQYT-EEQIWDALE--RTHMKECIAQLPLKLESEVMENGDN--------FSVGERQLLCIARALLRHCKILILD 1353
Cdd:cd03257 93 SSLNP--RMTiGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEEvlnrypheLSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1354 EATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 1407
Cdd:cd03257 171 EPTSALDVSVqaqilDLLKK--LQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
577-782 |
2.86e-35 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 143.32 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNI 643
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladytlaslrrqVALVSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 LFGK--EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 721
Cdd:TIGR02203 427 AYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 722 HIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 782
Cdd:TIGR02203 507 LV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1192-1406 |
3.72e-35 |
|
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: 132.44 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLTI 1271
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVRSNLdpfnqyteeqiwdalerthmkeciaqlplklesevmenGDNFSVGERQLLCIARALLRHCKILI 1351
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1352 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1406
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
578-778 |
4.04e-35 |
|
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: 134.54 E-value: 4.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNIL 644
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKE-FDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHI 723
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEHA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 724 FNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:cd03252 177 IMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
578-777 |
8.65e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 141.77 E-value: 8.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AVSGTFAYVAQQAWILNATLRDNIL 644
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 723
Cdd:PRK10789 411 LGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16758936 724 FNSaIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDY 777
Cdd:PRK10789 491 LHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
230-466 |
1.04e-34 |
|
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: 134.90 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 230 VVRSWSLALTWALNYRTGVRLRGAVLTMAFkkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLL 297
Cdd:cd18595 49 IIQSLLLHQYFHRCFRLGMRIRTALTSAIY----------RKALrlsnsarkkstvGEIVNLMSVDAQRIQDLVPYLNML 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 298 AGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAF 377
Cdd:cd18595 119 WSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 378 SQCVQKIREEERRILEKAGYFQSITV---GVAPIVVviaSVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPF 452
Cdd:cd18595 199 EKKILKIREKELKLLKKAAYLNAVSSflwTCAPFLV---SLATFATYVLSDPDnvLDAEKAFVSLSLFNILRFPLSMLPM 275
|
250
....*....|....
gi 16758936 453 SVKSLSEASVAVDR 466
Cdd:cd18595 276 VISNLVQASVSLKR 289
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1192-1404 |
2.09e-34 |
|
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: 130.03 E-value: 2.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVRSNLdpfnqyteeqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILI 1351
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16758936 1352 LDEATAAMDTETDLLIQETIREA-FADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1404
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1209-1357 |
4.75e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 128.15 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSG-TVRSNL 1287
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1288 -------DPFNQYTEEQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 1357
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
922-1407 |
1.36e-33 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 137.96 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 922 AVMLILKAIRGVVFVkgtlRASSRLHDEL----FRRILRSPMKFFDTTPTgRILNrfskDMDEVdvRlpfQaemFI-QNV 996
Cdd:COG4618 71 AVMGLLDAVRSRILV----RVGARLDRRLgprvFDAAFRAALRGGGGAAA-QALR----DLDTL--R---Q---FLtGPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 997 ILVFF----CVGMIAGVF---PWF-LVAVGPLLILFSV---LHIVSRVLIRELKRLDNITQSpflsHITSSIQGLATIHA 1065
Cdd:COG4618 134 LFALFdlpwAPIFLAVLFlfhPLLgLLALVGALVLVALallNERLTRKPLKEANEAAIRANA----FAEAALRNAEVIEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1066 -----------YNKRQEFLhRYQELLDDNQAPFFLFTCAMR------------WLAVRLDLisialitTTGLMI---VLM 1119
Cdd:COG4618 210 mgmlpalrrrwQRANARAL-ALQARASDRAGGFSALSKFLRlllqsavlglgaYLVIQGEI-------TPGAMIaasILM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1120 hgqipsayaGLAISYAVQLTGLFQFTVRlaseteARfTSVERINHYIKTLSLEaPARIKNKAPphdwpqEGEITFENAEM 1199
Cdd:COG4618 282 ---------GRALAPIEQAIGGWKQFVS------AR-QAYRRLNELLAAVPAE-PERMPLPRP------KGRLSVENLTV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1200 RYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLF 1279
Cdd:COG4618 339 VPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 SGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1359
Cdd:COG4618 419 DGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16758936 1360 DTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVVEF 1407
Cdd:COG4618 499 DDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
858-1142 |
2.13e-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: 130.84 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWIKQGSGNSTvfegnrssvSDSMRDNPFLQYYASIYALsmavMLILKAIRGVVFVK 937
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD---------PETQALNVYSLALLLLGLA----QFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 938 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVIlVFFCVGMIAGVFPWFL--- 1014
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLA-TIVGGIIVMFYYGWKLtlv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1015 -VAVGPLLILFSVlhIVSRVLiRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFFLFTCA 1093
Cdd:pfam00664 147 lLAVLPLYILVSA--VFAKIL-RKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1094 MRWLAVRLDLI---SIALITTTGlMIVLMHGQIPSAYAGLAISYAVQLTGLF 1142
Cdd:pfam00664 224 NGLSFGITQFIgylSYALALWFG-AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1166-1406 |
2.60e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 137.15 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1166 IKTLSLEAPARIKNKAP-PHdwpQEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 1244
Cdd:PRK10789 290 IRAMLAEAPVVKDGSEPvPE---GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1245 LSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL---DPfnQYTEEQIWDALERTHMKECIAQLPLKLESE 1321
Cdd:PRK10789 367 VSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1322 VMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQ 1401
Cdd:PRK10789 445 VGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQH 524
|
....*
gi 16758936 1402 GQVVE 1406
Cdd:PRK10789 525 GHIAQ 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1172-1416 |
2.00e-32 |
|
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: 133.88 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1172 EAPARIKNKAPPHDWPQEGE--ITFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS 1246
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1247 GGCIKIDGVRISDIG---LADLRSKLTIIPQEPVlfsgtvrSNLDPFnqYT-EEQIWDALE------RTHMKECIAQLpL 1316
Cdd:COG1123 319 SGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPY-------SSLNPR--MTvGDIIAEPLRlhgllsRAERRERVAEL-L 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1317 K---LESEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHR 1386
Cdd:COG1123 389 ErvgLPPDLADrYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL----DVSVQAQILNLLRDlqrelgLTYLFISHD 464
|
250 260 270
....*....|....*....|....*....|.
gi 16758936 1387 LHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:COG1123 465 LAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
272-467 |
8.18e-32 |
|
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: 126.59 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 272 SLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAAT 351
Cdd:cd18594 94 TTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 352 DDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAA 431
Cdd:cd18594 174 DERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTAR 253
|
170 180 190
....*....|....*....|....*....|....*...
gi 16758936 432 QAFTVVTVFNS--MTFALKVtPFSVKSLSEASVAVDRF 467
Cdd:cd18594 254 KVFTVISLLNAlrMTITRFF-PESIQTLSESRVSLKRI 290
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
578-778 |
2.44e-31 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 131.29 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlaslrnqVALVSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKEfdeERYNsvlnscclRPDL--------AI-----LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:PRK11176 439 YART---EQYS--------REQIeeaarmayAMdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 712 LSALDAHvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:PRK11176 508 TSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1192-1416 |
1.26e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 128.10 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDIGLADLRSK 1268
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1269 LTIIPQEPvlfsgtvRSNLDPFNqyTEEQIWDALE-----RTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIAR 1341
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALEnlglsRAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1342 ALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
578-778 |
5.34e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 128.30 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 723
Cdd:TIGR00958 577 YGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 724 FNSairKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
578-778 |
9.43e-30 |
|
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: 127.55 E-value: 9.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWI---LNATLRDNILFGKEFDEery 654
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLrrqMGVVLQENVLFSRSIRD--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 655 nsvlNSCCLRPDLAI------------------LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:TIGR01846 550 ----NIALCNPGAPFehvihaaklagahdfiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 717 AHvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR01846 626 YE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
563-778 |
9.72e-30 |
|
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: 127.75 E-value: 9.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 563 EGKQIHAGSMRLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AVSGTFAYV 628
Cdd:TIGR03796 479 ELRNITFGYSPLEPPLIeNFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEIlfdgipreeipreVLANSVAMV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 629 AQQAWILNATLRDNI-LFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:TIGR03796 559 DQDIFLFEGTVRDNLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 708 LDDPLSALDAHVgNHIFNSAIRKRlkSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR03796 639 LDEATSALDPET-EKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYA 706
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
578-757 |
2.05e-29 |
|
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: 117.25 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------FAYVAQQA---WILNATLRDNIL-- 644
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 ------FGKEFDEERYNSVLNScclrpdLAILpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERV---GLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16758936 718 HvGNHIFNSAIRK-RLKSKTVLFVTHQLQYLVD-CDEVIFMK 757
Cdd:cd03235 166 K-TQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
242-466 |
2.18e-29 |
|
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: 120.03 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 242 LNYRTGVRLRGAVLTMAF----KKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGP 317
Cdd:cd18591 79 IVIREGIRLKTALQAMIYekalRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 318 TGFLGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGY 397
Cdd:cd18591 159 SALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAV 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 398 FQSITVGVAPIVVVIASVVTFSVHMTL-GFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18591 239 YWSLMTFLTQASPILVTLVTFGLYPYLeGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1194-1403 |
4.07e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 116.41 E-value: 4.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1194 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIP 1273
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1274 QEP--VLFSGTVRSNL--DPFNQYTEEQ-----IWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1344
Cdd:cd03225 82 QNPddQFFGPTVEEEVafGLENLGLPEEeieerVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1345 RHCKILILDEATAAMDTETDLLIQETIREaFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQ 1403
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
542-744 |
6.22e-29 |
|
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: 123.24 E-value: 6.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 542 LAEQKGHLLLDSDERPSPEEEEG-----KQIHAGSMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLE 616
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLGKptlelRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 617 GSIAVSG-------------TFAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERG 682
Cdd:TIGR02868 390 GEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 683 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKRLKSKTVLFVTHQL 744
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLLAALSGRTVVLITHHL 530
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1193-1403 |
1.05e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.11 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1193 TFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTII 1272
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1273 PQepvlfsgtvrsnldpfnqyteeqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILIL 1352
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1353 DEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTV-LGSDRIMVLAQGQ 1403
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1192-1403 |
1.09e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 114.87 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRY---RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRISdigladlrsk 1268
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIA---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1269 ltIIPQEPVLFSGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1348
Cdd:cd03250 70 --YVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1349 ILILDEATAAMDTET-DLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQ 1403
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
578-778 |
1.11e-28 |
|
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: 123.39 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLI-----------SAIL--GQ----MTL--LEGSIAVsgtfayVAQQAWILNAT 638
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfydvtsGRILidGQdirdVTQasLRAAIGI------VPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:COG5265 448 IAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 718 HVGNHIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:COG5265 528 RTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
578-772 |
1.11e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------FAYVAQQA---WILNATLRDNILFG 646
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 647 --------KEFDEERYNSVLNScclrpdLAILpnsDLTE-----IGErganLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEA------LERV---GLEDladrpIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 714 ALDAHVGNHIFnsAIRKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITErGTHEELMN 772
Cdd:COG1121 169 GVDAATEEALY--ELLRELRRegKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
575-778 |
1.14e-28 |
|
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: 123.27 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRD 641
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVdlrqldpaelrarMALVPQDPVLFAASVME 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGK--EFDEERYNSVLNScclRPDLAI--LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:TIGR02204 433 NIRYGRpdATDEEVEAAARAA---HAHEFIsaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 718 HvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYA 569
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
575-765 |
4.09e-28 |
|
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: 112.41 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI------------AVSGTFAYVAQQAWILNATLRDN 642
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvsdlekALSSLISVLNQRPYLFDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 IlfgkefdeerynsvlnscclrpdlailpnsdlteigerGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:cd03247 95 L--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16758936 723 IFnSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERG 765
Cdd:cd03247 137 LL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
573-772 |
4.15e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 114.52 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQ-------- 631
Cdd:COG1124 16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQDpyaslhpr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 632 ---AWILNATLRdniLFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:COG1124 96 htvDRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL----------DRYPHQLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 709 DDPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1124 163 DEPTSALDVSVQAEILNllKDLREERGL-TYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
561-778 |
4.30e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 121.09 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 561 EEEGKQIHAGSMRL-----------QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----- 624
Cdd:PRK11160 328 TTSTAAADQVSLTLnnvsftypdqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiady 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 625 --------FAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNscclRPDLAILPNSDL---TEIGERGANLSGGQRQR 692
Cdd:PRK11160 408 seaalrqaISVVSQRVHLFSATLRDNLLLAApNASDEALIEVLQ----QVGLEKLLEDDKglnAWLGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 693 ISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
....*.
gi 16758936 773 LNGDYA 778
Cdd:PRK11160 563 QQGRYY 568
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
578-783 |
1.14e-27 |
|
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: 121.00 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILENLL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FG--KEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:TIGR01193 570 LGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 723 IFNSAIrkRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 783
Cdd:TIGR01193 650 IVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
575-759 |
1.43e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 110.03 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTfayvaQQAWILNATLRDNILFgkefdeery 654
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGY--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 655 nsvlnscclRPDLailpnsdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGnHIFNSAIRKRLKS 734
Cdd:cd00267 78 ---------VPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAEE 129
|
170 180
....*....|....*....|....*..
gi 16758936 735 -KTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd00267 130 gRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
272-466 |
2.30e-27 |
|
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: 113.85 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 272 SLGELINICSNDGQRMFEAAAVGSLLAGGPV--VAILGMIYNVIilGPTGFLGSAVFILFYPAMMFVSRLTAYFRRKCVA 349
Cdd:cd18593 95 TVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLqlIAVIYILWFEI--GWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 350 ATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLT 429
Cdd:cd18593 173 RTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILT 252
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16758936 430 AAQAFTVVTVFNS----MTFALkvtPFSVKSLSEASVAVDR 466
Cdd:cd18593 253 AERVFVTMALYNAvrltMTLFF---PFAIQFGSELSVSIRR 290
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1208-1415 |
2.37e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 112.20 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPvlfsgtvRSNL 1287
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP-------YASL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1288 DPF---------------NQYTEEQIWDALERTHMKECIA-QLPLKLesevmengdnfSVGERQLLCIARALLRHCKILI 1351
Cdd:COG1124 93 HPRhtvdrilaeplrihgLPDREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1352 LDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:COG1124 162 LDEPTSALDVSVqaeilNLL--KDLREER-GLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1192-1417 |
6.14e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 111.29 E-value: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVL-FSGTVR--------SNLDPFNQYTEE---QIWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCI 1339
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryPHLGLFGRPSAEdreAVEEALERTGLEH-LADRPV----------DELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1340 ARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
.
gi 16758936 1417 D 1417
Cdd:COG1120 229 E 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
580-772 |
9.76e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.15 E-value: 9.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT------------FAYVAQQAWI-LNATLRDNILF- 645
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALyPDLTVRENLRFf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 ------GKEFDEERYNSVLNSCclrpdlailpnsDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAh 718
Cdd:COG1131 98 arlyglPRKEARERIDELLELF------------GLTDaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 719 VGNHIFNSAIRkRLKS--KTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1131 165 EARRELWELLR-ELAAegKTVLLSTHYLeeaERL--CDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
578-761 |
1.22e-26 |
|
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: 107.69 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 fgkefdeerynsvlnscclrpdlailpnsdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIF 724
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 16758936 725 NSAIRK-RLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:cd03246 136 NQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
542-771 |
2.65e-26 |
|
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: 115.52 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 542 LAEQKGHLLLDS-DERPSPEEeegkqihagsmrlQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIA 620
Cdd:TIGR01842 310 LPEPEGHLSVENvTIVPPGGK-------------KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 621 VSG-------------TFAYVAQQAWILNATLRDNIL-FGKEFDEErynSVLNSCCLRP--DLAI-LPNSDLTEIGERGA 683
Cdd:TIGR01842 377 LDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPE---KIIEAAKLAGvhELILrLPDGYDTVIGPGGA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 684 NLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIrKRLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-EGEQALANAI-KALKARgiTVVVITHRPSLLGCVDKILVLQDGRI 531
|
250
....*....|
gi 16758936 762 TERGTHEELM 771
Cdd:TIGR01842 532 ARFGERDEVL 541
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
577-772 |
2.66e-26 |
|
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: 115.62 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNI 643
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 -LFGkEFDEERynsVLNSCclrpDLA-----I--LPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:COG4618 427 aRFG-DADPEK---VVAAA----KLAgvhemIlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 716 DAhVGNHIFNSAIRkRLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:COG4618 499 DD-EGEAALAAAIR-ALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1192-1417 |
3.67e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPvlfsgtvrsnlDpfNQY----TEEQIWDALE-----RTHMKECIAQLPLKLEsevMEN-----GDNFSVGERQLL 1337
Cdd:PRK13632 88 IFQNP-----------D--NQFigatVEDDIAFGLEnkkvpPKKMKDIIDDLAKKVG---MEDyldkePQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1338 CIARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
..
gi 16758936 1416 ND 1417
Cdd:PRK13632 232 NK 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
578-778 |
5.59e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 114.67 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrnIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKE--FDEERYNSVLNSCCLrpDLaILPNSD--LTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:PRK13657 431 VGRPdaTDEEMRAAAERAQAH--DF-IERKPDgyDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 721 NHIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:PRK13657 508 AKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
578-781 |
5.91e-26 |
|
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: 114.60 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIdintvtreslrksIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKE--FDEERYNSVLNSCCLRPDLAILPNSDlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:TIGR01192 431 LGREgaTDEEVYEAAKAAAAHDFILKRSNGYD-TLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEAR 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 723 IFNsAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF 781
Cdd:TIGR01192 510 VKN-AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
578-761 |
7.61e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.82 E-value: 7.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 F-----GKEFDEERYNSVLNSCCLRPDLAilpNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHv 719
Cdd:COG4619 96 FpfqlrERKFDRERALELLERLGLPPDIL---DKPVER-------LSGGERQRLALIRALLLQPDVLLLDEPTSALDPE- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16758936 720 gN-HIFNSAIRKRLKSK--TVLFVTH---QLQYLvdCDEVIFMKEGCI 761
Cdd:COG4619 165 -NtRRVEELLREYLAEEgrAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
580-765 |
9.61e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.60 E-value: 9.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIavsgtfayvaqqawilnatlrdnILFGKEFDEerynsvLN 659
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-----------------------LLDGKDLAS------LS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 660 SCCLRPDLAILPNS----DLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KRLK 733
Cdd:cd03214 68 PKELARKIAYVPQAlellGLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlARER 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 16758936 734 SKTVLFVTHQL----QYlvdCDEVIFMKEGCITERG 765
Cdd:cd03214 148 GKTVVMVLHDLnlaaRY---ADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
577-759 |
1.02e-25 |
|
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: 106.40 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------------FAYVAQQawILNATL 639
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkvglvFQNPDDQ--FFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNILFGKE---FDEERYNSVLNSCCLRPDLAILPNSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:cd03225 94 EEEVAFGLEnlgLPEEEIEERVEEALELVGLEGLRDRSP-------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16758936 717 AHVGNHIFnsAIRKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd03225 167 PAGRRELL--ELLKKLKAegKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
575-765 |
2.70e-25 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 105.67 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------------FAYVAQQA------ 632
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMVFQDPmsslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 633 -----WILNATLRDN-ILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISLARALYSDRSI 705
Cdd:cd03257 98 rmtigEQIAEPLRIHgKLSKKEARKEAVLLLLVGVGLPEEVLnRYPHE-----------LSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 706 YILDDPLSALDAHVGNHIFNsaIRKRLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERG 765
Cdd:cd03257 167 LIADEPTSALDVSVQAQILD--LLKKLQEElglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
578-756 |
3.11e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 106.71 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------FAYVAQQA----WilnATLRDNILF 645
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpW---LTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 G-------KEFDEERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALDA- 717
Cdd:COG1116 104 GlelrgvpKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16758936 718 ---HVGNHIFNsaIRKRLKsKTVLFVTHqlqylvDCDEVIFM 756
Cdd:COG1116 173 treRLQDELLR--LWQETG-KTVLFVTH------DVDEAVFL 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
580-772 |
3.35e-25 |
|
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: 106.28 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWI-LNATLRDNILF 645
Cdd:COG1120 19 DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEPPApFGLTVRELVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 G-----------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:COG1120 99 GryphlglfgrpSAEDREAVEEALERT------------GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 714 ALD-AH---VGNHIfnsairKRL---KSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1120 167 HLDlAHqleVLELL------RRLareRGRTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1208-1413 |
3.66e-25 |
|
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: 105.34 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRISDIGLAD--LRSKLTIIPQEPVLFS 1280
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegeVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1281 GTVRSNLD--------PFNQYTEEQIWDALERTHMKEciaqlplklesEVME--NGDNFSVGERQLLCIARALLRHCKIL 1350
Cdd:cd03260 95 GSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWD-----------EVKDrlHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758936 1351 ILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVL 1413
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
575-761 |
3.94e-25 |
|
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: 104.91 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQaWIL--NATLRD 641
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD-YALfpHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFG----KEFDEERYNSVLNScclrpdLAILpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:cd03259 92 NIAFGlklrGVPKAEIRARVREL------LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 717 AHVgnhifNSAIRKRLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCI 761
Cdd:cd03259 163 AKL-----REELREELKElqrelgITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1192-1427 |
4.07e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.94 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLTI 1271
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQE-------PVlfsgTVR----SNLDP----FNQYTE---EQIWDALERTHMKE----CIAQLplklesevmengdnf 1329
Cdd:COG1121 80 VPQRaevdwdfPI----TVRdvvlMGRYGrrglFRRPSRadrEAVDEALERVGLEDladrPIGEL--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1330 SVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 1407
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHG 220
|
250 260
....*....|....*....|
gi 16758936 1408 DTPSVLLSNDSSRFYAMCAA 1427
Cdd:COG1121 221 PPEEVLTPENLSRAYGGPVA 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
578-761 |
4.75e-25 |
|
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: 103.25 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVsgtfayvaqqawilnatlrdnilFGKEFDEERyNSV 657
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 658 LNSCCLRPDLAILPnSDLTeiGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIRKRLKS-KT 736
Cdd:cd03230 72 KRRIGYLPEEPSLY-ENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRELKKEgKT 147
|
170 180
....*....|....*....|....*.
gi 16758936 737 VLFVTHQLQYLVD-CDEVIFMKEGCI 761
Cdd:cd03230 148 ILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
580-776 |
7.94e-25 |
|
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: 104.94 E-value: 7.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGtFAYVAQQAWILNA--------------TLRDNI-L 644
Cdd:COG4555 19 DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQigvlpderglydrlTVRENIrY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FG---KEFDEERYNSVLNscclrpdlaILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVG 720
Cdd:COG4555 98 FAelyGLFDEELKKRIEE---------LIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 721 NHIFNSAIRkRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNLNGD 776
Cdd:COG4555 168 RRLLREILR-ALKKegKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1188-1411 |
9.81e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.87 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1188 QEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS 1267
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1268 KLTIIPQEP-VLFSG-TVRSNLdPF---NQYTE-----EQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLL 1337
Cdd:PRK13635 82 QVGMVFQNPdNQFVGaTVQDDV-AFgleNIGVPreemvERVDQALRQVGMEDFLNREPHRL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1338 CIARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPS 1411
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
909-1400 |
1.56e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 112.04 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 909 FLQYYASIYALSMAVMLILKAIRgVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFskdmdevdvrlpfq 988
Cdd:PTZ00265 111 FILSFISSFCMDVVTTKILKTLK-LEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKF-------------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 989 aemfiqnvILVFFCVGMIAGVFPWFLVAVGPLLI----LFSVLHIVSRVLIRELK---RLDNITQSPFLSHITSSIQGLA 1061
Cdd:PTZ00265 176 --------ITIFTYASAFLGLYIWSLFKNARLTLcitcVFPLIYICGVICNKKVKinkKTSLLYNNNTMSIIEEALVGIR 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1062 TIHAYNKRQEFLHRYQeLLDDNQAPFFLFTCAMRWLAVRLD----LISIALITTTGLMIVL--MHGQIPSA--YAGLAIS 1133
Cdd:PTZ00265 248 TVVSYCGEKTILKKFN-LSEKLYSKYILKANFMESLHIGMIngfiLASYAFGFWYGTRIIIsdLSNQQPNNdfHGGSVIS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1134 YAVQ-LTGLFQFTVRLASETEarftsverinhYIKtlSLEAPA---RIKNKAPPHDWPQEGE-------ITFENAEMRY- 1201
Cdd:PTZ00265 327 ILLGvLISMFMLTIILPNITE-----------YMK--SLEATNslyEIINRKPLVENNDDGKklkdikkIQFKNVRFHYd 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1202 -RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKI-DGVRISDIGLADLRSKLTIIPQEPVLF 1279
Cdd:PTZ00265 394 tRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLF 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 SGTVRSN----------LDPFNQYTEE---------------------------QIWDALERTHMK-------------- 1308
Cdd:PTZ00265 473 SNSIKNNikyslyslkdLEALSNYYNEdgndsqenknkrnscrakcagdlndmsNTTDSNELIEMRknyqtikdsevvdv 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1309 -------ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTML 1381
Cdd:PTZ00265 553 skkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
570 580
....*....|....*....|.
gi 16758936 1382 T--IAHRLHTVLGSDRIMVLA 1400
Cdd:PTZ00265 633 TiiIAHRLSTIRYANTIFVLS 653
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
578-756 |
1.58e-24 |
|
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: 103.32 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------FAYVAQQA----WilnATLRDNILF 645
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 GkefdeerynsvlnscclrPDLAILPNSDLTEIGER---------GAN-----LSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:cd03293 97 G------------------LELQGVPKAEARERAEEllelvglsgFENayphqLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 712 LSALDAHVGNHIFN--SAIRKRLKsKTVLFVTHqlqylvDCDEVIFM 756
Cdd:cd03293 159 FSALDALTREQLQEelLDIWRETG-KTVLLVTH------DIDEAVFL 198
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
864-1166 |
2.66e-24 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 104.60 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 864 LFMLNVGSTAFSTWWLSYWIKQgSGNSTVFEGnrssvsdsmrdnpflQYYASIYALSMAVMLILKAIRGVVFVKGTLRAS 943
Cdd:cd18559 7 LVLCNHVFSGPSNLWLLLWFDD-PVNGPQEHG---------------QVYLSVLGALAILQGITVFQYSMAVSIGGIFAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 944 SRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF---IQNVILVFFcvgMIAGVFPWFLVAVgPL 1020
Cdd:cd18559 71 RAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWmgpLQNVIGLYL---LILLAGPMAAVGI-PL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1021 LILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRyQELLDDNQAPFFLFTCAMRWLAVR 1100
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQ-VDAKRDNELAYLPSIVYLRALAVR 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1101 LDLISIALITTTGLMIVLMHGQIpSAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1166
Cdd:cd18559 226 LWCVGPCIVLFASFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
575-789 |
2.95e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 109.42 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRD 641
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 721
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 722 HIfNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNLLLGET 789
Cdd:PRK10790 514 AI-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
575-753 |
3.29e-24 |
|
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: 101.79 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT------------FAYVAQQ-AWILNATLR 640
Cdd:COG4133 14 ERLLFsGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHAdGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILF-----GKEFDEERYNSVLnscclrpdlAILpnsDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG4133 94 ENLRFwaalyGLRADREAIDEAL---------EAV---GLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16758936 715 LDAHvGNHIFNSAIRKRLKS-KTVLFVTHQLQYLVDCDEV 753
Cdd:COG4133 162 LDAA-GVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
575-772 |
3.79e-24 |
|
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: 102.58 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------------FAYVAQQAWILNA- 637
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 TLRDNILF-----GKEFDEERYNSV---LNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:cd03261 93 TVFENVAFplrehTRLSEEEIREIVlekLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 710 DPLSALDAhVGNHIFNSAIR--KRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1195-1405 |
4.78e-24 |
|
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: 100.59 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1195 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQ 1274
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1275 epvlfsgtvrsnldpfnqyteeqiwdALERT---HMKEC-IAQLplklesevmengdnfSVGERQLLCIARALLRHCKIL 1350
Cdd:cd03214 81 --------------------------ALELLglaHLADRpFNEL---------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1351 ILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRL-HTVLGSDRIMVLAQGQVV 1405
Cdd:cd03214 120 LLDEPTSHLDiahqIELLELLRRLARE--RGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
580-772 |
5.95e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 107.68 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------------FAYVAQ----QawiLNA-- 637
Cdd:COG1123 283 DVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelrrrVQMVFQdpysS---LNPrm 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 TLRDNILFG--------KEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:COG1123 360 TVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDLA----------DRYPHELSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 710 DPLSALDAHVGNHIFN--SAIRKRLKsKTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1123 430 EPTSALDVSVQAQILNllRDLQRELG-LTYLFISHDLA-VVRyiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
578-770 |
6.79e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.84 E-value: 6.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGqmtlLE----GSIAVSGT--F----------AYVAQQAwilnA---- 637
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGRdlFtnlpprerrvGFVFQHY----Alfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 -TLRDNILFGkefdeerynsvlnscclrpdLAILPNS---------------DLTEIGER-GANLSGGQRQRISLARALY 700
Cdd:COG1118 90 mTVAENIAFG--------------------LRVRPPSkaeirarveellelvQLEGLADRyPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 701 SDRSIYILDDPLSALDAHVgnhifnsaiRKRLKSK----------TVLFVTHQLQ--YLVdCDEVIFMKEGCITERGTHE 768
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKV---------RKELRRWlrrlhdelggTTVFVTHDQEeaLEL-ADRVVVMNQGRIEQVGTPD 219
|
..
gi 16758936 769 EL 770
Cdd:COG1118 220 EV 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1192-1403 |
7.78e-24 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 99.95 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG--LADLRSKL 1269
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSG-TVRSNLdpfnqyteeqiwdalerthmkeciaQLPLklesevmengdnfSVGERQLLCIARALLRHCK 1348
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------------------ALGL-------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1349 ILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQ 1403
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
574-766 |
9.72e-24 |
|
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: 100.56 E-value: 9.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 574 LQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLR 640
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNI-LFGKEFDEERYNSVlnscclrpdlailpnsdltEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 719
Cdd:cd03369 100 SNLdPFDEYSDEEIYGAL-------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 720 gNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 766
Cdd:cd03369 161 -DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1154-1386 |
1.01e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1154 ARFTS-VERINHYIKtlSLEAPARIKNKAPPHDWPQEGEITFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGK 1232
Cdd:COG4178 326 AEWRAtVDRLAGFEE--ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1233 SSLgmalFRLveLSG------GCIKI-DGVRISdigladlrskltIIPQEPVLFSGTVRSNL---DPFNQYTEEQIWDAL 1302
Cdd:COG4178 403 STL----LRA--IAGlwpygsGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1303 ERTHMKECIAQLplkleSEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLT 1382
Cdd:COG4178 465 EAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVIS 539
|
....
gi 16758936 1383 IAHR 1386
Cdd:COG4178 540 VGHR 543
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1212-1410 |
1.10e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 103.59 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGVRISDIGLADLR----SKLTIIPQEPVlfsgtvr 1284
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLDPFnqYT-EEQIWDALeRTH-------MKECIAQLpLKL-----ESEVMengDN----FSVGERQLLCIARALLRHC 1347
Cdd:COG0444 97 TSLNPV--MTvGDQIAEPL-RIHgglskaeARERAIEL-LERvglpdPERRL---DRypheLSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1348 KILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTP 1410
Cdd:COG0444 170 KLLIADEPTTALDVTIqaqilNLLKD--LQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelFENP 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1209-1406 |
1.15e-23 |
|
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: 107.08 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLTIIPQEPvlFsgtvrS 1285
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-----G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 NLDPfnQYTEEQI-----------WDALERTHMkecIAQLpLK---LESEVM-----EngdnFSVGERQLLCIARALLRH 1346
Cdd:COG4172 374 SLSP--RMTVGQIiaeglrvhgpgLSAAERRAR---VAEA-LEevgLDPAARhryphE----FSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1347 CKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHRLHTV--LgSDRIMVLAQGQVVE 1406
Cdd:COG4172 444 PKLLVLDEPTSAL----DVSVQAQILDLLRDlqrehgLAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
580-713 |
1.25e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 98.49 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNA-TLRDNILF 645
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPRlTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 646 GKEFdEERYNSVLNScclRPDLAI--LPNSDL--TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:pfam00005 83 GLLL-KGLSKREKDA---RAEEALekLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1194-1402 |
2.82e-23 |
|
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: 99.53 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1194 FENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLTIIP 1273
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1274 QE-------PVLFSGTVRSNLDP----FNQYTEEQ---IWDALERTHMKE----CIAQLplklesevmengdnfSVGERQ 1335
Cdd:cd03235 75 QRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSEladrQIGEL---------------SGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1336 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGS-DRIMVLAQG 1402
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1192-1404 |
3.76e-23 |
|
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: 97.85 E-value: 3.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLTI 1271
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSG-TVRSNLDpfnqyteeqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKIL 1350
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1351 ILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 1404
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1192-1416 |
6.55e-23 |
|
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: 99.19 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGVRISDIGLADL 1265
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGlerpTSGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1266 ---RSKLTIIPQEPVLFSG-TVRSNLD-PFnqyteeQIWdALERTHMKECIAQLpLK---LESEVMENGDNFSVGERQLL 1337
Cdd:cd03258 78 rkaRRRIGMIFQHFNLLSSrTVFENVAlPL------EIA-GVPKAEIEERVLEL-LElvgLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1338 CIARALLRHCKILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1411
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETtqsilALLRD--INREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 16758936 1412 VLLSN 1416
Cdd:cd03258 227 EVFAN 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
578-759 |
2.81e-22 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 95.33 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIavsgtfayvaqqaWILNATLRDNILFGKEFdEERYNSV 657
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-------------LIDGEDLTDLEDELPPL-RRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 658 LNSCCLRPDLAILPNsdlteIGERganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI--FNSAIRKRLKsK 735
Cdd:cd03229 82 FQDFALFPHLTVLEN-----IALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVraLLKSLQAQLG-I 152
|
170 180
....*....|....*....|....*
gi 16758936 736 TVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd03229 153 TVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1212-1406 |
3.62e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.42 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLTIIPQEPvlfsgtvRSNLD 1288
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-------YASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1289 PfnQYTEEQI----------WDALERthmKECIAQLPLK--LESEVM-----EngdnFSVGERQLLCIARALLRHCKILI 1351
Cdd:COG4608 110 P--RMTVGDIiaeplrihglASKAER---RERVAELLELvgLRPEHAdryphE----FSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1352 LDEATAAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRL----HTvlgSDRIMVLAQGQVVE 1406
Cdd:COG4608 181 CDEPVSAL----DVSIQaqvlnllEDLQDEL-GLTYLFISHDLsvvrHI---SDRVAVMYLGKIVE 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
565-759 |
5.28e-22 |
|
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: 96.02 E-value: 5.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 565 KQIHAGSMRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------------FAY 627
Cdd:cd03255 8 KTYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 628 VAQQAWILNA-TLRDNILFGKEF-------DEERYNSVLNSCCLRPDLAILPNsdlteigergaNLSGGQRQRISLARAL 699
Cdd:cd03255 87 VFQSFNLLPDlTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 700 YSDRSIYILDDPLSALDAHVGNHIFNsAIRK--RLKSKTVLFVTHQLQYLVDCDEVIFMKEG 759
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVME-LLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
580-765 |
5.39e-22 |
|
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: 95.82 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGkLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------------FAYVAQQAWIL-NATLRD 641
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGKEFDEERYNSVlnscclRPDlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:cd03297 95 NLAFGLKRKRNREDRI------SVD-ELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758936 721 NHIFNSaIRKRLKS--KTVLFVTH---QLQYLvdCDEVIFMKEGCITERG 765
Cdd:cd03297 168 LQLLPE-LKQIKKNlnIPVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
578-770 |
5.57e-22 |
|
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: 96.50 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------------FAYVAQQAWILNA-TLR 640
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMIFQHFNLLSSrTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILF-------GKEFDEERYNSVLNscclrpdlailpnsdLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:cd03258 101 ENVALpleiagvPKAEIEERVLELLE---------------LVGLEDKAdaypAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758936 710 DPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:cd03258 166 EATSALDPETTQSILAllRDINRELGL-TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
578-771 |
5.94e-22 |
|
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: 96.25 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------------FAYVAQQawILNATLR 640
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlrelrrkvglvFQNPDDQ--LFAPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFG-------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG1122 95 EDVAFGpenlglpREEIRERVEEALELV------------GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 713 SALDAHVGNHIFNsAIRK-RLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:COG1122 163 AGLDPRGRRELLE-LLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
576-778 |
9.42e-22 |
|
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: 101.96 E-value: 9.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AVSGTFAYVAQQAWILNATLRDN 642
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqdlagldvqAVRRQLGVVLQNGRLMSGSIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD----AH 718
Cdd:TIGR03797 547 IAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDnrtqAI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 719 VgnhifnSAIRKRLKSkTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 778
Cdd:TIGR03797 627 V------SESLERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
576-772 |
1.14e-21 |
|
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: 95.48 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFA-----------YVAQQ-AWILNATLRDNI 643
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 LFGKEFDEERYnsvlnscclRPDLA--------ILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:cd03296 96 AFGLRVKPRSE---------RPPEAeirakvheLLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 715 LDAHVgnhifnsaiRKRLKS----------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03296 167 LDAKV---------RKELRRwlrrlhdelhVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1208-1405 |
3.27e-21 |
|
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: 91.72 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrskltiipqEPVLFSGtvrsnl 1287
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFAS------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1288 dpfnqyteeqIWDALErtHMKECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAM-DTETDLL 1366
Cdd:cd03216 69 ----------PRDARR--AGIAMVYQL---------------SVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16758936 1367 IqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:cd03216 122 F-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1192-1406 |
3.82e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.58 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 1268
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1269 LTIIPQE-PVLFSGTVRSNL---------DPfnQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 1338
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgkSR--KEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1339 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREafADCTMLtIA-HRLHTVLGSD-RIMVLAQGQVVE 1406
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsweimELL--EEINR--RGTTVL-IAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
576-772 |
5.65e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.44 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILG---QMTLLEGSIAVSGT-------------FAYVAQQAWI-LN-A 637
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMTqLNpV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 TLRDNILFGKEFD----EERYNSVLnscclrpdlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG1123 100 TVGDQIAEALENLglsrAEARARVL---------ELLEAVGLERRLDRYpHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 713 SALDAHVGNHIFnSAIRK--RLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1123 171 TALDVTTQAEIL-DLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
578-761 |
6.12e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 93.30 E-value: 6.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNIL 644
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FG---KEFDE-----ERYNSVLNscclrpdLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:cd03248 110 YGlqsCSFECvkeaaQKAHAHSF-------ISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16758936 717 AHvGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:cd03248 183 AE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1192-1404 |
6.49e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 92.94 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE-LSGGCIKIDGV---RISDIGLADL 1265
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTdisKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1266 R-SKLTIIPQEPVLFSG-TVRSNLD-------PFNQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQL 1336
Cdd:cd03255 80 RrRHIGFVFQSFNLLPDlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1337 LCIARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1404
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
578-763 |
6.81e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 93.18 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISaILGqmTLL---EGSIAVSGT-----------------FAYVAQQAWIL-N 636
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILG--GLDrptSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLpE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 637 ATLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSI 705
Cdd:COG1136 101 LTALENVALplllagvSRKERRERARELL---------------ERVGLGDRLdhrpSQLSGGQQQRVAIARALVNRPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 706 YILDDPLSALDAHVGNHIFN--SAIRKRLKsKTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:COG1136 166 ILADEPTGNLDSKTGEEVLEllRELNRELG-TTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1208-1420 |
7.79e-21 |
|
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: 92.95 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLTIIPQEPVLFSG-TV 1283
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMGMLFQSGALFDSlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 RSNLD-PFNQYTEEQIWDALERThmKECIAQLPLKLESEVMEngDNFSVGERQLLCIARALLRHCKILILDEATAAMD-- 1360
Cdd:cd03261 95 FENVAfPLREHTRLSEEEIREIV--LEKLEAVGLRGAEDLYP--AELSGGMKKRVALARALALDPELLLYDEPTAGLDpi 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1361 --TETDLLIQeTIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1420
Cdd:cd03261 171 asGVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
576-770 |
7.85e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.91 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQaWIL--NATLRDN 642
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQS-YALypHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFG-------KEFDEERYNSVLnscclrpdlAILpnsDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG3839 96 IAFPlklrkvpKAEIDRRVREAA---------ELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 715 LDAHVGNH----IfnSAIRKRLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:COG3839 164 LDAKLRVEmraeI--KRLHRRLGT-TTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1192-1386 |
8.07e-21 |
|
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: 91.06 E-value: 8.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlRSKLTI 1271
Cdd:cd03223 1 IELENLSLATPDGRVLL-KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVRsnldpfnqyteEQI---WDalerthmkeciaqlplklesevmengDNFSVGERQLLCIARALLRHCK 1348
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 16758936 1349 ILILDEATAAMDTETDLLIQETIREAFAdcTMLTIAHR 1386
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1208-1406 |
1.07e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLTIIPQEPVLFSG-TVR 1284
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDA-QAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLdpF--NQYTEEQI--WDALERThMKECIAQL--PLKLESEVMEngdnFSVGERQLLCIARALLRHCKILILDEATAA 1358
Cdd:COG1129 98 ENI--FlgREPRRGGLidWRAMRRR-ARELLARLglDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1359 M-DTETDLLIqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:COG1129 171 LtEREVERLF-RIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1208-1416 |
1.62e-20 |
|
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: 91.73 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIgLADLRSKLTI--IPQEPVLFSG-TVR 1284
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL-PPHERARAGIgyVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNL--------DPFNQYTEEQIWDALERthMKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEAT 1356
Cdd:cd03224 94 ENLllgayarrRAKRKARLERVYELFPR--LKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1357 A----AMDTEtdllIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:cd03224 161 EglapKIVEE----IFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1192-1423 |
4.00e-20 |
|
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: 91.21 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSG-TVRSN--LDP-FNQYTEEQIwdaleRTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHC 1347
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKI-----RERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1348 KILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEFDTPS 1411
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFK-------------RLQQELGktivfvthdideafrlADRIAIMKNGEIVQVGTPD 221
|
250
....*....|..
gi 16758936 1412 VLLSNDSSRFYA 1423
Cdd:cd03295 222 EILRSPANDFVA 233
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
239-467 |
4.39e-20 |
|
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: 92.23 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 239 TWALNyRTGVRLRGAVLTMAF--KKILKLKNIKEKSLGELINICSNDGQRMfeAAAVGSL--LAGGPV-VAI-LGMIY-- 310
Cdd:cd18598 59 NFQMN-KVSLKVRAALVTAVYrkALRVRSSSLSKFSTGEIVNLMSTDADRI--VNFCPSFhdLWSLPLqIIVaLYLLYqq 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 311 -NVIILGptgflGSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEER 389
Cdd:cd18598 136 vGVAFLA-----GLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKEL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 390 RILEKAGYFQSITV---GVAPIVVviaSVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18598 211 KALKGRKYLDALCVyfwATTPVLI---SILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKR 287
|
.
gi 16758936 467 F 467
Cdd:cd18598 288 L 288
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1192-1373 |
5.92e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 89.85 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLTI 1271
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSG-TVRSNLDpF------NQYTEEQIWDALERTHMKECiAQLPLKlesevmengdNFSVGERQLLCIARALL 1344
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGL-ADLPVR----------QLSAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*....
gi 16758936 1345 RHCKILILDEATAAMDTETDLLIQETIRE 1373
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
578-770 |
8.36e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.84 E-value: 8.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDNILF 645
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 GKEFDEERYnsvlnscclRPDLAI--------LPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:PRK10851 98 GLTVLPRRE---------RPNAAAikakvtqlLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 717 AHVgnhifnsaiRKRLKS---------K-TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK10851 169 AQV---------RKELRRwlrqlheelKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
580-770 |
9.41e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.47 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQAwilnA-----TLRDNI 643
Cdd:COG3842 23 DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDY----AlfphlTVAENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 LFG-------KEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG3842 99 AFGlrmrgvpKAEIRARVAELL---------------ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 713 SALDAHVGNH----IFNsaIRKRLKsKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:COG3842 164 SALDAKLREEmreeLRR--LQRELG-ITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
573-776 |
1.88e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.04 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFAYVAQ-------QAWILNA--TLR 640
Cdd:COG3840 10 RYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAErpvsmlfQENNLFPhlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGkefdeerynsvlnsccLRPDL-----------AILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:COG3840 90 QNIGLG----------------LRPGLkltaeqraqveQALERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 709 DDPLSALD--------AHVgnhifnSAIRKRLKSkTVLFVTHQLQylvD----CDEVIFMKEGCITERGTHEELMNLNGD 776
Cdd:COG3840 154 DEPFSALDpalrqemlDLV------DELCRERGL-TVLMVTHDPE---DaariADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1192-1424 |
2.65e-19 |
|
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: 88.99 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSL-GMALFRLVELSGGCIKIDGVRISDIGLADLRSKL- 1269
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 --------TIIPQEPVL------FSGTVrsnlDPFNQYTEEQI---WDALERTHMKECIAQLPLKLesevmengdnfSVG 1332
Cdd:COG1119 82 lvspalqlRFPRDETVLdvvlsgFFDSI----GLYREPTDEQReraRELLELLGLAHLADRPFGTL-----------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1333 ERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF-D 1408
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAgP 226
|
250
....*....|....*.
gi 16758936 1409 TPSVLLSNDSSRFYAM 1424
Cdd:COG1119 227 KEEVLTSENLSEAFGL 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
573-771 |
3.83e-19 |
|
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: 90.93 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQR---TLyNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------------FAYVAQQA 632
Cdd:COG4148 8 RLRRggfTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 633 wILNATL--RDNILFG-----KEFDEERYNSVLnscclrpdlailpnsDLTEIG---ERG-ANLSGGQRQRISLARALYS 701
Cdd:COG4148 87 -RLFPHLsvRGNLLYGrkrapRAERRISFDEVV---------------ELLGIGhllDRRpATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 702 DRSIYILDDPLSALDAHvgnhifnsaiRK--------RLKSKT---VLFVTHQL---QYLvdCDEVIFMKEGCITERGTH 767
Cdd:COG4148 151 SPRLLLMDEPLAALDLA----------RKaeilpyleRLRDELdipILYVSHSLdevARL--ADHVVLLEQGRVVASGPL 218
|
....
gi 16758936 768 EELM 771
Cdd:COG4148 219 AEVL 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
578-770 |
4.29e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 87.62 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAVSG---------------TFAYVAQQAWILNA 637
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 TLRDNILFG--------KEFDEERYNSVLnscclrpDLAILPNsdltEIGER--GANLSGGQRQRISLARALYSDRSIYI 707
Cdd:cd03260 96 SIYDNVAYGlrlhgiklKEELDERVEEAL-------RKAALWD----EVKDRlhALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758936 708 LDDPLSALDAhVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 770
Cdd:cd03260 165 LDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
575-770 |
4.64e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.27 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAIlgqmTLLE---------GSIAVSGTFAYVAQQAWILNatLRDNILF 645
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeagtirvGDITIDTARSLSQQKGLIRQ--LRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 -GKEFDEERYNSVLNSCCLRP--------DLAI-LPNSDLTEIGERGAN------LSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK11264 90 vFQNFNLFPHRTVLENIIEGPvivkgepkEEATaRARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 710 DPLSALDAHVGNHIFNSaIRKRLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:PRK11264 170 EPTSALDPELVGEVLNT-IRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1208-1411 |
4.66e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.46 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLTIIPQEPvlfsgtvR 1284
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLDPfnQYTEEQIWDALERTHMKECIAQLPLKLESEVMEN-----------GDNFSVGERQLLCIARALLRHCKILILD 1353
Cdd:PRK15134 373 SSLNP--RLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvgldpetrhryPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1354 EATAAMDTETD-----LL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTPS 1411
Cdd:PRK15134 451 EPTSSLDKTVQaqilaLLksLQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVEqgdcervFAAPQ 518
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1192-1411 |
4.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.34 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLR 1266
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1267 SKLTIIPQEP--VLFSGTVRSNLD--PFN-QYTEEQIWDALERThMKEciaqlpLKLESEVMENGDNF--SVGERQLLCI 1339
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAfgPINlGLSEEEIENRVKRA-MNI------VGLDYEDYKDKSPFelSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1340 ARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI--AHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1411
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlvSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1208-1408 |
5.46e-19 |
|
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: 87.19 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADLRSKLTIIPQEPVLFSG-TVRSN 1286
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVFQDYALFPHlTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LDpF--------NQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 1358
Cdd:cd03259 93 IA-FglklrgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1359 MDTETDLLIQETIREAFA--DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1408
Cdd:cd03259 161 LDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
578-759 |
6.73e-19 |
|
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: 86.45 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTL--LEGSIAVSGT----------FAYVAQQ-AWILNATLRDNIL 644
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrkiIGYVPQDdILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FgkefdeerynsvlnSCCLRpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIF 724
Cdd:cd03213 105 F--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 16758936 725 NSAIRKRLKSKTVLFVTHQLQYLV--DCDEVIFMKEG 759
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1209-1402 |
6.92e-19 |
|
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: 87.00 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSK----LTIIPQEPVLFSGTVR 1284
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNL---DPFNQYTEEQIWDALErthMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1361
Cdd:cd03290 97 ENItfgSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16758936 1362 E-TDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQG 1402
Cdd:cd03290 174 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1192-1415 |
7.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLP-LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLT 1270
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1271 IIPQEP-VLFSG-TVRSNLdPF---NQ---YTE--EQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIA 1340
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDV-AFgleNKgipHEEmkERVNEALELVGMQDFKEREPARL-----------SGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1341 RALLRHCKILILDEATAAMDTETDL-LIQ--ETIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLeLIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1208-1404 |
8.18e-19 |
|
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: 86.43 E-value: 8.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKLTIIPQEPVLFSG-TVR 1284
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLdpfnqyTEEQIW--------------DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKIL 1350
Cdd:cd03262 95 ENI------TLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1351 ILDEATAAMDTEtdlLIQE---TIREAFAD-CTMLTIAHRlhtvLG-----SDRIMVLAQGQV 1404
Cdd:cd03262 158 LFDEPTSALDPE---LVGEvldVMKDLAEEgMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
578-772 |
1.21e-18 |
|
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: 86.62 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDNILF 645
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 G----KEFDEERYNSVLNsccLRPDLAIlpnsdlTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVg 720
Cdd:cd03299 95 GlkkrKVDKKEIERKVLE---IAEMLGI------DHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 721 nhifNSAIRKRLK------SKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03299 165 ----KEKLREELKkirkefGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
244-466 |
1.23e-18 |
|
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: 88.04 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 244 YRTGVRLRGAVLTMAFKKILKLKNIKEKS--LGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFL 321
Cdd:cd18559 63 SIGGIFASRAVHLDLYHKALRSPISFFERtpSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 322 GSAVFILFYPAMMFVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSI 401
Cdd:cd18559 143 GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAL 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 402 TVGVAPIVVVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd18559 223 AVRLWCVGPCIVLFASFFAYVSRHSLagLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1208-1416 |
1.23e-18 |
|
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: 86.72 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDIGlADLRSKLTIIP--QEPVLFSG 1281
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 -TVRSNLD---------------PFNQYTE--EQIWDALERTHMKEciaqlplKLESEVmengDNFSVGERQLLCIARAL 1343
Cdd:cd03219 90 lTVLENVMvaaqartgsglllarARREEREarERAEELLERVGLAD-------LADRPA----GELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1344 LRHCKILILDEATAAM-DTETDLLIqETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:cd03219 159 ATDPKLLLLDEPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
913-1354 |
1.52e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 91.01 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 913 YASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMD---EVDVRLPFqa 989
Cdd:COG4615 50 LLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 990 emFIQNVILVFFCVGMIAgvfpW-----FLVAVGPLLILFSVLHIVSRVLIRELKRLDNiTQSPFLSHITSSIQGLA--T 1062
Cdd:COG4615 128 --LLQSVALVLGCLAYLA----WlspplFLLTLVLLGLGVAGYRLLVRRARRHLRRARE-AEDRLFKHFRALLEGFKelK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1063 IHAyNKRQEFLHRY-----QELLDDNQAPFFLFTCAMRWlavrldlISIALITTTGLmIVLMHGQIPSAYAGLAISYAvq 1137
Cdd:COG4615 201 LNR-RRRRAFFDEDlqptaERYRDLRIRADTIFALANNW-------GNLLFFALIGL-ILFLLPALGWADPAVLSGFV-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1138 LTGLF------QFTVRLASETEARfTSVERINHYikTLSLEAPARIKNKAPPHDWPQE-GEITFENAEMRYR---ENLPL 1207
Cdd:COG4615 270 LVLLFlrgplsQLVGALPTLSRAN-VALRKIEEL--ELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPgedGDEGF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFsgtvRSNL 1287
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1288 DPFNQYTEEQIWDALERthmkeciaqlpLKLESEVMENGDNF-----SVGERQLLCIARALLRHCKILILDE 1354
Cdd:COG4615 423 GLDGEADPARARELLER-----------LELDHKVSVEDGRFsttdlSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1192-1405 |
1.98e-18 |
|
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: 85.50 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRSKL 1269
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSG-TVRSNLDPFNQYTeeqiwdALERTHMKECIAQLPLKLE-SEVME-NGDNFSVGERQLLCIARALLRH 1346
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLY------GLKGDELTARLEELADRLGmEELLDrRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1347 CKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
580-772 |
2.26e-18 |
|
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: 86.20 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQAWIL-NATLRDNI-- 643
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVEENIal 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 ---LFG--KEFDEERYNSVLNSCCLRPdlailpnsdlTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03295 99 vpkLLKwpKEKIRERADELLALVGLDP----------AEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 718 HVGNHIFNSAIR-KRLKSKTVLFVTHQLQ-YLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03295 169 ITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1208-1416 |
2.28e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 86.63 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISdiGL-ADLRSKLTI-----IPQepv 1277
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDIT--GLpPHRIARLGIartfqNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1278 LFSG-TVRSN-----------------LDPFNQYTEE-----QIWDALERTHMKECIAQLPlklesevmengDNFSVGER 1334
Cdd:COG0411 90 LFPElTVLENvlvaaharlgrgllaalLRLPRARREEreareRAEELLERVGLADRADEPA-----------GNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1335 QLLCIARALLRHCKILILDEATAAM-DTETDLLIqETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1410
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTP 237
|
....*.
gi 16758936 1411 SVLLSN 1416
Cdd:COG0411 238 AEVRAD 243
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1208-1417 |
2.30e-18 |
|
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: 85.80 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGL-ADLRSKLTI--IPQEPVLFSG-TV 1283
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLpPHRIARLGIgyVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 RSNLD--PFNQYTEEQIWDALERTH-----MKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEAT 1356
Cdd:COG0410 96 EENLLlgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1357 AAmdtetdL--LIQETIREAFAD-----CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1417
Cdd:COG0410 165 LG------LapLIVEEIFEIIRRlnregVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1192-1419 |
2.80e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.58 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYrENLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlRsKLTI 1271
Cdd:COG3840 2 LRLDDLTYRY-GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSG-TVRSN----LDPFNQYTEEQ---IWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARAL 1343
Cdd:COG3840 76 LFQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1344 LRHCKILILDEATAAMD----TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDS 1418
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEP 222
|
.
gi 16758936 1419 S 1419
Cdd:COG3840 223 P 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
566-780 |
4.05e-18 |
|
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: 85.73 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 566 QIHAGSMR----LQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYV 628
Cdd:cd03288 21 KIHDLCVRyennLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlrsrLSII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 629 AQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:cd03288 101 LQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 709 DDPLSALDAHVGNhIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELM-NLNGDYATI 780
Cdd:cd03288 181 DEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
577-765 |
7.08e-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: 83.84 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-----------TFAYVAQQ-AWILNATLRDNIL 644
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FG-------KEFDEERYNSVlnscclrpdlailpnSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:cd03301 95 FGlklrkvpKDEIDERVREV---------------AELLQIEHlldrKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 714 ALDAHVgnhifNSAIRKRLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERG 765
Cdd:cd03301 160 NLDAKL-----RVQMRAELKRlqqrlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
568-756 |
7.33e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.91 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 568 HAGSMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------FAYVAQQ----AWiL 635
Cdd:COG4525 13 YPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadRGVVFQKdallPW-L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 636 NAtlRDNILFGKefdeeRYNSVLNSCCLRPDLAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG4525 92 NV--LDNVAFGL-----RLRGVPKAERRARAEELLALVGLADFARRRiWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 715 LDAhvgnhifnsAIRKRLKS----------KTVLFVTHqlqylvDCDEVIFM 756
Cdd:COG4525 165 LDA---------LTREQMQEllldvwqrtgKGVFLITH------SVEEALFL 201
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
578-770 |
8.82e-18 |
|
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: 84.16 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------------FAYVAQQ-AWILNATLR 640
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGKEfdeeRYNSVLNSCCLRPD-------LAILPNSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:cd03256 97 ENVLSGRL----GRRSTWRSLFGLFPkeekqraLAALERVGLLDkAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 713 SALD---AHVGNHIFNSAIRKRlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:cd03256 173 ASLDpasSRQVMDLLKRINREE--GITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
571-771 |
1.07e-17 |
|
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: 86.32 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 571 SMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------------FAYVAQQAW 633
Cdd:TIGR02142 6 SKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 634 IL-NATLRDNILFGKEF--------DEERYNSVLNsccLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRS 704
Cdd:TIGR02142 86 LFpHLSVRGNLRYGMKRarpserriSFERVIELLG---IGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 705 IYILDDPLSALDAHVGNHIFnsAIRKRLKSKT---VLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEIL--PYLERLHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
578-772 |
1.55e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 84.23 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------------FAYVAQQ-AWILNATL 639
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrrkkISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNILFG-------KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 713 SALDahvgnhifnSAIRKRLKS----------KTVLFVTHqlqylvDCDEVI-------FMKEGCITERGTHEELMN 772
Cdd:cd03294 189 SALD---------PLIRREMQDellrlqaelqKTIVFITH------DLDEALrlgdriaIMKDGRLVQVGTPEEILT 250
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1187-1426 |
2.20e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.60 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1187 PQEGEITFENAEMRYRENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDI 1260
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1261 GladlrSKLTIIPQEPVLFs-gTVRSN---------LDPfnQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfS 1330
Cdd:COG1116 79 G-----PDRGVVFQEPALLpwlTVLDNvalglelrgVPK--AERRERARELLELVGLAGFEDAYPHQL-----------S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1331 VGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAH------RLhtvlgSDRIMVLAQ- 1401
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHdvdeavFL-----ADRVVVLSAr 215
|
250 260 270
....*....|....*....|....*....|.
gi 16758936 1402 -GQV-----VEFDTPSVLLSNDSSRFYAMCA 1426
Cdd:COG1116 216 pGRIveeidVDLPRPRDRELRTSPEFAALRA 246
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
578-754 |
2.96e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG--TFAYVAQQ---AWILNATLRDNI---LFGKEF 649
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 650 DEERYN----SVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 725
Cdd:NF040873 88 LWRRLTrddrAAVDDALERVGLADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....*....
gi 16758936 726 SAIRKRLKSKTVLFVTHQLQYLVDCDEVI 754
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
580-795 |
3.89e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.77 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFAYVAQ-------QAWIL--NATLRDNILFGK 647
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQrdicmvfQSYALfpHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 648 EF----DEERYNSVlnscclRPDLAILpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHvgnh 722
Cdd:PRK11432 104 KMlgvpKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDAN---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 723 ifnsaIRKRLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL---------MNLNGDyATIFN 782
Cdd:PRK11432 171 -----LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELyrqpasrfmASFMGD-ANIFP 244
|
250
....*....|...
gi 16758936 783 NLLLGETppVEIN 795
Cdd:PRK11432 245 ATLSGDY--VDIY 255
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
580-772 |
5.12e-17 |
|
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: 81.95 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------------FAYVAQQAwilnA-----T 638
Cdd:COG1127 23 GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelrrrIGMLFQGG----AlfdslT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFG-KEF----DEERYNSVLNScclrpdlailpnsdLTEIGERGAN------LSGGQRQRISLARALYSDRSIYI 707
Cdd:COG1127 99 VFENVAFPlREHtdlsEAEIRELVLEK--------------LELVGLPGAAdkmpseLSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 708 LDDPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1127 165 YDEPTAGLDPITSAVIDEliRELRDELGL-TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1192-1419 |
6.84e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIkPKEK-IGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLT 1270
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNI-PKGQwTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1271 IIPQEPV-LFSGT-----VRSNLDPFNQYTEEqiwdalerthMKECIAQLpLKlESEVMENGDN----FSVGERQLLCIA 1340
Cdd:PRK13648 87 IVFQNPDnQFVGSivkydVAFGLENHAVPYDE----------MHRRVSEA-LK-QVDMLERADYepnaLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1341 RALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 1418
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
.
gi 16758936 1419 S 1419
Cdd:PRK13648 235 E 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1209-1406 |
1.43e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLTIIPQEPVlfsgtvrS 1285
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 NLDPfNQYTEEQIWDALeRTH-----------MKECIAQLPLKLEsEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1354
Cdd:PRK10261 413 SLDP-RQTVGDSIMEPL-RVHgllpgkaaaarVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1355 ATAAMDTET-----DLL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:PRK10261 490 AVSALDVSIrgqiiNLLldLQRDFGIAY-----LFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
571-765 |
1.53e-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: 79.84 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 571 SMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFAYVAQQAwiLNATLRDNILFGK 647
Cdd:cd03298 7 RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRP--VSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 648 EFDEERYnsvlnscclrpDLAILPNSDLTEIgERGA-------------------NLSGGQRQRISLARALYSDRSIYIL 708
Cdd:cd03298 85 LTVEQNV-----------GLGLSPGLKLTAE-DRQAievalarvglaglekrlpgELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 709 DDPLSALDAHVGNHIFNSAIRKRLKSK-TVLFVTHQLQYLVDCDE-VIFMKEGCITERG 765
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
578-772 |
1.93e-16 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 81.44 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILgQMTLLEGSIAVSG-------------TFAYVAQQAWILNATLRDNI- 643
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 LFGKEFDEERYNsVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhI 723
Cdd:cd03289 99 PYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-----I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758936 724 FNSAIRKRLKSK----TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03289 173 TYQVIRKTLKQAfadcTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
554-743 |
2.09e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 554 DERPSPEEEEGKQIHAGSMRLQ----RTLY-NIDLEIEEGKLVGICGSVGSGKTSLISAILGqmtlL----EGSIAV--S 622
Cdd:COG4178 350 EAASRIETSEDGALALEDLTLRtpdgRPLLeDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 623 GTFAYVAQQAWILNATLRDNILF---GKEFDEERYNSVLNSCCLrPDLAilpnSDLTEIGERGANLSGGQRQRISLARAL 699
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHLA----ERLDEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16758936 700 YSDRSIYILDDPLSALDAHVGNHIFnSAIRKRLKSKTVLFVTHQ 743
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALY-QLLREELPGTTVISVGHR 543
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
575-772 |
2.13e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.97 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDN 642
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNyALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFG-------KEFDEERYNSVLnscclrpDLAilpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:cd03300 93 IAFGlrlkklpKAEIKERVAEAL-------DLV-----QLEGYANRKpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 715 LDAHVGNHIFN--SAIRKRLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03300 161 LDLKLRKDMQLelKRLQKELGI-TFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1208-1416 |
2.67e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.47 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRI--SDIGLADLRSKLTIIPQEPVLFS 1280
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1281 GTV---------------RSNLDpfnqyteEQIWDALERTHmkeciaqlplkLESEV----MENGDNFSVGERQLLCIAR 1341
Cdd:COG1117 106 KSIydnvayglrlhgiksKSELD-------EIVEESLRKAA-----------LWDEVkdrlKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1342 ALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGPTEQIFT 242
|
.
gi 16758936 1416 N 1416
Cdd:COG1117 243 N 243
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
578-761 |
3.10e-16 |
|
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: 79.11 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWilnATLRDNIlfGKEFdeERYN-- 655
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI---NELRQKV--GMVF--QQFNlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 656 ---SVLNSCCLRPDLAI-LPNSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03262 89 phlTVLENITLAPIKVKgMSKAEAEERALEllekvGladkadaypAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 718 HVGNHIFNsaIRKRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCI 761
Cdd:cd03262 169 ELVGEVLD--VMKDLAEEgmTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1208-1405 |
3.42e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLTI--IPQEPVLFSG-TVR 1284
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLD---PFNQYTEEQiwdalerthMKECIAQLPLKLESEVmeNGDNFSVGERQLLCIARALLRHCKILILDEATAAMD- 1360
Cdd:PRK15439 105 ENILfglPKRQASMQK---------MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 1361 TETDLLIQEtIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:PRK15439 174 AETERLFSR-IRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1192-1406 |
3.81e-16 |
|
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: 79.05 E-value: 3.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrSKL 1269
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFS-GTVRSN--LDPfnqytEEQIWDALE-RTHMKECIAQLPLKlesevmENGDNF----SVGERQLLCIAR 1341
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGL-----ELQGVPKAEaRERAEELLELVGLS------GFENAYphqlSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1342 ALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLH-TVLGSDRIMVLAQ--GQVVE 1406
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
563-762 |
4.03e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 78.45 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 563 EGKQIHAGSMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG----------TFAYVAQQA 632
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 633 wilnatlrDNILFGkefdeeryNSVLNSCCLRPDLA---------ILPNSDLTEIGERG-ANLSGGQRQRISLARALYSD 702
Cdd:cd03226 81 --------DYQLFT--------DSVREELLLGLKELdagneqaetVLKDLDLYALKERHpLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 703 RSIYILDDPLSALDAH----VGNHIfnsairKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT 762
Cdd:cd03226 145 KDLLIFDEPTSGLDYKnmerVGELI------RELAAqgKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1192-1424 |
4.66e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLRSKLT 1270
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1271 IIPQEP-VLFSG-TVRSNLdpfnQYTEEQIwdALERTHMKECI--AQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1346
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL----AFGPENL--CLPPIEIRKRVdrALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1347 CKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 1424
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1209-1405 |
6.17e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLgM-ALFRLVELSGGCIKIDG--VRISD--------IGLadlrskltiIPQEPV 1277
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSprdaialgIGM---------VHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1278 LFSG-TVRSNldpfnqyteeqIWDALERTH-----MKECIAQ---------LPLKLESEVmengDNFSVGERQLLCIARA 1342
Cdd:COG3845 91 LVPNlTVAEN-----------IVLGLEPTKggrldRKAARARirelserygLDVDPDAKV----EDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1343 LLRHCKILILDEATAAM-DTETDLLIqETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:COG3845 156 LYRGARILILDEPTAVLtPQEADELF-EILRR-LAAegKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
578-819 |
6.47e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------------FAYVAQQAWILNATLRD 641
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklvgIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGKEfdeerynsvlnSCCLRP-DLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK13644 98 DLAFGPE-----------NLCLPPiEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 715 LDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEelmnlngdyaTIFNNL---LLGETPP 791
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE----------NVLSDVslqTLGLTPP 236
|
250 260 270
....*....|....*....|....*....|
gi 16758936 792 --VEINSKKEASGSQKSQDKGPKPGSVKKE 819
Cdd:PRK13644 237 slIELAENLKMHGVVIPWENTSSPSSFAEE 266
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
564-770 |
7.13e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 80.51 E-value: 7.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 564 GKQIHAgsmrlqrtLYNIDLEIEEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAVSGT--------------- 624
Cdd:COG1135 15 GGPVTA--------LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGVdltalserelraarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 625 -----FayvaQQAWILNA-TLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSG 687
Cdd:COG1135 83 kigmiF----QHFNLLSSrTVAENVALpleiagvPKAEIRKRVAELL---------------ELVGLSDKAdaypSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 688 GQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKRLKsKTVLFVTHQLqylvD-----CDEVIFMKEGC 760
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDllKDINRELG-LTIVLITHEM----DvvrriCDRVAVLENGR 218
|
250
....*....|
gi 16758936 761 ITERGTHEEL 770
Cdd:COG1135 219 IVEQGPVLDV 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
575-790 |
8.84e-16 |
|
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: 79.08 E-value: 8.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG----------------TFAYVAQQA------ 632
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSpsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 633 -----WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:TIGR02769 104 rmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDA----------DKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 708 LDDPLSALDAHVGNHIFnsAIRKRLKSK---TVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMNLNGDYATIFN 782
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVIL--ELLRKLQQAfgtAYLFITHDLR-LVQsfCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQ 250
|
....*...
gi 16758936 783 NLLLGETP 790
Cdd:TIGR02769 251 SAVLPEHP 258
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1208-1405 |
8.98e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.21 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIglaDLRSKLTIIPQEPVLFSG-TVR 1284
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLdpfnQYTeeqiwdalerthmkeciAQLplklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1364
Cdd:cd03213 101 ETL----MFA-----------------AKL------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16758936 1365 LLIQETIRE-AFADCTMLTIAHRLHTVLGS--DRIMVLAQGQVV 1405
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
578-772 |
1.00e-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: 77.86 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVAQ-QAWILNATLRDN 642
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFG-----KEFDEERYNSVlnscclrpdLAILPNsdLTEI-GERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:cd03224 96 LLLGayarrRAKRKARLERV---------YELFPR--LKERrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 717 AHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03224 165 PKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
575-763 |
1.21e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.58 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG----------------TFAYVAQQA------ 632
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQMVFQDSisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 633 -----WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK10419 105 rktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL----------DKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 708 LDDPLSALDAHVGNHIFnsAIRKRLKSKT---VLFVTHQLQyLVD--CDEVIFMKEGCITE 763
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVI--RLLKKLQQQFgtaCLFITHDLR-LVErfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
910-1145 |
1.27e-15 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 78.97 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 910 LQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqA 989
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------N 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 990 EMFIQNVILVFFCVGMIAGVF----------PWFLVAVGPLLILFSVLH-IVSRVLIRELKRLdnitqspfLSHITS--- 1055
Cdd:cd18544 113 ELFTSGLVTLIGDLLLLIGILiamfllnwrlALISLLVLPLLLLATYLFrKKSRKAYREVREK--------LSRLNAflq 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1056 -SIQGLATIHAYNKRQEFLHRYQELlddNQApffLFTCAMRwlAVRLDLI---SIALITTTGLMIVLMHGqipsayAGLA 1131
Cdd:cd18544 185 eSISGMSVIQLFNREKREFEEFDEI---NQE---YRKANLK--SIKLFALfrpLVELLSSLALALVLWYG------GGQV 250
|
250
....*....|....
gi 16758936 1132 ISYAVQLTGLFQFT 1145
Cdd:cd18544 251 LSGAVTLGVLYAFI 264
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
575-771 |
1.62e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWI-LNATLR 640
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLsFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGKEFDEERYN-------SVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK09536 96 QVVEMGRTPHRSRFDtwtetdrAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 714 ALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
580-743 |
1.91e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFAYVAQQAWIL---NA-----TLRDNILFGKE 648
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiDDPDVAEACHYLghrNAmkpalTVAENLEFWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 649 FdeerynsvLNSCCLRPD--LAILPNSDLTEIgeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNS 726
Cdd:PRK13539 100 F--------LGGEELDIAaaLEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAE 168
|
170
....*....|....*...
gi 16758936 727 AIRKRLKSK-TVLFVTHQ 743
Cdd:PRK13539 169 LIRAHLAQGgIVIAATHI 186
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
578-759 |
1.92e-15 |
|
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: 75.16 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTfayvaqqawilnatlrdnilfgkefdEERYNSv 657
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 658 lnscclrPDLAIlpnsdlteigERGAN----LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLK 733
Cdd:cd03216 69 -------PRDAR----------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF--KVIRRLR 129
|
170 180
....*....|....*....|....*....
gi 16758936 734 S--KTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd03216 130 AqgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
582-765 |
2.67e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.44 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 582 DLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQAWIL-NATLRDNILFG--- 646
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 647 ----KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:TIGR01277 98 glklNAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 723 IFnsAIRKRL---KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
578-772 |
2.76e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.72 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKtSLISAIL-GQMTLLEGSIAVSG------TFAYVAQQAWI---------LNATLRD 641
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGK-STISKILtGLLKPQSGEIKIDGitiskeNLKEIRKKIGIifqnpdnqfIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIGERGA------NLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK13632 104 DIAFGLE----------NKKVPPKKMKDIIDDLAKKVGMEDYldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 716 DAHVGNHI--FNSAIRKRlKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13632 174 DPKGKREIkkIMVDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
905-1162 |
3.17e-15 |
|
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: 77.98 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 905 RDNPFLQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVR 984
Cdd:cd07346 33 GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 985 LPFQAEMFIQNVILVFFCVGMIAgVFPW--FLVAVGPLLILFSVLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLAT 1062
Cdd:cd07346 113 VSSGLLQLLSDVLTLIGALVILF-YLNWklTLVALLLLPLYVLILRYFRR-RIRKASREVRESLAELSAFLQESLSGIRV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1063 IHAYNKRQEFLHRYQELLDDNqapFFLFTCAMRWLAvrLDLISIALITTTGLMIVL-------MHGQIP----SAYagla 1131
Cdd:cd07346 191 VKAFAAEEREIERFREANRDL---RDANLRAARLSA--LFSPLIGLLTALGTALVLlyggylvLQGSLTigelVAF---- 261
|
250 260 270
....*....|....*....|....*....|.
gi 16758936 1132 ISYAVQLTGLFQFTVRLASETEARFTSVERI 1162
Cdd:cd07346 262 LAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
578-759 |
5.22e-15 |
|
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: 73.64 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--FAYVAQqawilnatlrdnilfgkefdeeryn 655
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 656 svlnscclrpdlailpnsdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDahvgnhIFN-SAIRKRLKS 734
Cdd:cd03221 71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD------LESiEALEEALKE 115
|
170 180
....*....|....*....|....*....
gi 16758936 735 --KTVLFVTHQlQYLVD--CDEVIFMKEG 759
Cdd:cd03221 116 ypGTVILVSHD-RYFLDqvATKIIELEDG 143
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
578-773 |
7.06e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFayvaqqAWIL--------NATLRDNILFG--- 646
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALLelgagfhpELTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 647 ----KEFDEERYNSVLnscclrpdlailpnsDLTEIGE------RgaNLSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 717 AHvgnhiFN----SAIRKRLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNL 773
Cdd:COG1134 179 AA-----FQkkclARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
580-770 |
7.60e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.80 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAVSGTfaYVAQQAWILNAtLRDNIlfGKEFdeERYN 655
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCI----NLLEepdsGTITVDGE--DLTDSKKDINK-LRRKV--GMVF--QQFN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 656 -----SVLNSCCLRPdlaI----LPNSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG1126 88 lfphlTVLENVTLAP---IkvkkMSKAEAEERAMEllervGladkadaypAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 713 SALD----AHVGNHIfnsairKRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:COG1126 165 SALDpelvGEVLDVM------RDLAKEgmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1208-1412 |
7.70e-15 |
|
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: 75.55 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKL--------TIIPQ-- 1274
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARHvgfvfqsfQLLPTlt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1275 --EPVLFSGTVRSNLDPFNQYTEEqiwdaLERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1352
Cdd:COG4181 107 alENVMLPLELAGRRDARARARAL-----LERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1353 DEATAAMDTET-----DLLIQETiREAFAdcTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1412
Cdd:COG4181 171 DEPTGNLDAATgeqiiDLLFELN-RERGT--TLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
576-761 |
9.99e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.00 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQM---TLLEGSIAVSGT----------FAYVAQQ-AWILNATLRD 641
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQprkpdqfqkcVAYVRQDdILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILF------GKEFDEERYNSVLNSCCLRpDLAIlpnsdlTEIG-ERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:cd03234 101 TLTYtailrlPRKSSDAIRKKRVEDVLLR-DLAL------TRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 715 LDAHVGNHIFNSAIRKRLKSKTVLFVTHQ-----LQYLvdcDEVIFMKEGCI 761
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1195-1415 |
1.13e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1195 ENAEMRY-RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIP 1273
Cdd:PRK13642 8 ENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1274 QEP-VLFSGTVRSNLDPFNQYTE--------EQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1344
Cdd:PRK13642 88 QNPdNQFVGATVEDDVAFGMENQgipreemiKRVDEALLAVNMLDFKTREPARL-----------SGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1345 RHCKILILDEATAAMD----TETDLLIQEtIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHE-IKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1192-1416 |
1.52e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLV---ELSGGCIKIDGVRISDIGLADLRSK 1268
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1269 LTIIPQepvlfsgtvrsnlDPFNQYTEEQIWD---------ALERTHMKECIAQLplkLESEVMEN-----GDNFSVGER 1334
Cdd:PRK13640 86 VGIVFQ-------------NPDNQFVGATVGDdvafglenrAVPRPEMIKIVRDV---LADVGMLDyidsePANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1335 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1412
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
....
gi 16758936 1413 LLSN 1416
Cdd:PRK13640 230 IFSK 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
578-773 |
1.62e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.91 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-TFAYVAQQAWILNA-----------TLRDNILF 645
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 GkefdeerynsvlnsccLRpdLAILPNSD-------------LTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:PRK09452 110 G----------------LR--MQKTPAAEitprvmealrmvqLEEFAQRKpHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 712 LSALDAHVGNHIFNSAirKRLKSK---TVLFVTH-QLQYLVDCDEVIFMKEGCITERGT----HEELMNL 773
Cdd:PRK09452 172 LSALDYKLRKQMQNEL--KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTpreiYEEPKNL 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1192-1416 |
1.73e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYREN----LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLR 1266
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1267 SKLTIIPQEP------------VLFSgtvRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGER 1334
Cdd:PRK13633 85 NKAGMVFQNPdnqivativeedVAFG---PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1335 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1412
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
....
gi 16758936 1413 LLSN 1416
Cdd:PRK13633 231 IFKE 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1208-1417 |
1.77e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.19 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVL-FSGTV--- 1283
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVeev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 ----RSNLDPFNQYTEEQIWDALERThmkECIA-------QLplklesevmengdnfSVGERQLLCIARAL--LRHC--- 1347
Cdd:PRK13548 97 vamgRAPHGLSRAEDDALVAAALAQV---DLAHlagrdypQL---------------SGGEQQRVQLARVLaqLWEPdgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1348 -KILILDEATAAMdtetDLLIQETIreafadctmLTIAHR------------LH----TVLGSDRIMVLAQGQVVEFDTP 1410
Cdd:PRK13548 159 pRWLLLDEPTSAL----DLAHQHHV---------LRLARQlaherglavivvLHdlnlAARYADRIVLLHQGRLVADGTP 225
|
....*..
gi 16758936 1411 SVLLSND 1417
Cdd:PRK13548 226 AEVLTPE 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1208-1406 |
1.81e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.95 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRISDIGLADLRSKLTIIPQEP------ 1276
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1277 VLFS----GTVRSNLDPFNQYTEEQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILIL 1352
Cdd:PRK14247 98 SIFEnvalGLKLNRLVKSKKELQERVRWALEK-------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1353 DEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVE 1406
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1208-1406 |
2.02e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 75.23 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKLTIIPQE-PVLFSG-- 1281
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 TVRSNL-DPFNQYTEeqiwdaLERTHMKECIAQL--PLKLESEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEATA 1357
Cdd:TIGR02769 106 TVRQIIgEPLRHLTS------LDESEQKARIAELldMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1358 AMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:TIGR02769 180 NLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
575-756 |
2.02e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-----AVSGTFA---YVAQQAWILN-ATLRDNILF 645
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkPVEGPGAergVVFQNEGLLPwRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 GKEF----DEERYNSVLnscclrpdlAILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 720
Cdd:PRK11248 94 GLQLagveKMQRLEIAH---------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 16758936 721 NHIFNSAIRK-RLKSKTVLFVTHqlqylvDCDEVIFM 756
Cdd:PRK11248 165 EQMQTLLLKLwQETGKQVLLITH------DIEEAVFM 195
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
581-759 |
2.36e-14 |
|
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: 73.47 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 581 IDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---------TFAYVAQQAWI-LNATLRDNILF----- 645
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVYlaqlk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 --GKEFDEERYNSVLNscclRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHI 723
Cdd:cd03269 99 glKKEEARRRIDEWLE----RLELSEYANKRVEE-------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVEL 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 16758936 724 FNSAIRK-RLKSKTVLFVTHQLQyLVD--CDEVIFMKEG 759
Cdd:cd03269 167 LKDVIRElARAGKTVILSTHQME-LVEelCDRVLLLNKG 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
575-765 |
2.84e-14 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 73.41 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTF------------AYVAQQAWILNATLRDN 642
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrrigALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILF---GKEFDEERYNSVLNSCCLRpdlailpnsdlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 719
Cdd:cd03268 93 LRLlarLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 720 GNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1208-1403 |
3.12e-14 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 73.62 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI-------KIDGVRISDIGLADLRSK--------LTII 1272
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1273 PQ--------EPVLFSGTVRsnldpfnQYTEEQIWDALERTHMKECIAQLPLKlesevmengdNFSVGERQLLCIARALL 1344
Cdd:COG4778 106 PRvsaldvvaEPLLERGVDR-------EEARARARELLARLNLPERLWDLPPA----------TFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1345 RHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQ 1403
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
625-772 |
3.40e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 625 FAYVAQQAWILNATLRDNILFGKE-FDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDR 703
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 704 SIYILDDPLSALDAHVGNHIFNSAIRKRLKS-KTVLFVTHQLQYLVDCDEVIFM----KEGCITE-RGTHEELMN 772
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLS 1452
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
580-759 |
4.35e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 72.08 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVA----QQAWILNATLRD 641
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVLDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILfgkefdeerynsvlnscclrpdLAILpnsdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDahVG- 720
Cdd:cd03215 98 NIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VGa 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16758936 721 -NHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:cd03215 140 kAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1202-1421 |
4.41e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1202 RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS----KLTIIPQEPV 1277
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1278 LFSG-TVRSNldpfNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1356
Cdd:PRK10070 117 LMPHmTVLDN----TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1357 AAMDTETDLLIQETI--REAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRF 1421
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
593-770 |
4.47e-14 |
|
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: 75.22 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 593 ICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-FAYVAQ---------QAWIL--NATLRDNILFG----KEFDEERYNS 656
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdVTNVPPhlrhinmvfQSYALfpHMTVEENVAFGlkmrKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 657 VLnscclrpdlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNS--AIRKRLk 733
Cdd:TIGR01187 81 VL---------EALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLElkTIQEQL- 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 16758936 734 SKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:TIGR01187 151 GITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
580-772 |
5.29e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.72 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT------FAYVAQQ------------------AWIL 635
Cdd:COG4167 31 PVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdYKYRCKHirmifqdpntslnprlniGQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 636 NATLRDNILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG4167 111 EEPLRLNTDLTAEEREERIFATLRLVGLLPEHAnFYPHM-----------LSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 715 LDAHVGNHIFN--SAIRKRLKSKTVlFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG4167 180 LDMSVRSQIINlmLELQEKLGISYI-YVSQHLG-IVKhiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1192-1406 |
7.00e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.73 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLVEL----SGGCIKIDGVRISDI---GL 1262
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINLlerpTSGSVLVDGVDLTALserEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1263 ADLRSKLTIIPQEPVLFSG-TVRSNldpfnqyteeqiwdalerthmkecIAqLPLKL--------ESEVME--------- 1324
Cdd:COG1135 78 RAARRKIGMIFQHFNLLSSrTVAEN------------------------VA-LPLEIagvpkaeiRKRVAEllelvglsd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1325 NGDNF----SVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SD 1394
Cdd:COG1135 133 KADAYpsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsilDLL--KDINREL-GLTIVLITHEMDVVRRiCD 209
|
250
....*....|..
gi 16758936 1395 RIMVLAQGQVVE 1406
Cdd:COG1135 210 RVAVLENGRIVE 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
573-743 |
8.01e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT------------FAYVAQQAWILNA-T 638
Cdd:TIGR01189 10 RGERMLFeGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFGKEFDEERYNSVLNScclrpdlailpnsdLTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTIEDA--------------LAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 16758936 713 SALDAHvGNHIFNSAIRKRL-KSKTVLFVTHQ 743
Cdd:TIGR01189 156 TALDKA-GVALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
575-776 |
1.16e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.13 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGtFAYVAQQAW----------------ILNAT 638
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvfqnpdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:PRK13635 99 VQDDVAFGLE----------NIGVPREEMVERVDQALRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 713 SALDAhVGNHIFNSAIRkRLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGD 776
Cdd:PRK13635 169 SMLDP-RGRREVLETVR-QLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1211-1405 |
1.44e-13 |
|
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: 71.17 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1211 KVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLTIIPQEPVLFSG-TVRS 1285
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 NL--------DPFNQYTEEQIWDALERTHMKEciaQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 1357
Cdd:cd03297 95 NLafglkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1358 AMDTETDLLIQETIREAFAD--CTMLTIAHRLHTV-LGSDRIMVLAQGQVV 1405
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
580-770 |
1.46e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.91 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDNILFG- 646
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergVGMVFQSyALYPHLSVAENMSFGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 647 ------KEFDEERYNSVLnscclrpdlAILPNSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA--H 718
Cdd:PRK11000 101 klagakKEEINQRVNQVA---------EVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758936 719 VGNHIFNSAIRKRLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK11000 170 VQMRIEISRLHKRLGR-TMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1204-1415 |
1.82e-13 |
|
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: 72.58 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1204 NLPL----VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRISdigladlrskltIIPQEPVLF 1279
Cdd:cd03291 44 NLCLvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RIS------------FSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 SGTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1359
Cdd:cd03291 111 PGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1360 DTETDLLIQET-IREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:cd03291 191 DVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1209-1408 |
1.94e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRI--SDIGLADLRSKLTIIPQEPVLFSG 1281
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 TVRSNLD---PFNQYTEEQIWDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 1358
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1359 MDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1408
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1212-1416 |
2.43e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.82 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLTIIPQEPvLFSGTVRSNL- 1287
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1288 ----DPFNQYTEEqiwdaLERTHMKECIAQLPLK---LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1360
Cdd:PRK15079 119 eiiaEPLRTYHPK-----LSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1361 TETDL----LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:PRK15079 194 VSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1192-1423 |
2.92e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 70.73 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrsklti 1271
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVlfsGTVRSNLDPFNQYT-EEQIWDALERTHMKECI------AQLPL-KLESEVMENGDNFSVGERQLLCIARAL 1343
Cdd:cd03300 69 PHKRPV---NTVFQNYALFPHLTvFENIAFGLRLKKLPKAEikervaEALDLvQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1344 LRHCKILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEF 1407
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELK-------------RLQKELGitfvfvthdqeealtmSDRIAVMNKGKIQQI 212
|
250
....*....|....*.
gi 16758936 1408 DTPSVLLSNDSSRFYA 1423
Cdd:cd03300 213 GTPEEIYEEPANRFVA 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1192-1404 |
2.99e-13 |
|
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: 70.51 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 1268
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1269 LTIIPQEPVLFSG-TVRSNLDPFNQYTEEQIWDALERthMKECIAQLPLKLESEVMENGdnFSVGERQLLCIARALLRHC 1347
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKR--VPAALELVGLSHKHRALPAE--LSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1348 KILILDEATAAMDTET-----DLLiqETIREAFADCTMLTIAHRLHTVLgSDRIMVLAQGQV 1404
Cdd:cd03292 156 TILIADEPTGNLDPDTtweimNLL--KKINKAGTTVVVATHAKELVDTT-RHRVIALERGKL 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1192-1407 |
3.09e-13 |
|
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: 70.30 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLTI 1271
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSG-TVRSNLDPF-------NQYTEEQIWDALERTHM----KECIAQLplklesevmengdnfSVGERQLLCI 1339
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDYIawlkgipSKEVKARVDEVLELVNLgdraKKKIGSL---------------SGGMRRRVGI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1340 ARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF 1407
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1195-1430 |
3.11e-13 |
|
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: 70.83 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1195 ENAEMRYREnlpLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGVRIS----DI-GLADLRSKL 1269
Cdd:cd03299 4 ENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVL-------LETIAGFIKPDSGKILlngkDItNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSG-TVRSNLdpfnQY-----------TEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLL 1337
Cdd:cd03299 74 SYVPQNYALFPHmTVYKNI----AYglkkrkvdkkeIERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1338 CIARALLRHCKILILDEATAAMDTET-DLLIQE--TIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVL 1413
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTkEKLREElkKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEV 217
|
250
....*....|....*..
gi 16758936 1414 LSNDSSRFYAMCAAAEN 1430
Cdd:cd03299 218 FKKPKNEFVAEFLGFNN 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1192-1406 |
3.29e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.53 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGVRI---SDIGL 1262
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLlerpTSGRVLVDGQDLtalSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1263 ADLRSKLTIIPQEPVLFSG-TVRSNldpfnqyteeqiwdalerthmkecIAqLPLKL--------ESEVMENGD------ 1327
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSSrTVFDN------------------------VA-LPLELagtpkaeiKARVTELLElvglsd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1328 -------NFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIreafaDCTMLTIAHRLHTVLG- 1392
Cdd:PRK11153 133 kadrypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRi 207
|
250
....*....|....
gi 16758936 1393 SDRIMVLAQGQVVE 1406
Cdd:PRK11153 208 CDRVAVIDAGRLVE 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
578-765 |
5.36e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.87 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGtfayvaQQAWIL--------NATLRDNILFG--- 646
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLglgggfnpELTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 647 ----KEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 718
Cdd:cd03220 112 lglsRKEIDEKIDEII---------------EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758936 719 vgnhiF----NSAIRKRLK-SKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:cd03220 177 -----FqekcQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
578-761 |
5.81e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISaILGQMtllegSIAVSGTFAYVAQQAWILN----ATLRDNiLFGKEFdeER 653
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL-----DKPTSGTYRVAGQDVATLDadalAQLRRE-HFGFIF--QR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 654 YNsvlnsccLRPDLAILPNSDLTEI----------------------GER----GANLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK10535 95 YH-------LLSHLTAAQNVEVPAVyaglerkqrllraqellqrlglEDRveyqPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 708 LDDPLSALDAHVGNHIFnsAIRKRLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 761
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
576-777 |
6.53e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMT----------LLEGSIAVSGTFA-----------YVAQQAWI 634
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLArdirksrantgYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 635 LNA-TLRDNILFGKEFDEERYNSvlnscCLR---PDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRS 704
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRT-----CFSwftREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 705 IYILDDPLSALDAHVGnHIFNSAIR--KRLKSKTVLFVTHQLQY-LVDCDEVIFMKEGCITERGTHEELMNLNGDY 777
Cdd:PRK09984 173 VILADEPIASLDPESA-RIVMDTLRdiNQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFDH 247
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
578-772 |
7.19e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.74 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAI--LGQMT---LLEGSIAVSGTFA----------YVAQQAWIL-NATLRD 641
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdLIVDGLKVNDPKVderlirqeagMVFQQFYLFpHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFG--------KEFDEERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK09493 97 NVMFGplrvrgasKEEAEKQARELLAKVGLAERAHHYP-----------SELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 714 ALDAHVGNHIFNsaIRKRLKSK--TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 772
Cdd:PRK09493 166 ALDPELRHEVLK--VMQDLAEEgmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
578-770 |
7.68e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILG-QMTLLE--GSIAVSGT----------FAYVAQQAWILNA-TLRDNI 643
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKgsGSVLLNGMpidakemraiSAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 LFGKEF--------DE--ERYNSVLNscclrpDLAILPNSDlTEIGERGA--NLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:TIGR00955 121 MFQAHLrmprrvtkKEkrERVDEVLQ------ALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 712 LSALDAHVGNHIFnsAIRKRL--KSKTVLFVTHQLQYLVDC--DEVIFMKEGCITERGTHEEL 770
Cdd:TIGR00955 194 TSGLDSFMAYSVV--QVLKGLaqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1195-1420 |
7.85e-13 |
|
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: 69.49 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1195 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLaDLRSKLTII-- 1272
Cdd:cd03218 4 ENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1273 PQEPVLFSG-TVRSNLDPFNQYTEEQIWDALERThmKECIAQLplKLESEVMENGDNFSVGERQLLCIARALLRHCKILI 1351
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLSKKEREEKL--EELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1352 LDEATAAMDTETDLLIQETIREaFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1420
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKI-LKDRGIgvLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
578-772 |
1.02e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.00 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAY----------VAQQAWILNATLRDNILFgK 647
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 648 EFDEERYNSVLNSCCLRPDLAI-LPNSDLTE----------IGERG-----ANLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVLgLSKQEAREravkylakvgIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 712 LSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 772
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
580-772 |
1.25e-12 |
|
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: 69.34 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEG-SIAVSGT-------------FAYV--AQQAWIL-NATLRDN 642
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkrIGLVspALQLRFPrDETVLDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 IL---FG-----KEFDEERYNSVLNScclrpdLAILpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:COG1119 101 VLsgfFDsiglyREPTDEQRERAREL------LELL---GLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 714 ALDAHvGNHIFNSAIRK--RLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 772
Cdd:COG1119 172 GLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1192-1416 |
1.25e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI----SDIGLAD 1264
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1265 LRSKLTIIPQ--EPVLFSGTVRSNLD--PFN-----QYTEEQIWDALERTHMKE-CIAQLPLKLesevmengdnfSVGER 1334
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKNfgfseDEAKEKALKWLKKVGLSEdLISKSPFEL-----------SGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1335 QLLCIARALLRHCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1408
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHA 227
|
....*...
gi 16758936 1409 TPSVLLSN 1416
Cdd:PRK13641 228 SPKEIFSD 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1208-1406 |
1.42e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS----GGCIKIDGVRISDIGLADLR----SKLTIIPQEPVlf 1279
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 sgtvrSNLDPF----NQYTE--------------EQIWDALERTHMKE---CIAQLPLKLesevmengdnfSVGERQLLC 1338
Cdd:COG4172 103 -----TSLNPLhtigKQIAEvlrlhrglsgaaarARALELLERVGIPDperRLDAYPHQL-----------SGGQRQRVM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1339 IARALLRHCKILILDEATAAMDTET-----DLL--IQETIREAfadctMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVqaqilDLLkdLQRELGMA-----LLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
685-772 |
1.50e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKRLKSK---TVLFVTHQLQ---YLvdCDEVIFMKE 758
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAvvrAL--AHRVMVMKD 501
|
90
....*....|....
gi 16758936 759 GCITERGTHEELMN 772
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
581-765 |
1.55e-12 |
|
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: 68.55 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 581 IDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAY-----VAQQAWILNA--------TLRDNILF-- 645
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkepaeARRRLGFVSDstglydrlTARENLEYfa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 ------GKEFdEERYNSVlnscclrpdlailpnSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:cd03266 104 glyglkGDEL-TARLEEL---------------ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 716 DAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1209-1416 |
1.58e-12 |
|
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: 69.59 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL----RSKLTIIPQEPVLFSG-TV 1283
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 RSNLdPF--------NQYTEEQIWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:cd03294 120 LENV-AFglevqgvpRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1356 TAAMDTetdlLIQETIREAFADC------TMLTIAHRLHTV--LGsDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:cd03294 188 FSALDP----LIRREMQDELLRLqaelqkTIVFITHDLDEAlrLG-DRIAIMKDGRLVQVGTPEEILTN 251
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1192-1419 |
1.87e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.58 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRskltI 1271
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDER----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEpvlfSGTVRSNLDPFNQYTeeqiwdALE---------RTHMKECIAQLPLKLESEV--MENGDNF----SVGERQL 1336
Cdd:PRK09493 75 IRQE----AGMVFQQFYLFPHLT------ALEnvmfgplrvRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1337 LCIARALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRL---HTVlGSdRIMVLAQGQVVEFDT 1409
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKvmQDLAEegMTMVIVTHEIgfaEKV-AS-RLIFIDKGRIAEDGD 219
|
250
....*....|
gi 16758936 1410 PSVLLSNDSS 1419
Cdd:PRK09493 220 PQVLIKNPPS 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1203-1404 |
1.92e-12 |
|
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: 67.07 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1203 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLTIIPQEP-- 1276
Cdd:cd03215 8 RGLsvKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDA-IRAGIAYVPEDRkr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1277 --VLFSGTVRSNLdpfnqyteeqiwdalerthmkeCIAQLplklesevmengdnFSVGERQLLCIARALLRHCKILILDE 1354
Cdd:cd03215 87 egLVLDLSVAENI----------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1355 ATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQV 1404
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
576-772 |
1.96e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.69 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------------TFAYVAQQawILN 636
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkkvglVFQYPEYQ--LFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 637 ATLRDNILFGK----EFDEERYNSVLNSCclrpDLAILPNSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:PRK13637 99 ETIEKDIAFGPinlgLSEEEIENRVKRAM----NIVGLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 713 SALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13637 173 AGLDPKGRDEILNkiKELHKEYNM-TIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
578-754 |
1.97e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNATLRDNIL 644
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 F-----GKEFDEERynsvlnsccLRPDLAI--LPNSDLTEigeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:PRK10247 103 FpwqirNQQPDPAI---------FLDDLERfaLPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 16758936 718 HvGNHIFNSAIRKRLKSK--TVLFVTHQLQYLVDCDEVI 754
Cdd:PRK10247 171 S-NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
573-743 |
2.20e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSgtfayVAQQAWILNATLRDNILFGKEFDE 651
Cdd:COG2401 40 VVERYVLrDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 652 ERYnsVLNSCCLrpdlailpnSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAI 728
Cdd:COG2401 115 AVE--LLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLA 183
|
170
....*....|....*
gi 16758936 729 RKRlkSKTVLFVTHQ 743
Cdd:COG2401 184 RRA--GITLVVATHH 196
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
580-743 |
2.27e-12 |
|
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: 66.41 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI---AVSGTFaYVAQQAWILNATLRDNIlfgkefdeeryns 656
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmpEGEDLL-FLPQRPYLPLGTLREQL------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 657 vlnscclrpdlaILPNSDlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKRLksKT 736
Cdd:cd03223 85 ------------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY-QLLKELG--IT 140
|
....*..
gi 16758936 737 VLFVTHQ 743
Cdd:cd03223 141 VISVGHR 147
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
578-772 |
2.37e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.06 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTS---LISAILGQMTLLEGSIAVSGTfAYVAQQAW----------------ILNAT 638
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGI-TLTAKTVWdirekvgivfqnpdnqFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:PRK13640 102 VGDDVAFGLE----------NRAVPRPEMIKIVRDVLADVGmldyidSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 713 SALDAHVGNHIFnSAIRKRLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13640 172 SMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
580-770 |
2.56e-12 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 67.92 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG----TFAYVAQQA-----------WILnaTLRDNIL 644
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQSlgycpqfdalfDEL--TVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 F-----GKEFDEERYNSvlnscclrpdLAILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 718
Cdd:cd03263 98 FyarlkGLPKSEIKEEV----------ELLLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 719 VGNHIFNsAIRKRLKSKTVLFVTHQLQ---YLvdCDEVIFMKEG---CIterGTHEEL 770
Cdd:cd03263 168 SRRAIWD-LILEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGklrCI---GSPQEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1192-1405 |
2.78e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYrENLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLG--MALFRLVElsGGCIKIDGVRISDIGLAdlRSKL 1269
Cdd:PRK10771 2 LKLTDITWLY-HHLPM---RFDLTVERGERVAILGPSGAGKSTLLnlIAGFLTPA--SGSLTLNGQDHTTTPPS--RRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1270 TIIPQEPVLFSG-TVRSN----LDP---FNQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIAR 1341
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1342 ALLRHCKILILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
580-772 |
3.31e-12 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 67.85 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG------------------TFayvaQQAWIL-NATLR 640
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrTF----QIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGKEFDEERYNSVLNSCCLRPDL-----AILpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 712 LSALD----AHVGNHIfnSAIRKRlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03219 171 AAGLNpeetEELAELI--RELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1208-1414 |
3.34e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLAdlRSKLTIIPQEPVL-FSGTVRS 1285
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 NLDPFNQYTeeqiwdaleRTHMKECIAQLPLKLESEVMENGDNFSV-----GERQLLCIARALLRHCKILILDEATAAMD 1360
Cdd:PRK13536 134 NLLVFGRYF---------GMSTREIEAVIPSLLEFARLESKADARVsdlsgGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1361 TETDLLIQETIREAFA--DCTMLTI-----AHRLhtvlgSDRIMVLAQGQVVEFDTPSVLL 1414
Cdd:PRK13536 205 PHARHLIWERLRSLLArgKTILLTThfmeeAERL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1208-1416 |
3.44e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID------GVRISDIGLADLRSKLTIIPQEPVLFSG 1281
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 -TVRSNLD-PFNQYTeeqIWDALE-RTHMKECIAQLPL--KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1356
Cdd:PRK14246 105 lSIYDNIAyPLKSHG---IKEKREiKKIVEECLRKVGLwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1357 AAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1203-1408 |
3.49e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1203 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDI------GLA----DlRSK 1268
Cdd:COG1129 260 EGLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPrdairaGIAyvpeD-RKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1269 LTIIPQEPVLFSGTVrSNLDPFNQYTeeQIWDALERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLR 1345
Cdd:COG1129 339 EGLVLDLSIRENITL-ASLDRLSRGG--LLDRRRERALAEEYIKRLRIKtpsPEQPVG----NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1346 HCKILILDEATAAMD----TEtdllIQETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 1408
Cdd:COG1129 412 DPKVLILDEPTRGIDvgakAE----IYRLIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIVgELD 477
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1183-1408 |
3.51e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 67.56 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1183 PHDWPQEGEITFENAEMRYREnlplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS---D 1259
Cdd:cd03220 16 GSSSLKKLGILGRKGEVGEFW----ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSsllG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1260 IGLAdLRSKLTIIpqEPVLFSGTVRSNLDPFNQYTEEQIWDALErthMKECIaQLPLKlesevmengdNFSVGERQLLCI 1339
Cdd:cd03220 91 LGGG-FNPELTGR--ENIYLNGRLLGLSRKEIDEKIDEIIEFSE---LGDFI-DLPVK----------TYSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1340 ARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIA-HRLHTVLG-SDRIMVLAQGQVVEFD 1408
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1208-1420 |
3.68e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLTIIPQEPVLFSG-TVRS 1285
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 NLDPFNQYTEEQIWdaleRTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDL 1365
Cdd:PRK11614 100 NLAMGGFFAERDQF----QERIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1366 LIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1420
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
575-772 |
3.85e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 68.22 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRT-LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG------------------------TFAYVA 629
Cdd:COG4559 13 GRTlLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarrravlpqhsslAFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 630 QQ-------AWILNATLRDNILfgkefdEErynsvlnscCL-RPDLAILPNSDLTEigerganLSGGQRQRISLARAL-- 699
Cdd:COG4559 93 EEvvalgraPHGSSAAQDRQIV------RE---------ALaLVGLAHLAGRSYQT-------LSGGEQQRVQLARVLaq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 700 -----YSDRSIYILDDPLSALD-AHVgNHIFNSAirKRLKSK--TVLFVTHQL----QYlvdCDEVIFMKEGCITERGTH 767
Cdd:COG4559 151 lwepvDGGPRWLFLDEPTSALDlAHQ-HAVLRLA--RQLARRggGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTP 224
|
....*
gi 16758936 768 EELMN 772
Cdd:COG4559 225 EEVLT 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1208-1415 |
4.20e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL-----VELSGGCIKIDGVRISDIGLADLR----SKLTIIPQEPVL 1278
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1279 fsgtvrsNLDPFNQyTEEQIWDALE----------RTHMKEC-----IAQLPLKLEsevmENGDNFSVGERQLLCIARAL 1343
Cdd:PRK15134 104 -------SLNPLHT-LEKQLYEVLSlhrgmrreaaRGEILNCldrvgIRQAAKRLT----DYPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1344 LRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1207-1392 |
4.30e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1207 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvriSDIGLADLRSKLTII----PQEPVLfsgT 1282
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLghrnAMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1283 VRSNLD---PFNQYTEEQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAM 1359
Cdd:PRK13539 90 VAENLEfwaAFLGGEELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|...
gi 16758936 1360 DTETDLLIQETIREAFADCTMLTIAhrLHTVLG 1392
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAA--THIPLG 189
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1184-1406 |
4.40e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1184 HDWPQEGEITFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG------- 1254
Cdd:PRK10261 5 DELDARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1255 ---VRISDIGLADLR----SKLTIIPQEPVlfsgtvrSNLDPFNQyTEEQIWDALeRTHM----KECIAQLPLKL----- 1318
Cdd:PRK10261 85 rqvIELSEQSAAQMRhvrgADMAMIFQEPM-------TSLNPVFT-VGEQIAESI-RLHQgasrEEAMVEAKRMLdqvri 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1319 -ESEVM--ENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG- 1392
Cdd:PRK10261 156 pEAQTIlsRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEi 235
|
250
....*....|....
gi 16758936 1393 SDRIMVLAQGQVVE 1406
Cdd:PRK10261 236 ADRVLVMYQGEAVE 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1208-1420 |
4.67e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVL-FSGTVR-- 1284
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 ---------SNLDPFNQYTEEQIWDALERTHMKECIAQlPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:PRK09536 98 vemgrtphrSRFDTWTETDRAAVERAMERTGVAQFADR-PV----------TSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1356 TAAMDTETDLLIQETIRE-------AFADCTMLTIAHRLhtvlgSDRIMVLAQGQVVEFDTPSVLLSNDSSR 1420
Cdd:PRK09536 167 TASLDINHQVRTLELVRRlvddgktAVAAIHDLDLAARY-----CDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
585-768 |
5.19e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 585 IEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGtfAYVAQQAWILNA---------------TLRDNIL-FGKE 648
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARArigvvpqfdnldlefTVRENLLvFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 649 FdeeRYNSvlnscclRPDLAILPNsdLTEIGE-------RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGN 721
Cdd:PRK13536 142 F---GMST-------REIEAVIPS--LLEFARleskadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-AR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758936 722 HIFNSAIRKRL-KSKTVLFVTHQLQYLVD-CDEVIFMKEGC-ITERGTHE 768
Cdd:PRK13536 209 HLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRkIAEGRPHA 258
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
575-770 |
5.35e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.12 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLI---SAIL----GQMTLLEGSIA--------------VSGTFAYVAQQaw 633
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLqhlNGLLqptsGTVTIGERVITagkknkklkplrkkVGIVFQFPEHQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 634 ILNATLRDNILFG-------KEFDEERYNSVLNSCCLRPDLaiLPNSDLteigergaNLSGGQRQRISLARALYSDRSIY 706
Cdd:PRK13634 98 LFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEEL--LARSPF--------ELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 707 ILDDPLSALDAHVGNHIFN--SAIRKRlKSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEmfYKLHKE-KGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREI 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
578-772 |
6.32e-12 |
|
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: 66.93 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVAQQAWIL-NATLRDN 642
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFpSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFG------KEFDEERYNSVLNsccLRPDLAilpnsdlteigER----GANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:COG0410 99 LLLGayarrdRAEVRADLERVYE---LFPRLK-----------ERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 713 SALDAHVGNHIFNsAIRkRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG0410 165 LGLAPLIVEEIFE-IIR-RLNREgvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
564-766 |
6.49e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.67 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 564 GKQIHAgsmrlqrtLYNIDLEIEEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAVSGT--------------- 624
Cdd:PRK11153 15 GRTIHA--------LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGQdltalsekelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 625 -FAYVAQQAWILNA-TLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQ 691
Cdd:PRK11153 83 qIGMIFQHFNLLSSrTVFDNVALplelagtPKAEIKARVTELL---------------ELVGLSDKAdrypAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 692 RISLARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGT 766
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILEllKDINRELGL-TIVLITHEMD-VVKriCDRVAVIDAGRLVEQGT 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1208-1416 |
6.79e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.37 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGVRISD--IGLADLRSKLTIIPQEPVLFS 1280
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1281 GTVRSNLdpfnQYTEEQI-W------DALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILD 1353
Cdd:PRK14258 102 MSVYDNV----AYGVKIVgWrpkleiDDIVESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1354 EATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVL-----------GSDRImvlaqGQVVEFDTPSVLLSN 1416
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrlsdftaffkgNENRI-----GQLVEFGLTKKIFNS 246
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1209-1411 |
8.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.57 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLADLRSKLTIIPQEP--VLFSGTVR 1284
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLD--PFN-QYTEEQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEATAAMD- 1360
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1361 ---TETDLLIQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVEFDTPS 1411
Cdd:PRK13636 175 mgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPK 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
573-765 |
8.65e-12 |
|
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: 66.59 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG----------------TFAYVAQQAWILN 636
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrkkflrrigvVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 637 AtlRDNILFGKE---FDEERYNSVLNSCClrpdlailpnsDLTEIGE------RgaNLSGGQRQRISLARALYSDRSIYI 707
Cdd:cd03267 112 V--IDSFYLLAAiydLPPARFKKRLDELS-----------ELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 708 LDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHqlqYLVD----CDEVIFMKEGCITERG 765
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEyNRERGTTVLLTSH---YMKDiealARRVLVIDKGRLLYDG 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
575-772 |
9.39e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.65 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT------FAYVAQQAWIL---NA-----TLR 640
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAKRLAILrqeNHinsrlTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGkefdeeRYnsvlnscclrP---------DLAILPNS----DLTEIGERGAN-LSGGQRQRISLARALYSDRSIY 706
Cdd:COG4604 94 ELVAFG------RF----------PyskgrltaeDREIIDEAiaylDLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 707 ILDDPLSALDahvgnhIFNS-AIRKRLKS------KTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:COG4604 158 LLDEPLNNLD------MKHSvQMMKLLRRladelgKTVVIVLHDInfasCY---ADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
580-770 |
9.51e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.44 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFayvaqqawiLNATLRDNI--LfgkefDEERynsv 657
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---------LDPEDRRRIgyL-----PEER---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 658 lnscCLRPDLAI------------LPNSDLT----------EIGERGA----NLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:COG4152 81 ----GLYPKMKVgeqlvylarlkgLSKAEAKrradewlerlGLGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 712 LSALDAhVGNHIFNSAIR-KRLKSKTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEEL 770
Cdd:COG4152 157 FSGLDP-VNVELLKDVIReLAAKGTTVIFSSHQME-LVEelCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
575-744 |
1.00e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.98 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAiLGQMTLLEGSIAVSGTFAYVAQQAWI----LNATLRD-NILFGKE- 648
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYErrvnLNRLRRQvSMVHPKPn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 649 -FDEERYNSVLNSCCL---RPDLAI-------LPNSDL-----TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:PRK14258 99 lFPMSVYDNVAYGVKIvgwRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190
....*....|....*....|....*....|...
gi 16758936 713 SALDAHVGNHIFNSAIRKRLKSK-TVLFVTHQL 744
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
580-773 |
1.02e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYV----AQQAWILNATLRD 641
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVpedrKGEGLVLDLSIRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGkefdeeRYNSVLNSCCLRP------------DLAILPNSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILD 709
Cdd:COG1129 350 NITLA------SLDRLSRGGLLDRrreralaeeyikRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 710 DPLSALDahVGNH--IFNsAIRKRLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEELMNL 773
Cdd:COG1129 420 EPTRGID--VGAKaeIYR-LIRELAAEgKAVIVISSELPELLGlSDRILVMREGRIVgeldrEEATEEAIMAA 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1212-1404 |
1.07e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE-LSGGCIKIDG--VRIS------DIGLADL---RSKLTIIPQEPVLF 1279
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRnpqqaiAQGIAMVpedRKRDGIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 SGTVrSNLDPFNQYTeeQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAM 1359
Cdd:PRK13549 361 NITL-AALDRFTGGS--RIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758936 1360 DT----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 1404
Cdd:PRK13549 437 DVgakyEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
580-770 |
1.23e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 65.85 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG------------TFAYVAQQAWILNA-TLRDNI--- 643
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyih 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 --LFGKEFDE--ERYNSVLNSCclrpdlailpnsDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 718
Cdd:cd03265 98 arLYGVPGAErrERIDELLDFV------------GLLEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 719 VGNHIFnSAIRKRLKSK--TVLFVTHqlqYLVD----CDEVIFMKEGCITERGTHEEL 770
Cdd:cd03265 166 TRAHVW-EYIEKLKEEFgmTILLTTH---YMEEaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
858-1079 |
1.30e-11 |
|
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: 67.04 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWIKQgsgnstVFEGNRSSVSDSMrdNPFLQY---YASIYALSMAVMLILkairGVV 934
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDL------IIEGLGGGGGVDF--SGLLRIlllLLGLYLLSALFSYLQ----NRL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 935 FVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqAEMFIQNVILVFFCVGMIAGVF---- 1010
Cdd:cd18547 69 MARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNI-------SQALSQSLTQLISSILTIVGTLimml 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1011 ---PWF-LVAVGPLLILFSVLHIV---SRVLIREL-KRLDNITqspflSHITSSIQGLATIHAYNKRQEFLHRYQEL 1079
Cdd:cd18547 142 yisPLLtLIVLVTVPLSLLVTKFIakrSQKYFRKQqKALGELN-----GYIEEMISGQKVVKAFNREEEAIEEFDEI 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
575-761 |
1.30e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRT-LYNIDLEIEEGKLVGICGSVGSGKTSLISAILG-----QMTLLEGSIAVsgtfayvaqqawilnATLRDNILFgkE 648
Cdd:PRK11247 24 ERTvLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsAGELLAGTAPL---------------AEAREDTRL--M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 649 FDEER---YNSVLNSCCL------RPD-LAILPNSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:PRK11247 87 FQDARllpWKKVIDNVGLglkgqwRDAaLQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16758936 718 HvgNHIFNSAIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCI 761
Cdd:PRK11247 167 L--TRIEMQDLIESLWQQhgfTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
573-769 |
1.34e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.98 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------------FAYVAQQAWIL 635
Cdd:PRK11144 9 QLGDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 636 -NATLRDNILFG-KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK11144 89 pHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 714 ALDAHvgnhifnsaiRKR-----LK--SKTV----LFVTHQLQYLVD-CDEVIFMKEGCITERGTHEE 769
Cdd:PRK11144 158 SLDLP----------RKRellpyLErlAREInipiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1166-1406 |
1.36e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1166 IKTLSLEAP-ARIKNKAPPHDWPQegeITFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 1244
Cdd:PRK10522 299 LNKLALAPYkAEFPRPQAFPDWQT---LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1245 LSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTvrsnLDPFNQYTEEQIWDA-LERTHMKEciaqlplKLEsevM 1323
Cdd:PRK10522 375 PQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAH-------KLE---L 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1324 ENGD----NFSVGERQLLCIARALLRHCKILILDEATAAMDTE------TDLL--IQETIREAFAdctmltIAHRLHTVL 1391
Cdd:PRK10522 441 EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLplLQEMGKTIFA------ISHDDHYFI 514
|
250
....*....|....*
gi 16758936 1392 GSDRIMVLAQGQVVE 1406
Cdd:PRK10522 515 HADRLLEMRNGQLSE 529
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1192-1413 |
1.45e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 65.47 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDiglaDLRSK 1268
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvVREPR----EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1269 LTIIPQEPVLFSG-TVRSNLdpfnqYTEEQIWdALERTHMKECIAQLpLKLeSEVMENGD----NFSVGERQLLCIARAL 1343
Cdd:cd03265 75 IGIVFQDLSVDDElTGWENL-----YIHARLY-GVPGAERRERIDEL-LDF-VGLLEAADrlvkTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1344 LRHCKILILDEATAAMDTETDLLIQETIR---EAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1413
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
576-810 |
1.55e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGqMTLLEGSIAVSGTFAYVAQ---------------------QAWI 634
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG-LIISETGQTIVGDYAIPANlkkikevkrlrkeiglvfqfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 635 LNATLRDNILFGK----EFDEERYNSVLNSCclrpDLAILPNsdltEIGERGA-NLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK13645 104 FQETIEKDIAFGPvnlgENKQEAYKKVPELL----KLVQLPE----DYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 710 DPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEElmnlngdyatIFNNLLLg 787
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFE----------IFSNQEL- 244
|
250 260
....*....|....*....|...
gi 16758936 788 eTPPVEINSKKEASGSQKSQDKG 810
Cdd:PRK13645 245 -LTKIEIDPPKLYQLMYKLKNKG 266
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1209-1403 |
1.56e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDGVRISDIGLADL-RSKLTIIPQEPVLF 1279
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKV-----LSGvyphgtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 SG-TVRSNLDPFNQYTEEQI--WDALERtHMKECIAQLPLKL--ESEVMENGdnfsVGERQLLCIARALLRHCKILILDE 1354
Cdd:PRK13549 95 KElSVLENIFLGNEITPGGImdYDAMYL-RAQKLLAQLKLDInpATPVGNLG----LGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1355 ATAAM-DTETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 1403
Cdd:PRK13549 170 PTASLtESETAVLL-DIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1212-1415 |
1.56e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.68 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGG--CIKI--DGVRISDIGLaDLRSKLT----IIPQEPVLFsgTV 1283
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVgdEWVDMTKPGP-DGRGRAKryigILHQEYDLY--PH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 RSNLDPFNQYTEEQIWDALERthMKECIAQLPLKLESEVMEN-----GDNFSVGERQLLCIARALLRHCKILILDEATAA 1358
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELAR--MKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1359 MDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
576-742 |
1.62e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLY-NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG--TFAYVAQQAWIL-NATLRDNILFG-KEFD 650
Cdd:COG0488 11 RPLLdDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDdDLTVLDTVLDGdAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 651 E--ERYNSVLNSCCLRPDLAILPNSDLTEIGERGA--------------------------NLSGGQRQRISLARALYSD 702
Cdd:COG0488 91 AleAELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16758936 703 RSIYILDDPLSALDAHvgnhifnsAIR---KRLKS--KTVLFVTH 742
Cdd:COG0488 171 PDLLLLDEPTNHLDLE--------SIEwleEFLKNypGTVLVVSH 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
578-749 |
1.74e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.46 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------------FAYVAQQAWIL-NATLR 640
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDFRLLpDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILF-----GKEFDE--ERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:COG2884 98 ENVALplrvtGKSRKEirRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16758936 710 DPLSALDAHVGNHIFN--SAIRKRlkSKTVLFVTHQLQyLVD 749
Cdd:COG2884 163 EPTGNLDPETSWEIMEllEEINRR--GTTVLIATHDLE-LVD 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1212-1416 |
1.77e-11 |
|
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: 67.43 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLTIIPQEPVLFSG-TVRSN 1286
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFPHlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LdpfnQYTEEQIWDALERTHMKECIAQL---PLkLESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1363
Cdd:COG4148 98 L----LYGRKRAPRAERRISFDEVVELLgigHL-LDRRP----ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1364 -----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:COG4148 169 kaeilPYL--ERLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1208-1423 |
1.97e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.27 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElsggciKIDGVRIS-DIGLA-----------DLRSKLTIIPQE 1275
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMND------KVSGYRYSgDVLLGgrsifnyrdvlEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1276 PVLFSGTVRSN---------LDPFNQY--------TEEQIWDALerthmKECIAQLPLKLesevmengdnfSVGERQLLC 1338
Cdd:PRK14271 110 PNPFPMSIMDNvlagvrahkLVPRKEFrgvaqarlTEVGLWDAV-----KDRLSDSPFRL-----------SGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1339 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN- 1416
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSp 253
|
250
....*....|
gi 16758936 1417 ---DSSRFYA 1423
Cdd:PRK14271 254 khaETARYVA 263
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1212-1406 |
2.01e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.91 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLTIIPQEPVlfsgtvrSNLD 1288
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEAQKLLRQKIQIVFQNPY-------GSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1289 P---FNQYTEE--QIWDALERTHMKECIAQLPLK--LESEV------MengdnFSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:PRK11308 107 PrkkVGQILEEplLINTSLSAAERREKALAMMAKvgLRPEHydryphM-----FSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1356 TAAMDTEtdllIQETIREAFAD------CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:PRK11308 182 VSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
576-772 |
2.04e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.29 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSI------------------------AVSGTFAYVA 629
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgepcpVCGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 630 QQAWILNATLRDN------ILFGKEF----DEERYNSVLNS---CCLRPDLAILPNSDLTE---IGER----GANLSGGQ 689
Cdd:TIGR03269 94 VDFWNLSDKLRRRirkriaIMLQRTFalygDDTVLDNVLEAleeIGYEGKEAVGRAVDLIEmvqLSHRithiARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 690 RQRISLARALYSDRSIYILDDPLSALDAHVGNhIFNSAIRKRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 766
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252
|
....*.
gi 16758936 767 HEELMN 772
Cdd:TIGR03269 253 PDEVVA 258
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
575-765 |
2.09e-11 |
|
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: 64.91 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGkLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG------------TFAYVAQQ-AWILNATLRD 641
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NIlfgkefdeeRYNSVLNSC----CLRPDLAILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:cd03264 92 FL---------DYIAWLKGIpskeVKARVDEVLELVNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 717 ahVGNHI-FNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 765
Cdd:cd03264 163 --PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
578-757 |
2.32e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----------FAYVAQQA---WILNATLRDNIL 644
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FG-----------KEFDEERYNSVLNscclRPDLAILPNSdltEIGErganLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK15056 103 MGryghmgwlrraKKRDRQIVTAALA----RVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16758936 714 ALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMK 757
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1213-1405 |
2.52e-11 |
|
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: 64.82 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1213 SFTIKPKEKIGIVGRTGSGKSSLG--MALFrLVELSGGcIKIDGVrisDIGLADL-RSKLTIIPQEPVLFSG-TVRSNLD 1288
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLnlIAGF-ETPQSGR-VLINGV---DVTAAPPaDRPVSMLFQENNLFAHlTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1289 ----PFNQYTEEQ---IWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMD- 1360
Cdd:cd03298 93 lglsPGLKLTAEDrqaIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDp 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16758936 1361 ---TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:cd03298 162 alrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1209-1415 |
2.61e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdIGLADLRS-KLTIIPQEPV---------- 1277
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1278 -LFSGTVRSNLDPFNQYTEEQIWDALERTHM-KECIAQLPLKLESevmengdnfsvGERQLLCIARALLRHCKILILDEA 1355
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1356 TAAMDTETD-------LLIQETIREAFADCTMlTIAHRLHTvlgSDRIMVLAQGQVVEF-DTPSVLLS 1415
Cdd:PRK15112 177 LASLDMSMRsqlinlmLELQEKQGISYIYVTQ-HLGMMKHI---SDQVLVMHQGEVVERgSTADVLAS 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
578-742 |
3.25e-11 |
|
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: 64.35 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT---------FAYVAQQ--------AWILNATLR 640
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRKigvvfqdfRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGKEFDE-------ERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:cd03292 97 ENVAFALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*....
gi 16758936 714 ALDAHVGNHIFNSAIRKRLKSKTVLFVTH 742
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1192-1417 |
3.32e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTI 1271
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEP--VLFSGTVRSNL--DPFNQ-----YTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARA 1342
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVafGPVNMgldkdEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1343 LLRHCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRLhnqgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
.
gi 16758936 1417 D 1417
Cdd:PRK13647 229 D 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
578-772 |
3.63e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIA------------------------------------- 620
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklviqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 621 ----VSGTFAYVAQQawILNATLRDNILFG-------KEFDEERYNSVLNSCCLrpDLAILPNSDLteigergaNLSGGQ 689
Cdd:PRK13651 103 irrrVGVVFQFAEYQ--LFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRSPF--------ELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 690 RQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKRL--KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG- 765
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGd 248
|
....*..
gi 16758936 766 THEELMN 772
Cdd:PRK13651 249 TYDILSD 255
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
580-770 |
3.63e-11 |
|
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: 66.23 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGqmtLLEGSIAVSGT-----------------------FAYVAQQA---- 632
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILG---LLPPPGITSGEilfdgedllklsekelrkirgreIQMIFQDPmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 633 -------WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAIL---PNsdlteigergaNLSGGQRQRISLARALYSD 702
Cdd:COG0444 100 npvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 703 RSIYILDDPLSALDAHVGNHIFN--SAIRKRLKSkTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEEL 770
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAQILNllKDLQRELGL-AILFITHDLgvvAEI--ADRVAVMYAGRIVEEGPVEEL 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1194-1408 |
3.69e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1194 FENAEMRYreNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLvelsggcikIDGVRISDIGLADLRSKLTI-- 1271
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKI---------LAGELEPDSGEVSIPKGLRIgy 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSG-TVRSN-LDPFNQYTEeqIWDALERTHMKECIAQLPLKLESEVME-----NG------------------ 1326
Cdd:COG0488 66 LPQEPPLDDDlTVLDTvLDGDAELRA--LEAELEELEAKLAEPDEDLERLAELQEefealGGweaearaeeilsglgfpe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1327 -------DNFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLLIQEtireafaDCTMLTIAH-R--LHTVl 1391
Cdd:COG0488 144 edldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY-------PGTVLVVSHdRyfLDRV- 215
|
250
....*....|....*..
gi 16758936 1392 gSDRIMVLAQGQVVEFD 1408
Cdd:COG0488 216 -ATRILELDRGKLTLYP 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1191-1410 |
3.85e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.81 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1191 EITFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIdGVRISDIG-----L 1262
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1263 ADLRSKLTIIPQ--EPVLFSGTVRSNL--DPFNQYTEEQiwDALERThmKECIAQlpLKLESEVMENGD-NFSVGERQLL 1337
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDIcfGPMNFGVSEE--DAKQKA--REMIEL--VGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1338 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1410
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
578-780 |
4.42e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.50 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTfAYVAQQAWILN----------------ATLRD 641
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWNLRrkigmvfqnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGKEFDEERYNSVLNscclRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 721
Cdd:PRK13642 102 DVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 722 HIFNsaIRKRLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATI 780
Cdd:PRK13642 178 EIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
580-772 |
4.68e-11 |
|
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: 64.49 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTF--------------AYVAQQAWIL-NATLRDNIL 644
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarlgiGYLPQEASIFrKLTVEENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 -------FGKEFDEERYNSVLNscclrpDLAILPNSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03218 98 avleirgLSKKEREEKLEELLE------EFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 718 HVGNHIfnSAIRKRLKSKT--VLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:cd03218 167 IAVQDI--QKIIKILKDRGigVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
583-781 |
5.11e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.60 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 583 LEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTfayvaQQAWILNATLRdnilfgkEFDEERYNSVLNSCC 662
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIAKISDAELR-------EVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 663 LRPDLAILPNSD--------------------LTEIG-ERGAN-----LSGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:PRK10070 117 LMPHMTVLDNTAfgmelaginaeerrekaldaLRQVGlENYAHsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 717 AHVGNHIFNSAIRKRLK-SKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELM-NLNGDYATIF 781
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILnNPANDYVRTF 264
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
578-768 |
5.55e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.27 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAilgqMTLLEgsIAVSGTFAyVAQQAWILNAT--------LRDNIlfGKEF 649
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLE--MPRSGTLN-IAGNHFDFSKTpsdkaireLRRNV--GMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 650 deERYN-----SVLNSCCLRP--------------DLAILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK11124 89 --QQYNlwphlTVQQNLIEAPcrvlglskdqalarAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 710 DPLSALDAHVGNHIFNsaIRKRLKSK--TVLFVTHQlqylVD-----CDEVIFMKEGCITERGTHE 768
Cdd:PRK11124 167 EPTAALDPEITAQIVS--IIRELAETgiTQVIVTHE----VEvarktASRVVYMENGHIVEQGDAS 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
578-763 |
6.18e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 63.99 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--FAyvaqqawiLN----ATLR-DNILFgkefd 650
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlFA--------LDedarARLRaRHVGF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 651 eerynsVLNSCCLRPDLAILPN----------SDLTEI----------GERG----ANLSGGQRQRISLARALYSDRSIY 706
Cdd:COG4181 95 ------VFQSFQLLPTLTALENvmlplelagrRDARARarallervglGHRLdhypAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 707 ILDDPLSALDAHVGNHI----FnsAIRKRLKSkTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:COG4181 169 FADEPTGNLDAATGEQIidllF--ELNRERGT-TLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
566-742 |
7.01e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.27 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 566 QIHAGSMRLqrtLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQmtlLEGSIAVSGtfayvaqQAWI-------LNAT 638
Cdd:COG4136 8 TITLGGRPL---LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFSASG-------EVLLngrrltaLPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LR------------------DNILFG---KEFDEERYNSVLNScclrpdlaiLPNSDLTEIGERG-ANLSGGQRQRISLA 696
Cdd:COG4136 75 QRrigilfqddllfphlsvgENLAFAlppTIGRAQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758936 697 RALYSDRSIYILDDPLSALDAH----VGNHIFNSAIRKRLkskTVLFVTH 742
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAAlraqFREFVFEQIRQRGI---PALLVTH 192
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1208-1417 |
8.83e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGL-ADLRSKLTIIPQEPVLFSG-TVRS 1285
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 NLdpfnqYTEEQIWDALERTHMKECIAQLPLKLESEVMEN--GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1363
Cdd:PRK10895 98 NL-----MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1364 DLLIQETIrEAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1417
Cdd:PRK10895 173 VIDIKRII-EHLRDSGLgvLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1207-1416 |
9.56e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.03 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1207 LVLKKVSFTIkPKEKI-GIVGRTGSGKSSLGMALFRLVELSGGCiKIDGVRI--------SDIGLADLRSKLTIIPQEPV 1277
Cdd:PRK14243 24 LAVKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1278 LFSGTVRSNLD---PFNQYTEEQiwDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1354
Cdd:PRK14243 102 PFPKSIYDNIAygaRINGYKGDM--DELVERSLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1355 ATAAMDTETDLLIQETIREAFADCTMLTIAHRLH---------------TVLGSDRimvlaQGQVVEFDTPSVLLSN 1416
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQqaarvsdmtaffnveLTEGGGR-----YGYLVEFDRTEKIFNS 249
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
575-771 |
9.79e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.88 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-------------FAYVAQQAWILNA-TLR 640
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGK-----------EFDEERYNSVLNscclRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK11231 95 ELVAYGRspwlslwgrlsAEDNARVNQAME----QTRINHLADRRLTD-------LSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 710 DPLSALDAhvgNHIFN--SAIRK-RLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELM 771
Cdd:PRK11231 164 EPTTYLDI---NHQVElmRLMRElNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1208-1406 |
1.04e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.54 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIgLADLRSK--LTIIPQEPVLFSGtv 1283
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDL-PPEERARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 rsnldpfnqyteeqiwdalerthmkeciaqlpLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1363
Cdd:cd03217 92 --------------------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16758936 1364 DLLIQETIRE-AFADCTMLTIAH--RLHTVLGSDRIMVLAQGQVVE 1406
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1212-1404 |
1.09e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-GGCIKIDGVRISDIGLAD-LRSKLTIIPQE-------PVLFSG- 1281
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQaIRAGIAMVPEDrkrhgivPILGVGk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 -TVRSNLDPFNQYTeeQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMD 1360
Cdd:TIGR02633 359 nITLSVLKSFCFKM--RIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16758936 1361 T----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 1404
Cdd:TIGR02633 436 VgakyEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
578-766 |
1.15e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTfaYVAQQAWILNATLRDNIL-FGKEFDEeryns 656
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQKLgFIYQFHH----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 657 vlnsccLRPDLAILPN--------------------SDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:PRK11629 98 ------LLPDFTALENvamplligkkkpaeinsralEMLAAVGlehranHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 711 PLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 766
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1201-1371 |
1.15e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1201 YRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFS 1280
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1281 GTVRSNLD-PF---NQYTEEQ-IWDALERTHMKECIAQLPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:PRK10247 95 DTVYDNLIfPWqirNQQPDPAiFLDDLERFALPDTILTKNI----------AELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170
....*....|....*.
gi 16758936 1356 TAAMDTETDLLIQETI 1371
Cdd:PRK10247 165 TSALDESNKHNVNEII 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1192-1405 |
1.15e-10 |
|
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: 62.68 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiglADLRSKLTI 1271
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSG-TVRSNLDPFNQ-------YTEEQIWDALERTHMKEciaqlplKLESEVMEngdnFSVGERQLLCIARAL 1343
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYLAQlkglkkeEARRRIDEWLERLELSE-------YANKRVEE----LSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758936 1344 LRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
584-743 |
1.17e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.31 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 584 EIEEGKLVGICGSVGSGKTSLISaILGQMTLLEG---SIAVSGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNS 660
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 661 cclrpDL-AILPNSDLTEIGERGAN----------LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR 729
Cdd:TIGR00954 553 -----DLeQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE 627
|
170
....*....|....
gi 16758936 730 KRLkskTVLFVTHQ 743
Cdd:TIGR00954 628 FGI---TLFSVSHR 638
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
573-743 |
1.17e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT------------FAYVAQQAWI---LN 636
Cdd:PRK13538 11 RDERILFsGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrdeyhqdLLYLGHQPGIkteLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 637 AtlrdnilfgkefdEE--RYNSVLnSCCLRPDLAIlpnSDLTEIGERG------ANLSGGQRQRISLARALYSDRSIYIL 708
Cdd:PRK13538 91 A-------------LEnlRFYQRL-HGPGDDEALW---EALAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16758936 709 DDPLSALD--------AHVGNHIFNSAIrkrlksktVLFVTHQ 743
Cdd:PRK13538 154 DEPFTAIDkqgvarleALLAQHAEQGGM--------VILTTHQ 188
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1215-1398 |
1.20e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.58 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1215 TIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdigladlRSKLTIIPQepvlFSGTVRSNLdpfnqyt 1294
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------YKPQYIKAD----YEGTVRDLL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1295 EEQIWDALERTHMKECIAQlPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREa 1374
Cdd:cd03237 83 SSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR- 160
|
170 180
....*....|....*....|....*...
gi 16758936 1375 FA---DCTMLTIAHRLHTV-LGSDRIMV 1398
Cdd:cd03237 161 FAennEKTAFVVEHDIIMIdYLADRLIV 188
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
578-772 |
1.50e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-----------------TFAYVAQ--QAWILNAT 638
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFG-KEFdeerynsvlnscclrpdlailpNSDLTEIGERGANL------------------SGGQRQRISLARAL 699
Cdd:PRK13646 103 VEREIIFGpKNF----------------------KMNLDEVKNYAHRLlmdlgfsrdvmsqspfqmSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 700 YSDRSIYILDDPLSALDAHVGNHIFNsaIRKRLK---SKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMR--LLKSLQtdeNKTIILVSHDMnevaRY---ADEVIVMKEGSIVSQTSPKELFK 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1208-1406 |
1.54e-10 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 62.93 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLTI--IPQEPVLFSG-TVR 1284
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-PHERARAGIayVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLdpfnqyteEQIWDALERTHMK--ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTE 1362
Cdd:TIGR03410 94 ENL--------LTGLAALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 1363 TDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:TIGR03410 166 IIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVA 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1209-1410 |
1.61e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 62.87 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrskltiiPQEPVLFSG------- 1281
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQNysllpwl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 TVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEvmENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1361
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAAD--KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1362 ETDLLIQETIREAFAD--CTMLTIAHRL-HTVLGSDRIMVLAQ------GQVVEFDTP 1410
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEhrVTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEVPFP 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1192-1417 |
1.77e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.06 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADL-RSKLT 1270
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRARHaRQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1271 IIPQ----EPVLfsgTVRSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLESEVMEngdnFSVGERQLLCIARALLRH 1346
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1347 CKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSVLLSND 1417
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
904-1033 |
1.85e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 63.72 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 904 MRDNPFLQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV 983
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSD 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 16758936 984 RLPFQAEMFIQNVILVFFCVGMIAGVfPWFLVAVGplLILFSVLHIVSRV 1033
Cdd:cd18572 109 PLSTNLNVFLRNLVQLVGGLAFMFSL-SWRLTLLA--FITVPVIALITKV 155
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1416 |
1.99e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.17 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI--SDIGLADLRSKLTIIPQEP--VLFSGTV 1283
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 RSNL--DPFN-----QYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEAT 1356
Cdd:PRK13639 97 EEDVafGPLNlglskEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1357 AAMD----TETDLLIQETIREAfadctmLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:PRK13639 166 SGLDpmgaSQIMKLLYDLNKEG------ITIIISTHDVdlvpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1208-1406 |
1.99e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKLTIIPQEP---VLFSG 1281
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 TVRSNLD-PFNQYT----EEQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEAT 1356
Cdd:PRK10419 107 TVREIIRePLRHLLsldkAERLARASEMLRAVDLDDSVLDKRPPQL-------SGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1357 AAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:PRK10419 180 SNL----DLVLQagvirllKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
560-770 |
2.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.18 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 560 EEEEGKQIHAgsmrlqrtLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAW------ 633
Cdd:PRK13633 16 SNEESTEKLA--------LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnka 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 634 ----------ILNATLRDNILFGKEfdeerynsvlnscclrpDLAILPNsdltEIGERGAN-----------------LS 686
Cdd:PRK13633 88 gmvfqnpdnqIVATIVEEDVAFGPE-----------------NLGIPPE----EIRERVDEslkkvgmyeyrrhaphlLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 687 GGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAirKRLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTI--KELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVM 224
|
....*..
gi 16758936 764 RGTHEEL 770
Cdd:PRK13633 225 EGTPKEI 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1159-1408 |
2.53e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1159 VERINHYIKtLSLEAPARIKNKApphdwpqegeITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSlgma 1238
Cdd:COG0488 294 PPRRDKTVE-IRFPPPERLGKKV----------LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1239 LFRL----VELSGGCIKI-DGVRIS--DIGLADLRSKLTIIpqepvlfsgtvrsnldpfnqyteEQIWDALERTHMKECI 1311
Cdd:COG0488 357 LLKLlageLEPDSGTVKLgETVKIGyfDQHQEELDPDKTVL-----------------------DELRDGAPGGTEQEVR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1312 AQL------PLKLESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliqetiREAFADC------T 1379
Cdd:COG0488 414 GYLgrflfsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgT 481
|
250 260 270
....*....|....*....|....*....|..
gi 16758936 1380 MLTIAH-R--LHTVlgSDRIMVLAQGQVVEFD 1408
Cdd:COG0488 482 VLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
577-772 |
2.64e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI------AVSGTFAYVAQQAWIL---------NATLRD 641
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHIGIVfqnpdnqfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGKE-----FDE--ERYNSVLNscclrpDLAILPNSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK13648 104 DVAFGLEnhavpYDEmhRRVSEALK------QVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 715 LDAHVGNHIFNsaIRKRLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13648 173 LDPDARQNLLD--LVRKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
683-772 |
2.65e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 683 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKE 758
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL--ALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQ 501
|
90
....*....|....
gi 16758936 759 GCITERGTHEELMN 772
Cdd:PRK15134 502 GEVVEQGDCERVFA 515
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1192-1385 |
2.81e-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: 59.77 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcikidgvrisdigladlrskLTI 1271
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1272 IPQEPVLFSGTVrsnldpfnqyteeqiwdaleRTHMKECIAQLPlklesevmengdNFSVGERQLLCIARALLRHCKILI 1351
Cdd:cd03221 46 IAGELEPDEGIV--------------------TWGSTVKIGYFE------------QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 16758936 1352 LDEATAAMDTETDLLIQETIREaFaDCTMLTIAH 1385
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-Y-PGTVILVSH 125
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
580-765 |
3.05e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG----TFAYVAQQAWIL---------NATLRDNIL-F 645
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVvpqfdnldpDFTVRENLLvF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 GKEFD------EERYNSVLnscclrpDLAILPNSDLTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHv 719
Cdd:PRK13537 105 GRYFGlsaaaaRALVPPLL-------EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 720 GNHIfnsaIRKRLKS-----KTVLFVTHqlqylvdcdeviFMKEG-------CITERG 765
Cdd:PRK13537 173 ARHL----MWERLRSllargKTILLTTH------------FMEEAerlcdrlCVIEEG 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
582-780 |
3.51e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 582 DLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFAYVAQQ-AWIL--------NATLRDNILFGkef 649
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRpVSMLfqennlfsHLTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 650 deerynsvlnsccLRPDL-----------AILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:PRK10771 96 -------------LNPGLklnaaqreklhAIARQMGIEDLLARlPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 718 HVGNHIFN----SAIRKRLkskTVLFVTHQLQylvDCDEV----IFMKEGCITERGTHEELMNLNGDYATI 780
Cdd:PRK10771 163 ALRQEMLTlvsqVCQERQL---TLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
179-447 |
3.53e-10 |
|
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: 62.66 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 179 LILSIVCLMITQLAGFSGPaFVVKHLLE-YTQATESNLQYSLLLVLGLLLTEVVRSWSLALTWALNYRTGVRLRGAVLTM 257
Cdd:pfam00664 1 LILAILLAILSGAISPAFP-LVLGRILDvLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 258 AFKKILKLKNI--KEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPT-GFLGSAVFILFYPAMM 334
Cdd:pfam00664 80 LFKKILRQPMSffDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 335 FVSRLTAYFRRKCVAATDDRVQKMNEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIAS 414
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 16758936 415 VVT--FSVHMTLGFDLTAAQAFTVVTVFNSMTFAL 447
Cdd:pfam00664 240 ALAlwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1211-1409 |
4.33e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1211 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDI---GLADLRS-KLTIIPQEPVlfsgtv 1283
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLpekELNKLRAeQISMIFQDPM------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 rSNLDPFNQyTEEQIWDAL-------------ERTHMKECIaQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKIL 1350
Cdd:PRK09473 108 -TSLNPYMR-VGEQLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARKRMKMYPHE-FSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758936 1351 ILDEATAAMDTETD----LLIQETIREaFaDCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEFDT 1409
Cdd:PRK09473 184 IADEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
580-771 |
4.93e-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: 63.67 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGqmtLLEGSiavSGTFAYVAQQAWIlNATLRDNILFGKEfdeERYNSVLN 659
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG---VLEPT---SGEVNVRVGDEWV-DMTKPGPDGRGRA---KRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 660 S-CCLRPDLAILPNsdLT---------EIGERGA-----------------------NLSGGQRQRISLARALYSDRSIY 706
Cdd:TIGR03269 372 QeYDLYPHRTVLDN--LTeaiglelpdELARMKAvitlkmvgfdeekaeeildkypdELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 707 ILDDPLSALDAHVGNHIFNSAIRKRLK-SKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
577-770 |
4.93e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.06 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 577 TLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTfAYVAQQAW----------------ILNATLR 640
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvfqnpdnqFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGKE-----FDE--ERYNSVLNSCclrpdlailpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:PRK13650 101 DDVAFGLEnkgipHEEmkERVNEALELV------------GMQDFKEREpARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 713 SALDAHVGNHIFNS--AIRKRLKsKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13650 169 SMLDPEGRLELIKTikGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
575-772 |
6.59e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.33 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAIlGQMTLLEGSIAVSGTFAY---------------------VAQQAW 633
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 634 ILNATLRDNILFGKEFDEERYNSVLNSCCLRpdlAILPNSDLTEIGER----GANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK14239 97 PFPMSIYENVVYGLRLKGIKDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 710 DPLSALDAHVGNHIFNSAIrkRLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERG-THEELMN 772
Cdd:PRK14239 174 EPTSALDPISAGKIEETLL--GLKDDyTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNdTKQMFMN 237
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
891-1138 |
6.61e-10 |
|
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: 62.11 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 891 TVFEGNRSSVSDSMRDnpfLQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRI 970
Cdd:cd18577 30 TDFGSGESSPDEFLDD---VNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 971 LNRFSKDMDEVdvrlpfQ---AE---MFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLLILfsVLHIVSRVLIR-E 1037
Cdd:cd18577 107 TSRLTSDTNLI------QdgiGEklgLLIQSLSTFIagFIIAFIYS---WkltlVLLATLPLIAI--VGGIMGKLLSKyT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1038 LKRLDNITQSpfLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDnqapfflftcAMRWlAVRLDLISialitttGLMIV 1117
Cdd:cd18577 176 KKEQEAYAKA--GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEK----------ARKA-GIKKGLVS-------GLGLG 235
|
250 260
....*....|....*....|.
gi 16758936 1118 LMHGQIPSAYAgLAISYAVQL 1138
Cdd:cd18577 236 LLFFIIFAMYA-LAFWYGSRL 255
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
281-770 |
6.78e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.28 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 281 SNDGQRMFEAAAVGSLLAGGPVVAILGMIYnVIILGPTGFLGSAVFI----LFYpaMMFVSRLTAYFRRkcVAATDDRVQ 356
Cdd:COG4615 112 TEDVRTISQAFVRLPELLQSVALVLGCLAY-LAWLSPPLFLLTLVLLglgvAGY--RLLVRRARRHLRR--AREAEDRLF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 357 K-MNEVLTYIKFIKM--------YAwvKAFSQCVQKIREEERRilekAGYFQSITVGVAPIV--VVIASVVTFSVHMtlg 425
Cdd:COG4615 187 KhFRALLEGFKELKLnrrrrrafFD--EDLQPTAERYRDLRIR----ADTIFALANNWGNLLffALIGLILFLLPAL--- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 426 FDLTAAQAFTVVTVF----NSMTFALKVTPfsvkSLSEASVAVDRFKSLFLMEE------VHMIKNKPASPHIKIEMKNA 495
Cdd:COG4615 258 GWADPAVLSGFVLVLlflrGPLSQLVGALP----TLSRANVALRKIEELELALAaaepaaADAAAPPAPADFQTLELRGV 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 496 TLAWdsshsstqsspkltpkvkkdkrapkgkkeksrqlqhtehqavlaeqkghllldsderpsPEEEEGKQIHAGsmrlq 575
Cdd:COG4615 334 TYRY-----------------------------------------------------------PGEDGDEGFTLG----- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 rtlyNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGtfAYVAQQAWilnATLRDNI--------LF-- 645
Cdd:COG4615 350 ----PIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNR---EAYRQLFsavfsdfhLFdr 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 ----GKEFDEERYNSVLNscclrpDLAIlpnSDLTEIgERGA----NLSGGQRQRISLARALYSDRSIYILD------DP 711
Cdd:COG4615 421 llglDGEADPARARELLE------RLEL---DHKVSV-EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDewaadqDP 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 712 lsaldahVGNHIFNSAIRKRLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:COG4615 491 -------EFRRVFYTELLPELKArgKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
581-770 |
7.06e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.55 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 581 IDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-----------FAYVAQQ-AWILNATLRDNILFG-- 646
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSVRENMAYGlk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 647 -----KEFDEERynsvlnscclrpdlaILPNSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:PRK11650 103 irgmpKAEIEER---------------VAEAARILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 718 HVGNHIfNSAIRK---RLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK11650 168 KLRVQM-RLEIQRlhrRLKT-TSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1208-1410 |
7.55e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.87 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS---DIGLAdLRSKLTIIpqEPVLFSGTVr 1284
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSallELGAG-FHPELTGR--ENIYLNGRL- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 snldpfNQYTEEQIwdaleRTHMKECIA--------QLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEAT 1356
Cdd:COG1134 116 ------LGLSRKEI-----DEKFDEIVEfaelgdfiDQPVK----------TYSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1357 AAMDTE-----TDlLIQETIREAfadCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1410
Cdd:COG1134 175 AVGDAAfqkkcLA-RIRELRESG---RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1209-1417 |
7.63e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.18 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----------VELSGGCIKIDGVRISDIGLA-----------DLRS 1267
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARDIRKSrantgyifqqfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1268 KLTIIpqEPVLFS--GTV---RSNLDPFNQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARA 1342
Cdd:PRK09984 100 RLSVL--ENVLIGalGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTL-----------SGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1343 LLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVeFDTPSVLLSND 1417
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQFDNE 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
565-761 |
7.92e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.26 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 565 KQIHAGSMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFAYVAQQA-WIL----- 635
Cdd:COG1101 9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRAkYIGrvfqd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 636 -------NATLRDNILF----GKEF---------DEERYnsvlnscclRPDLAILpnsDL-------TEIGergaNLSGG 688
Cdd:COG1101 89 pmmgtapSMTIEENLALayrrGKRRglrrgltkkRRELF---------RELLATL---GLglenrldTKVG----LLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 689 QRQRISLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAIRKrlKSKTVLFVTHQLQYLVDC-DEVIFMKEGCI 761
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDpktAALVLELTEKIVEE--NNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1208-1401 |
8.01e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID-GVRISDIgladlRSKLTIIPQEPVLFSGTVRsn 1286
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYV-----PQKLYLDTTLPLTVNRFLR-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LDPFNQytEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDL- 1365
Cdd:PRK09544 92 LRPGTK--KEDILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVa 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16758936 1366 ---LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQ 1401
Cdd:PRK09544 159 lydLIDQLRRE--LDCAVLMVSHDLHLVMAkTDEVLCLNH 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
580-771 |
8.08e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 8.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVS------GTFAYVAQQ------------------AWIL 635
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRirmifqdpstslnprqriSQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 636 NATLRDNILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK15112 111 DFPLRLNTDLEPEQREKQIIETLRQVGLLPDHAsYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 715 LDAHVGNHIFNSAIRKRLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 771
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
905-1121 |
8.15e-10 |
|
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: 61.71 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 905 RDNPFLQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvr 984
Cdd:cd18545 34 GDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 985 lpfqAEMF---IQNVILVFFCVGMIAGV---FPWFL----VAVGPLLILFSvlhIVSRVLIRELKRLDNITQSPFLSHIT 1054
Cdd:cd18545 111 ----SDLLsngLINLIPDLLTLVGIVIImfsLNVRLalvtLAVLPLLVLVV---FLLRRRARKAWQRVRKKISNLNAYLH 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1055 SSIQGLATIHAYNKRQEFLHRYQELLDDNQAPFflftcaMRwlAVRL-DLI--SIALITTTGLMIVLMHG 1121
Cdd:cd18545 184 ESISGIRVIQSFAREDENEEIFDELNRENRKAN------MR--AVRLnALFwpLVELISALGTALVYWYG 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1192-1411 |
9.32e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE----LSGGCI----------------- 1250
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDqyepTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1251 ---------------KIDGVRISDIGLADLRSKLTIIPQEPVLFSG--TVRSN-LDPFNQ--YT-EEQIWDALERTHMke 1309
Cdd:TIGR03269 78 vgepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvLEALEEigYEgKEAVGRAVDLIEM-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1310 ciaqlpLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAF--ADCTMLTIAHRL 1387
Cdd:TIGR03269 156 ------VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWP 229
|
250 260
....*....|....*....|....*
gi 16758936 1388 HTVLG-SDRIMVLAQGQVVEFDTPS 1411
Cdd:TIGR03269 230 EVIEDlSDKAIWLENGEIKEEGTPD 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
573-743 |
9.43e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.81 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLYN-IDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT------------FAYVAQQAWILNA-T 638
Cdd:cd03231 10 RDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIKTTlS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFGKEFDEEryNSVLNScclrpdlaiLPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:cd03231 90 VLENLRFWHADHSD--EQVEEA---------LARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*..
gi 16758936 718 HvGNHIFNSAIRKRL-KSKTVLFVTHQ 743
Cdd:cd03231 159 A-GVARFAEAMAGHCaRGGMVVLTTHQ 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
576-763 |
9.55e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLY-NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--FAYVAQQAWIL--NATLRDNILFGKEFD 650
Cdd:COG0488 328 KTLLdDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvkIGYFDQHQEELdpDKTVLDELRDGAPGG 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 651 EERY-NSVLNSCCLRPDLAilpnsdLTEIGergaNLSGGQRQRISLARALYSDRSIYILDDP------------LSALDA 717
Cdd:COG0488 408 TEQEvRGYLGRFLFSGDDA------FKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldietlealEEALDD 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16758936 718 HVGnhifnsairkrlkskTVLFVTHQlQYLVD--CDEVIFMKEGCITE 763
Cdd:COG0488 478 FPG---------------TVLLVSHD-RYFLDrvATRILEFEDGGVRE 509
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1215-1398 |
1.29e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1215 TIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDgVRISdigladlrSKltiiPQE-PVLFSGTVRSNLdpfnqy 1293
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS--------YK----PQYiKPDYDGTVEDLL------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1294 teEQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 1372
Cdd:PRK13409 422 --RSITDDLGSSYYKSEIIK-PLQLE-RLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170 180 190
....*....|....*....|....*....|
gi 16758936 1373 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 1398
Cdd:PRK13409 498 R-IAeerEATALVVDHDIYMIdYISDRLMV 526
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1192-1406 |
1.32e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.63 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGVRI--SDIGLAD 1264
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1265 LRSKLTIIPQEPVLFS----------GTVRSNLDPFNQYTEEQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGER 1334
Cdd:PRK14267 83 VRREVGMVFQYPNPFPhltiydnvaiGVKLNGLVKSKKELDERVEWALKK-------AALWDEVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1335 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHR-LHTVLGSDRIMVLAQGQVVE 1406
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
575-756 |
1.52e-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: 58.87 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILgqmtllegsiavsgtfayvaqqawilnatlrdnilfgKEFDEERY 654
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------------------------------YASGKARL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 655 NSVLNSCCLRPDLAILPNSDLTEIG------ERGAN-LSGGQRQRISLARALYSD--RSIYILDDPLSALDAHVGNHIFN 725
Cdd:cd03238 51 ISFLPKFSRNKLIFIDQLQFLIDVGlgyltlGQKLStLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLE 130
|
170 180 190
....*....|....*....|....*....|.
gi 16758936 726 SAIRKRLKSKTVLFVTHQLQYLVDCDEVIFM 756
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
916-1084 |
1.70e-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: 60.54 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 916 IYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmdevDVrlpfqaeM 991
Cdd:cd18570 43 IISIGLILLYLFQSllsyIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN------DA-------N 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 992 FIQNVI-----------LVFFCVGMIAGVFPW--FLVAVGPLLILFSVLHIVSRVLIRELKRLdNITQSPFLSHITSSIQ 1058
Cdd:cd18570 110 KIREAIssttislfldlLMVIISGIILFFYNWklFLITLLIIPLYILIILLFNKPFKKKNREV-MESNAELNSYLIESLK 188
|
170 180
....*....|....*....|....*.
gi 16758936 1059 GLATIHAYNKRQEFLHRYQELLDDNQ 1084
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1208-1415 |
1.84e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSG-TVR-- 1284
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 ---------SNLDPFNQYTEEQIWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:PRK11231 97 vaygrspwlSLWGRLSAEDNARVNQAMEQTRINH-LADRRL----------TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1356 TAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
580-771 |
1.98e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.90 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-FAYVAQQAW------------------------- 633
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrmqmvfqdpyaslnprmtvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 634 -ILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteigERGAN-LSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:COG4608 116 dIIAEPLRIHGLASKAERRERVAELLELVGLRPEHA-----------DRYPHeFSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 712 LSALDAHVGNHIFNsaIRKRLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELM 771
Cdd:COG4608 185 VSALDVSIQAQVLN--LLEDLQDElglTYLFISHDLsvvRHI--SDRVAVMYLGKIVEIAPRDELY 246
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
571-772 |
2.02e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 571 SMRL-QRT-LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQAWIL 635
Cdd:PRK13548 9 SVRLgGRTlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 636 NA-TLRDNILFGKE---FDEERYNSVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARAL------YSDRSI 705
Cdd:PRK13548 89 FPfTVEEVVAMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVLaqlwepDGPPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 706 YILDDPLSALD-AHvGNHIFNSAirKRLKSK---TVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13548 162 LLLDEPTSALDlAH-QHHVLRLA--RQLAHErglAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVLT 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1192-1418 |
2.28e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS----DIGLAD 1264
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1265 LRSKLTIIPQ--EPVLFSGTVRSNLD--P--FNQYTEEqiwdalerthMKECIAQLPLKL--ESEVMENGD-NFSVGERQ 1335
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIfgPknFKMNLDE----------VKNYAHRLLMDLgfSRDVMSQSPfQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1336 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSV 1412
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
....*.
gi 16758936 1413 LLSNDS 1418
Cdd:PRK13646 233 LFKDKK 238
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1208-1405 |
2.37e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 59.71 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADL-RSKLtI--IPQEPVL---FSG 1281
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYkRAKY-IgrVFQDPMMgtaPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 TVRSNLdpfnqyteeqiwdAL-----------------ERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALL 1344
Cdd:COG1101 98 TIEENL-------------ALayrrgkrrglrrgltkkRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1345 RHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVL--GsDRIMVLAQGQVV 1405
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnnLTTLMVTHNMEQALdyG-NRLIMMHEGRII 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
578-783 |
2.52e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 59.67 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAiLGQMTLLEGSIAVSGTFAY---------------------VAQQAWILN 636
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLIPGARVEGEILLdgediydpdvdvvelrrrvgmVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 637 ATLRDNILFG---------KEFDE--ERynsvlnscCLRpdLAILPNsdltEIGER----GANLSGGQRQRISLARALYS 701
Cdd:COG1117 106 KSIYDNVAYGlrlhgikskSELDEivEE--------SLR--KAALWD----EVKDRlkksALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 702 DRSIYILDDPLSALD----AHVGNHIfnsairKRLKSK-TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEElmnlng 775
Cdd:COG1117 172 EPEVLLMDEPTSALDpistAKIEELI------LELKKDyTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQ------ 239
|
....*...
gi 16758936 776 dyatIFNN 783
Cdd:COG1117 240 ----IFTN 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
576-766 |
2.79e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILG-----QMTLLEGSIAVSGTfayvAQQAWILNATLRDNILFgkEFD 650
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSST----SKQKEIKPVRKKVGVVF--QFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 651 EERY--NSVLNSCCLRPDLAILPNSDLTEIGERGAN---------------LSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:PRK13643 94 ESQLfeETVLKDVAFGPQNFGIPKEKAEKIAAEKLEmvgladefwekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16758936 714 ALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 766
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1209-1405 |
2.86e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLTIIPQE-PVLFSGTVRSN 1286
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LdPFNQYTEEQIW--DALERTHMKECIAQLPLK--LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM-DT 1361
Cdd:PRK09700 101 L-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16758936 1362 ETD---LLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:PRK09700 180 EVDylfLIMNQLRKEGTA---IVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
910-1080 |
3.91e-09 |
|
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: 59.53 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 910 LQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVRLPFQA 989
Cdd:cd18782 41 LYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 990 EMFIQNVILVFFCVGMIAgVFPWFL----VAVGPLLILFSVLhiVSRVLIRELKRLdNITQSPFLSHITSSIQGLATIHA 1065
Cdd:cd18782 120 LTTLLDVLFSVIYIAVLF-SYSPLLtlvvLATVPLQLLLTFL--FGPILRRQIRRR-AEASAKTQSYLVESLTGIQTVKA 195
|
170
....*....|....*
gi 16758936 1066 YNKRQEFLHRYQELL 1080
Cdd:cd18782 196 QNAELKARWRWQNRY 210
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
918-1082 |
3.99e-09 |
|
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: 59.50 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 918 ALSMAVMLILKAIrgVVFVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 991
Cdd:cd18557 39 ALILLAIYLLQSV--FTFVRYYLfniageRIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 992 FIQNVILVFFCVGMIAgVFPWFLVAVgpLLILFSVLHIVSRVLIRELKRLDNITQSPFL---SHITSSIQGLATIHAYNK 1068
Cdd:cd18557 117 LLRNILQVIGGLIILF-ILSWKLTLV--LLLVIPLLLIASKIYGRYIRKLSKEVQDALAkagQVAEESLSNIRTVRSFSA 193
|
170
....*....|....
gi 16758936 1069 RQEFLHRYQELLDD 1082
Cdd:cd18557 194 EEKEIRRYSEALDR 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1208-1405 |
4.14e-09 |
|
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: 58.50 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVR--------ISDIGLAdLRSKLTIIPQEPVLf 1279
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrrkkfLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 sgtvrsnlDPFnqYTEEQIWDaLERTHMKECIAQLP--LKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 1357
Cdd:cd03267 114 --------DSF--YLLAAIYD-LPPARFKKRLDELSelLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1358 AMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1215-1398 |
4.21e-09 |
|
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: 60.95 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1215 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGvrisdiGLADLRSKLTIIPQEPV-LFSGTVRSNLdpfnqy 1293
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTF-------AKILAGVLKPDE------GEVDEDLKISYKPQYISpDYDGTVEEFL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1294 tEEQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 1372
Cdd:COG1245 423 -RSANTDDFGSSYYKTEIIK-PLGLE-KLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|
gi 16758936 1373 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 1398
Cdd:COG1245 500 R-FAenrGKTAMVVDHDIYLIdYISDRLMV 528
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
578-770 |
4.27e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWILNA-------------------- 637
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 TLRDNILF---GKEFDEERYNSVLNSCCLRPdlAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK14246 106 SIYDNIAYplkSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 715 LDAhVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1212-1423 |
4.39e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.23 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIglADLRSKLTIIPQEPVLFSG-TVRSNL--- 1287
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQNIafg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1288 --------DPFNQYTEEQiwdaLERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAM 1359
Cdd:PRK11607 116 lkqdklpkAEIASRVNEM----LGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1360 DTE----TDLLIQETIREAFADCTMLTiaH---RLHTVLGsdRIMVLAQGQVVEFDTPSVLLSNDSSRFYA 1423
Cdd:PRK11607 181 DKKlrdrMQLEVVDILERVGVTCVMVT--HdqeEAMTMAG--RIAIMNRGKFVQIGEPEEIYEHPTTRYSA 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1209-1405 |
4.42e-09 |
|
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: 60.61 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVELSG---GCIKIDGVRISDIGLADLRSK-LTIIPQEPVLFSG-TV 1283
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 RSNLDPFNQYTEE--QIWDALERTHMKECIAQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKILILDEATAAM-D 1360
Cdd:TIGR02633 96 AENIFLGNEITLPggRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSSLtE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 1361 TETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:TIGR02633 175 KETEILL-DIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1198-1419 |
4.63e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.83 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1198 EMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG-----VRISD--IGLAD------ 1264
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDgqLKVADknqlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1265 LRSKLTIIPQEPVLFSG-TVRSNLdpfnQYTEEQIWdALERTHMKECIAQLPLKL---ESEVMENGDNFSVGERQLLCIA 1340
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHmTVLENV----MEAPIQVL-GLSKQEARERAVKYLAKVgidERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1341 RALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
....
gi 16758936 1416 NDSS 1419
Cdd:PRK10619 242 NPQS 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1210-1404 |
5.88e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1210 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLTIIP---QEPVLF------ 1279
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 ---SGTVRSNLDPFNQYTEEQiwDALERTHmkeciAQLPLKLeSEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1356
Cdd:PRK15439 360 wnvCALTHNRRGFWIKPAREN--AVLERYR-----RALNIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758936 1357 AAMDTETDLLIQETIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQV 1404
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
906-1119 |
5.97e-09 |
|
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: 59.39 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 906 DNPFLQYYASIYALSM----AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTP--TGRILNRFSKDMD 979
Cdd:cd18578 43 DDDELRSEANFWALMFlvlaIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDAS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 980 EV----DVRLPfqaeMFIQNVILVFFCVGmIAGVFPWFL----VAVGPLLILFSVLHIvsRVLIR-ELKRLDNITQSpfl 1050
Cdd:cd18578 123 DVrglvGDRLG----LILQAIVTLVAGLI-IAFVYGWKLalvgLATVPLLLLAGYLRM--RLLSGfEEKNKKAYEES--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1051 SHITS-SIQGLATIHAYNKRQEFLHRYQELLDDNQ-------------------APFFLFTCAMRWLAVrldLISIALIT 1110
Cdd:cd18578 193 SKIASeAVSNIRTVASLTLEDYFLEKYEEALEEPLkkglrralisglgfglsqsLTFFAYALAFWYGGR---LVANGEYT 269
|
....*....
gi 16758936 1111 TTGLMIVLM 1119
Cdd:cd18578 270 FEQFFIVFM 278
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
578-757 |
6.74e-09 |
|
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: 56.60 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAIlgqmtllegsiavsgtfayvaqqawILNATLRDNILFGKEFDEERYNSV 657
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAI-------------------------GLALGGAQSATRRRSGVKAGCIVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 658 LNSCCLRpdlailpnsdLTEIGerganLSGGQRQRISLARAL----YSDRSIYILDDPLSALDAHVGNHIFNSAIRKRLK 733
Cdd:cd03227 66 AVSAELI----------FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK 130
|
170 180
....*....|....*....|....
gi 16758936 734 SKTVLFVTHQLQYLVDCDEVIFMK 757
Cdd:cd03227 131 GAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
858-1121 |
8.68e-09 |
|
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: 58.59 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 858 FLVIMVLFMLNVGSTAFSTWWLSYWIKQgsgnstVFEGNRSSVsdsmrdnpflqyyasIYALSMAVMLILkAIRGVV-FV 936
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDD------IFVEKDLEA---------------LLLVPLAIIGLF-LLRGLAsYL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 937 KGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVG-MIagV 1009
Cdd:cd18552 59 QTYLmayvgqRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGvLF--Y 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1010 FPWFL----VAVGPLLILfsvlhiVSRVLIRELKRLDNITQSpFLSHITS----SIQGLATIHAYNKRQEFLHRYQELLD 1081
Cdd:cd18552 137 LDWKLtliaLVVLPLAAL------PIRRIGKRLRKISRRSQE-SMGDLTSvlqeTLSGIRVVKAFGAEDYEIKRFRKANE 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16758936 1082 DNqapfflFTCAMRWLAVRlDLIS--IALITTTGLMIVLMHG 1121
Cdd:cd18552 210 RL------RRLSMKIARAR-ALSSplMELLGAIAIALVLWYG 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
686-799 |
1.03e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 686 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKRLKSKTVlFVTHQLQyLVD--CDEVIFMKEGCI 761
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNlmMDLQQELGLSYV-FISHDLS-VVEhiADEVMVMYLGRC 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 16758936 762 TERGTHEelmnlngdyaTIFNN-------LLLGETPPVEINSKKE 799
Cdd:PRK11308 234 VEKGTKE----------QIFNNprhpytqALLSATPRLNPDDRRE 268
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
569-772 |
1.08e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.60 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 569 AGSMRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVAQQAWI 634
Cdd:PRK10895 10 AKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 635 LNA-TLRDNIL--------FGKEFDEERYNSVL---NSCCLRPDLailpnsdlteigerGANLSGGQRQRISLARALYSD 702
Cdd:PRK10895 90 FRRlSVYDNLMavlqirddLSAEQREDRANELMeefHIEHLRDSM--------------GQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 703 RSIYILD------DPLSALD-AHVGNHIFNSAIrkrlkskTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK10895 156 PKFILLDepfagvDPISVIDiKRIIEHLRDSGL-------GVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
576-772 |
1.18e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.82 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWILN---------------ATLR 640
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFG-------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPL 712
Cdd:PRK13647 99 DDVAFGpvnmgldKDEVERRVEEALKAV------------RMWDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 713 SALDAHVGNHIFnsAIRKRL--KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK13647 167 AYLDPRGQETLM--EILDRLhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
580-771 |
1.41e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI--------------AVSGTFAYVAQQ----AWILNATLRD 641
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkdisprspldAVKKGMAYITESrrdnGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGKEFDEERYNSVLN----------SCCLRPDLAILPNSDLTEIGErganLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:PRK09700 361 NMAISRSLKDGGYKGAMGlfhevdeqrtAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 712 LSALDAHVGNHIFnSAIRKRLKS-KTVLFVTHQL-QYLVDCDEVIFMKEGCITE------RGTHEELM 771
Cdd:PRK09700 437 TRGIDVGAKAEIY-KVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQiltnrdDMSEEEIM 503
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1192-1411 |
1.74e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG----LAD 1264
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1265 LRSKLTIIPQEP--VLFSGTVRSNL----DPFNQYTEEQIWDALERTHM----KECIAQLPLKLesevmengdnfSVGER 1334
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMvglaDEFWEKSPFEL-----------SGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1335 QLLCIARALLRHCKILILDEATAAMDTETDLLIQ---ETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1410
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
.
gi 16758936 1411 S 1411
Cdd:PRK13643 229 S 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
565-740 |
1.92e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 565 KQIHAGSMRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWILNA------- 637
Cdd:PRK11614 9 DKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 --------TLRDNILFGKEF-DEERYNSVLNSCC-LRPDLailpnsdLTEIGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK11614 88 grrvfsrmTVEENLAMGGFFaERDQFQERIKWVYeLFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190
....*....|....*....|....*....|...
gi 16758936 708 LDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFV 740
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1200-1388 |
2.28e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.36 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1200 RYREN--LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV---RISDIGLADLRS-KLTIIP 1273
Cdd:PRK11629 14 RYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1274 QEPVLfsgtvrsnLDPFNqyteeqiwdALERTHMKECIAQLPLK--------------LESEVMENGDNFSVGERQLLCI 1339
Cdd:PRK11629 94 QFHHL--------LPDFT---------ALENVAMPLLIGKKKPAeinsralemlaavgLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1340 ARALLRHCKILILDEATAAMDTET-----DLLIQETIRE--AFADCTM-LTIAHRLH 1388
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNadsifQLLGELNRLQgtAFLVVTHdLQLAKRMS 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
554-749 |
2.33e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 554 DERPSPEEEEGKQIHAGSmRLQRTLYNIDLEIEEGKL-----VGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYV 628
Cdd:PRK13409 327 EERPPRDESERETLVEYP-DLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 629 AQ----------QAWILNATlrdnilfgKEFDEERYNSVLnsccLRP-DLAILPNSDLTEigerganLSGGQRQRISLAR 697
Cdd:PRK13409 406 PQyikpdydgtvEDLLRSIT--------DDLGSSYYKSEI----IKPlQLERLLDKNVKD-------LSGGELQRVAIAA 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 698 ALYSDRSIYILDDPLSALDAH----VGnhifnSAIRK--RLKSKTVLFVTHQLqYLVD 749
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEqrlaVA-----KAIRRiaEEREATALVVDHDI-YMID 518
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
554-749 |
2.65e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.26 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 554 DERPSPEEEEGKQIHAGSmRLQRTLYNIDLEIEEGKL-----VGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYV 628
Cdd:COG1245 328 EVHAPRREKEEETLVEYP-DLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 629 AQqaWILN-------ATLRDNIlfGKEFDEERYNSVLnsccLRPdLAI--LPNSDLTEigerganLSGGQRQRISLARAL 699
Cdd:COG1245 407 PQ--YISPdydgtveEFLRSAN--TDDFGSSYYKTEI----IKP-LGLekLLDKNVKD-------LSGGELQRVAIAACL 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 700 YSDRSIYILDDPLSALDA----HVGnhifnSAIRK--RLKSKTVLFVTHQLqYLVD 749
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVeqrlAVA-----KAIRRfaENRGKTAMVVDHDI-YLID 520
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
572-749 |
3.21e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 56.26 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 572 MRLQRTLYNIDLEIEEGKL-----VGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-TFAYVAQQAWILNATLRDNILF 645
Cdd:cd03237 4 PTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 646 GKEfdeeryNSVLNSCCLRPDlaILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDahVGNHIF 724
Cdd:cd03237 84 SIT------KDFYTHPYFKTE--IAKPLQIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLM 153
|
170 180 190
....*....|....*....|....*....|.
gi 16758936 725 NSAIRKRL---KSKTVLFVTHQL---QYLVD 749
Cdd:cd03237 154 ASKVIRRFaenNEKTAFVVEHDIimiDYLAD 184
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1208-1422 |
3.28e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.19 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFR----LVELSGGCIKIDGVRISDIGLaDLRSKLTI--IPQEPVLFSG 1281
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 -TVRSNLDPFNQYTEeqiwdaLERTHMKECIAQLplkLE----SEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:COG1137 93 lTVEDNILAVLELRK------LSKKEREERLEEL---LEefgiTHLRKSkAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1356 TAAMD--TETDllIQETIREafadctmLT---IA-----HRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR-FY 1422
Cdd:COG1137 164 FAGVDpiAVAD--IQKIIRH-------LKergIGvlitdHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPLVRkVY 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
917-1121 |
3.39e-08 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 56.72 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 917 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 992
Cdd:cd18576 38 IALLLLGLFLLQAVfsffRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 993 IQNVILVFFCVGMIAGVFP---WFLVAVGPLLILFSVlhIVSRVlIREL--KRLDNITQSpfLSHITSSIQGLATIHAYN 1067
Cdd:cd18576 118 LRQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAV--LFGRR-IRKLskKVQDELAEA--NTIVEETLQGIRVVKAFT 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1068 KRQEFLHRYQELLDDnqapffLFTCAMRWLAVRLDLIS-IALITTTGLMIVLMHG 1121
Cdd:cd18576 193 REDYEIERYRKALER------VVKLALKRARIRALFSSfIIFLLFGAIVAVLWYG 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1211-1415 |
3.62e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1211 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRlVELSGGCIKIDGVRISDIGLADL----RSKL-----TIIPQEPvlfsg 1281
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLspreRRKLvghnvSMIFQEP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 tvRSNLDPfNQYTEEQIWDAL----------ERTHMK-----ECIAQLPLKLESEVMENGD-NFSVGERQLLCIARALLR 1345
Cdd:PRK15093 99 --QSCLDP-SERVGRQLMQNIpgwtykgrwwQRFGWRkrraiELLHRVGIKDHKDAMRSFPyELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1346 HCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1207-1405 |
3.93e-08 |
|
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: 55.74 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1207 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDG--------------VRISDIGLADL--RS 1267
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGqprkpdqfqkcvayVRQDDILLPGLtvRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1268 KLTIIPQ--EPVLFSGTVRSNLDPFnqyteeqiwdalerTHMKECiAQLPLKleSEVMENgdnFSVGERQLLCIARALLR 1345
Cdd:cd03234 101 TLTYTAIlrLPRKSSDAIRKKRVED--------------VLLRDL-ALTRIG--GNLVKG---ISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1346 HCKILILDEATAAMDTETDLLIQETIREafadctmltIAHRLHTVLGS------------DRIMVLAQGQVV 1405
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQ---------LARRNRIVILTihqprsdlfrlfDRILLLSSGEIV 223
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
922-1027 |
4.28e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 56.29 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 922 AVMLILKAIRGVV-FVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ 994
Cdd:cd18542 43 LLILGVALLRGVFrYLQGYLaekasqKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVR 122
|
90 100 110
....*....|....*....|....*....|....*.
gi 16758936 995 NVILVFFCVGMIAGVFP---WFLVAVGPLLILFSVL 1027
Cdd:cd18542 123 AVLLFIGALIIMFSINWkltLISLAIIPFIALFSYV 158
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
576-759 |
4.90e-08 |
|
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: 57.53 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSIAVSGT--------------FAYVAQQ-AWILNAT 638
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFGKEFDEE----RYNSVLNSC-CLRPDLAILPNSDLTEIGERGanlsGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:TIGR02633 95 VAENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16758936 714 ALDAHVGNHIFNsaIRKRLKSKTV--LFVTHQLQYL-VDCDEVIFMKEG 759
Cdd:TIGR02633 171 SLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVkAVCDTICVIRDG 217
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
918-1162 |
5.02e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 56.36 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 918 ALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVI 997
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 998 LVFFCVGMIAGVFPWFLVAV---GPLLILFSVLH--IVSRVLIRELKRLDNITqspflSHITSSIQGLATIHAYNK---- 1068
Cdd:cd18563 130 MIIGIGVVLFSLNWKLALLVlipVPLVVWGSYFFwkKIRRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAFGQekre 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1069 RQEFLHRYQELLDDNqapfflftcamrwlaVRLDLIS------IALITTTGLMIV-------LMHGQIP----SAYagla 1131
Cdd:cd18563 205 IKRFDEANQELLDAN---------------IRAEKLWatffplLTFLTSLGTLIVwyfggrqVLSGTMTlgtlVAF---- 265
|
250 260 270
....*....|....*....|....*....|.
gi 16758936 1132 ISYAVQLTGLFQFTVRLASETEARFTSVERI 1162
Cdd:cd18563 266 LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
580-770 |
5.52e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFAYV--AQQAWI------LN----ATLRDNIL 644
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvRFRSPrdAQAAGIaiihqeLNlvpnLSVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKE------FD----EERYNSVLNscclRPDLAILPNsdlTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG1129 102 LGREprrgglIDwramRRRARELLA----RLGLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 715 LDAHVGNHIFNsAIRkRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:COG1129 171 LTEREVERLFR-IIR-RLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1208-1416 |
6.72e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLADLRSKLTIIPQEpvlfSGTVRSN 1286
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQH----VGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LDPFNQYTeeqiwdALE---------RTHMKECIAQLPLKLESEVMENGDN------FSVGERQLLCIARALLRHCKILI 1351
Cdd:PRK11264 94 FNLFPHRT------VLEniiegpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 1352 LDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1416
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
910-1123 |
7.00e-08 |
|
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: 55.88 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 910 LQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQA 989
Cdd:cd18541 39 LLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 990 EMFIQNVILVFFCVGMIAGVFPWF-LVAVGPLLILFsvlhIVSRVLIRELKRLDNITQSPFlSHITSSIQ----GLATIH 1064
Cdd:cd18541 119 LYLVDALFLGVLVLVMMFTISPKLtLIALLPLPLLA----LLVYRLGKKIHKRFRKVQEAF-SDLSDRVQesfsGIRVIK 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1065 AYNKRQEFLHRYQELLDDNQApfflftcamRWLA-VRLD---LISIALITTTGLMIVL-------MHGQI 1123
Cdd:cd18541 194 AFVQEEAEIERFDKLNEEYVE---------KNLRlARVDalfFPLIGLLIGLSFLIVLwyggrlvIRGTI 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
580-772 |
7.42e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.01 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAV----------SGTFAYVAQQAWILNA------------ 637
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFkelrrrvsmvfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 ---------TLRDNILFG-------KEFDEERYNSVLNSCCLRPDLAilpnsdlteigERGA-NLSGGQRQRISLARALY 700
Cdd:PRK13631 124 fpeyqlfkdTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYL-----------ERSPfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 701 SDRSIYILDDPLSALDAHvGNHIFNSAIRKRLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT-HEELMN 772
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTpYEIFTD 266
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
578-754 |
7.49e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.31 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQ--MTLLEGSIAVSGTFAYVAQQAWI----------LNATLRDN--- 642
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPalARRLHLKKEQPGNHDRIEGLEHIdkvividqspIGRTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ---------ILF-----GKEFDEE----RYN-----SVLNSCC------------LRPDLAILPNSDLTEI--GERGANL 685
Cdd:cd03271 91 ytgvfdeirELFcevckGKRYNREtlevRYKgksiaDVLDMTVeealeffenipkIARKLQTLCDVGLGYIklGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 686 SGGQRQRISLARALySDRS----IYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVI 754
Cdd:cd03271 171 SGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1410 |
8.26e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.63 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKpKEKI-GIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDigLADLRSKLTIIPQEPVLFSGTVRSN 1286
Cdd:PRK13631 41 ALNNISYTFE-KNKIyFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD--KKNNHELITNPYSKKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LDPFNQYTEEQIW-DALERTHMKECIAQLPLKLES--------EVMENGDNF--------SVGERQLLCIARALLRHCKI 1349
Cdd:PRK13631 118 VSMVFQFPEYQLFkDTIEKDIMFGPVALGVKKSEAkklakfylNKMGLDDSYlerspfglSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1350 LILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1410
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
578-763 |
9.66e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGqmtLLEGSiavSGTFAYVAQQAWILN----ATLR-DNILFgkefdee 652
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGS---SGEVSLVGQPLHQMDeearAKLRaKHVGF------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 653 rynsVLNSCCLRPDLAILPNSDLTEI----------------------GER----GANLSGGQRQRISLARALYSDRSIY 706
Cdd:PRK10584 93 ----VFQSFMLIPTLNALENVELPALlrgessrqsrngakalleqlglGKRldhlPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 707 ILDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSlNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1208-1411 |
1.06e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSK-LTIIPQEPVLFSgtv 1283
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRREhFGFIFQRYHLLS--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 rsnldpfnQYTEEQ------IWDALERTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:PRK10535 100 --------HLTAAQnvevpaVYAGLERKQRLLRAQELlqRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1356 TAAMDT---ETDLLIQETIREafADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEfDTPS 1411
Cdd:PRK10535 172 TGALDShsgEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPA 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
685-770 |
1.27e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 56.23 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLKSKT---VLFVTHQLQyLVD--CDEVIFMKEG 759
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIL--DLLKDLQRELgmaLLLITHDLG-VVRrfADRVAVMRQG 233
|
90
....*....|.
gi 16758936 760 CITERGTHEEL 770
Cdd:COG4172 234 EIVEQGPTAEL 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1209-1409 |
1.31e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG------GCIKIDG--VRISDIGLAdLRSKLTIIPQE----P 1276
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL------LKILSGnyqpdaGSILIDGqeMRFASTTAA-LAAGVAIIYQElhlvP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1277 VLfsgTVRSNLdpfnqyteeqiwdalerthmkeCIAQLPLK--------LESEVMEN----GDNF---------SVGERQ 1335
Cdd:PRK11288 93 EM---TVAENL----------------------YLGQLPHKggivnrrlLNYEAREQlehlGVDIdpdtplkylSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1336 LLCIARALLRHCKILILDEATAAMDT-ETDLLIQeTIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQVVE-FDT 1409
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAEGRvILYVSHRMEEIFAlCDAITVFKDGRYVAtFDD 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
576-759 |
1.51e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVAQQAWILNA-TLR 640
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGKE----------FDEERYNSVLNSCCLRPDLAILPNsdlteigERGANLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:PRK09700 99 ENLYIGRHltkkvcgvniIDWREMRVRAAMMLLRVGLKVDLD-------EKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 711 PLSALDAHVGNHIFnsAIRKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:PRK09700 172 PTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1190-1416 |
1.64e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1190 GEITFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSL------------GMALFRLVELSGGCIKIDG 1254
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMiqltngliisetGQTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1255 VRisdiglaDLRSKLTIIPQEP--VLFSGTVRSNL--DPFNQYTEEQiwDALERTHMKECIAQLPlklESEVMENGDNFS 1330
Cdd:PRK13645 85 VK-------RLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKKVPELLKLVQLP---EDYVKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1331 VGERQLLCIARALLRHCKILILDEATAAMDT--ETDL--LIQETIREAFADCTMLTiaHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgEEDFinLFERLNKEYKKRIIMVT--HNMDQVLRiADEVIVMHEGKVI 230
|
250
....*....|.
gi 16758936 1406 EFDTPSVLLSN 1416
Cdd:PRK13645 231 SIGSPFEIFSN 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
575-743 |
1.76e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT------------FAYVAQQAWI-LNATLRD 641
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqLCFVGHRSGInPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGKEFDEEryNSVLNSCCLRPDLAILpnsdlteIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 721
Cdd:PRK13540 94 NCLYDIHFSPG--AVGITELCRLFSLEHL-------IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 16758936 722 HIFNSAIRKRLKSKTVLFVTHQ 743
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1208-1408 |
1.76e-07 |
|
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: 53.41 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLTIIPQEPVLFSG-TVRSN 1286
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYPHmTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LD---PFNQYTEEQIwdaLERTHMkecIAQLpLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTEt 1363
Cdd:cd03301 93 IAfglKLRKVPKDEI---DERVRE---VAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1364 dlliqetIREAfadctMLTIAHRLHTVLG----------------SDRIMVLAQGQVVEFD 1408
Cdd:cd03301 165 -------LRVQ-----MRAELKRLQQRLGtttiyvthdqveamtmADRIAVMNDGQIQQIG 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
576-759 |
1.92e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) 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: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.02 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMT--LLEGSIAVSG-----TFA----YVAQQ-AWILNATLRDNI 643
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGrpldkNFQrstgYVEQQdVHSPNLTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 644 LFgkefdeerynsvlnSCCLRpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 723
Cdd:cd03232 101 RF--------------SALLR-------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16758936 724 FNsAIRKRLKS-KTVLFVTHQ-----LQYLvdcDEVIFMKEG 759
Cdd:cd03232 148 VR-FLKKLADSgQAILCTIHQpsasiFEKF---DRLLLLKRG 185
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
899-1082 |
1.97e-07 |
|
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: 54.44 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 899 SVSDSMRDNPFLQYYASIYALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRF 974
Cdd:cd18573 25 VASKESGDIEIFGLSLKTFALALLGVFVVGAAanfgRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 975 SKDMDEVdvrlpfqAEMFIQNV-------ILVFFCVGMIAGVFPwFLVAVGplLILFSVLHIVSRVLIRELKRLDNITQS 1047
Cdd:cd18573 105 SSDTSVV-------GKSLTQNLsdglrslVSGVGGIGMMLYISP-KLTLVM--LLVVPPIAVGAVFYGRYVRKLSKQVQD 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 16758936 1048 PfLSHITSS----IQGLATIHAYNKRQEFLHRYQELLDD 1082
Cdd:cd18573 175 A-LADATKVaeerLSNIRTVRAFAAERKEVERYAKKVDE 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
576-772 |
2.01e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYN-IDLEIEEGKLVGICGSVGSGKTSLI------------SAILGQMTLLE-GSIAVSGTFAYVAQQawiLNA---- 637
Cdd:PRK10575 24 RTLLHpLSLTFPAGKVTGLIGHNGSGKSTLLkmlgrhqppsegEILLDAQPLESwSSKAFARKVAYLPQQ---LPAaegm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 TLRDNIL------------FGKEfDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRSI 705
Cdd:PRK10575 101 TVRELVAigrypwhgalgrFGAA-DREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 706 YILDDPLSALD-AHvgnHIFNSAIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:PRK10575 169 LLLDEPTSALDiAH---QVDVLALVHRLSQErglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
561-768 |
2.25e-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: 52.91 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 561 EEEGKQIhagsmrlqrtLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQM--TLLEGSIAVSGTFayvaqqawILNAT 638
Cdd:cd03217 9 SVGGKEI----------LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGED--------ITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDNILFG--KEFDE-ERYNSVLNSCCLRpdlailpnsdltEIGErgaNLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:cd03217 71 PEERARLGifLAFQYpPEIPGVKNADFLR------------YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 716 DAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYL--VDCDEVIFMKEGCITERGTHE 768
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1185-1417 |
2.46e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.64 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1185 DWPQEGEITFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD 1264
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1265 LRSKLTIIPQE-PVLFSGTVRSnLDPFNQYTeeqiWD-------ALERTHMKECIAQLPLK-LESEVMengDNFSVGERQ 1335
Cdd:PRK10575 83 FARKVAYLPQQlPAAEGMTVRE-LVAIGRYP----WHgalgrfgAADREKVEEAISLVGLKpLAHRLV---DSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1336 LLCIARALLRHCKILILDEATAAMD----TETDLLIQETIREafadcTMLTIAHRLHTVLGS----DRIMVLAQGQVVEF 1407
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQE-----RGLTVIAVLHDINMAarycDYLVALRGGEMIAQ 229
|
250
....*....|
gi 16758936 1408 DTPSVLLSND 1417
Cdd:PRK10575 230 GTPAELMRGE 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1191-1421 |
2.70e-07 |
|
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: 53.11 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1191 EITFENAEMRYrENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLT 1270
Cdd:cd03296 2 SIEVRNVSKRF-GDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1271 IIPQEPVLFSG-TVRSNL-----------DPFNQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 1338
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1339 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
....*.
gi 16758936 1416 NDSSRF 1421
Cdd:cd03296 227 HPASPF 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
575-770 |
2.94e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-FAYVAQ---------QAWIL--NATLRDN 642
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPPyqrpinmmfQSYALfpHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFGKEFDEERYNSVLNSCClrpdlAILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDahvgn 721
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALD----- 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 722 hifnSAIRKRLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK11607 182 ----KKLRDRMQLEvvdilervgvTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1207-1416 |
3.15e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1207 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLadlrskltiiPQEPVLFSGTVRS- 1285
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GL----------PGHQIARMGVVRTf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 -NLDPFNQYTE-EQIWDALERtHMKECIAQLPLKL------ESEVMENG-----------------DNFSVGERQLLCIA 1340
Cdd:PRK11300 87 qHVRLFREMTViENLLVAQHQ-QLKTGLFSGLLKTpafrraESEALDRAatwlervgllehanrqaGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1341 RALLRHCKILILDEATAAMD-TETDLLiQETI---REAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1415
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNpKETKEL-DELIaelRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRN 243
|
.
gi 16758936 1416 N 1416
Cdd:PRK11300 244 N 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1212-1405 |
6.48e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLTIIP----QEPVLFSGTVRSN 1286
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LD--------PFNQYteeqIWDALERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:PRK11288 352 INisarrhhlRAGCL----INNRWEAENADRFIRSLNIKtpsREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1356 TAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1405
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
576-805 |
6.61e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVAQQAWIL-NATLR 640
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFG---KEFDEERYNSVLN--SCCLRPDLAilpnsdlteigerGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 716 DAHVGNHIFnSAIRKrLKSKTV--LFVTHQLQYLVD-CDEVIFMKEGCITergtheelmnLNGDYATIFNNLLLGETPPV 792
Cdd:PRK15439 172 TPAETERLF-SRIRE-LLAQGVgiVFISHKLPEIRQlADRISVMRDGTIA----------LSGKTADLSTDDIIQAITPA 239
|
250
....*....|...
gi 16758936 793 EINskKEASGSQK 805
Cdd:PRK15439 240 ARE--KSLSASQK 250
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
575-754 |
6.77e-07 |
|
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: 51.87 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSL----------------ISA----ILGQM-----TLLEG-SIAVS------ 622
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAyarqFLGQMdkpdvDSIEGlSPAIAidqktt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 623 -----GTFAYVAQqawiLNATLRdnILFGKEFDEERYNSvlnscclrpdlailpnsdLTEIG------ERGAN-LSGGQR 690
Cdd:cd03270 88 srnprSTVGTVTE----IYDYLR--LLFARVGIRERLGF------------------LVDVGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 691 QRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVI 754
Cdd:cd03270 144 QRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVI 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1206-1406 |
7.35e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1206 PLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----VELSGGCIKIDGVRISdigLADLRSKLT-IIPQEPvlfs 1280
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVA---PCALRGRKIaTIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1281 gtvRSNLDPFNQYteeqiwdaleRTHMKECI---------AQLPLKLESEVMENGD--------NFSVGERQLLCIARAL 1343
Cdd:PRK10418 89 ---RSAFNPLHTM----------HTHARETClalgkpaddATLTAALEAVGLENAArvlklypfEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1344 LRHCKILILDEATaamdTETDLLIQETIREAFADCT------MLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:PRK10418 156 LCEAPFIIADEPT----TDLDVVAQARILDLLESIVqkralgMLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
915-1082 |
7.48e-07 |
|
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: 52.51 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 915 SIYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmDEVDVRlpfqaE 990
Cdd:cd18555 42 NVLGIGILILFLLYGlfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAN---SNVYIR-----Q 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 991 MFIQNVI--------LVFFCVGMIagVFPWFL----VAVGPLLILFSVLhivSRVLIRELKRLDNITQSPFLSHITSSIQ 1058
Cdd:cd18555 114 ILSNQVIsliidlllLVIYLIYML--YYSPLLtlivLLLGLLIVLLLLL---TRKKIKKLNQEEIVAQTKVQSYLTETLY 188
|
170 180
....*....|....*....|....
gi 16758936 1059 GLATIHAYNKRQEFLHRYQELLDD 1082
Cdd:cd18555 189 GIETIKSLGSEKNIYKKWENLFKK 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
580-771 |
9.77e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT----FAY--VAQQAWIL--NATLRDNILFGKEFDE 651
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhYASkeVARRIGLLaqNATTPGDITVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 652 ERY-NSVLNSCCLRPD----LAILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD-AHVGNHIF 724
Cdd:PRK10253 105 GRYpHQPLFTRWRKEDeeavTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16758936 725 NSAIRKRLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELM 771
Cdd:PRK10253 185 LLSELNREKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
578-784 |
9.87e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWiLNATLR--DNI--------LFGK 647
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSG-LNGQLTgiENIelkglmmgLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 648 EFDEerynsvlnscclrpdlaILPNS-DLTEIG----ERGANLSGGQRQRISLARALYSDRSIYILDDPLSaldahVGNH 722
Cdd:PRK13545 119 KIKE-----------------IIPEIiEFADIGkfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 723 IFNSAIRKRL-----KSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNL 784
Cdd:PRK13545 177 TFTKKCLDKMnefkeQGKTIFFISHSLsQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQM 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1187-1386 |
1.01e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1187 PQEGEITFENAEMRYrENLPLV-------LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVelsGGCIKIDGVRISd 1259
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSL----FRIL---GELWPVYGGRLT- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1260 iglADLRSKLTIIPQEPVLFSGTVRSNL---DPFNQYTE--------EQIWDALERTHMkeciaqlpLKLE---SEVMEN 1325
Cdd:TIGR00954 511 ---KPAKGKLFYVPQRPYMTLGTLRDQIiypDSSEDMKRrglsdkdlEQILDNVQLTHI--------LEREggwSAVQDW 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1326 GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREafADCTMLTIAHR 1386
Cdd:TIGR00954 580 MDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
576-776 |
1.06e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTFAYVAQQAWILNA---------------TLR 640
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgvaiiyqelhlvpemTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGK------EFDEERYNSVLNSCCLRPDLAILPNSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:PRK11288 98 ENLYLGQlphkggIVNRRLLNYEAREQLEHLGVDIDPDTPL-------KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758936 715 LDAHVGNHIFnSAIRK-RLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITErgTHEELMNLNGD 776
Cdd:PRK11288 171 LSAREIEQLF-RVIRElRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDMAQVDRD 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1208-1363 |
1.11e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKI-DGVRISDIGLADLRSKLTI--IPQEPVL-FSGTV 1283
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTL--------------LRImAGVDKDFNGEARPQPGIKVgyLPQEPQLdPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 RSN-----------LDPFNQ----YTEEQI-WDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFSVG 1332
Cdd:TIGR03719 86 RENveegvaeikdaLDRFNEisakYAEPDAdFDKLaaEQAELQEIIDAADAwDLDSQLeiaMDalrcpPWDadvtKLSGG 165
|
170 180 190
....*....|....*....|....*....|.
gi 16758936 1333 ERQLLCIARALLRHCKILILDEATAAMDTET 1363
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1208-1373 |
1.24e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 51.17 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVEL-SGGCIKIDG------VRISDIGLADLRSKLTIIPQE----P 1276
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEMpRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1277 VLfsgTVRSNL--DPFN------QYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCK 1348
Cdd:PRK11124 96 HL---TVQQNLieAPCRvlglskDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQRVAIARALMMEPQ 161
|
170 180
....*....|....*....|....*
gi 16758936 1349 ILILDEATAAMDTETDLLIQETIRE 1373
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
576-753 |
1.37e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSL---ISAILGQMTLlEGSIAVSG---TFAYV--AQQAWIL----------NA 637
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTY-EGEIIFEGeelQASNIrdTERAGIAiihqelalvkEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 638 TLRDNILFGKE---FDEERYNSVLNSC--CLRP-DLAILPNsdlTEIGergaNLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:PRK13549 98 SVLENIFLGNEitpGGIMDYDAMYLRAqkLLAQlKLDINPA---TPVG----NLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16758936 712 LSALDAHVGNHIFNsaIRKRLKSKTV--LFVTHQLqylvdcDEV 753
Cdd:PRK13549 171 TASLTESETAVLLD--IIRDLKAHGIacIYISHKL------NEV 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
581-770 |
1.38e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 581 IDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAvsgtfayvaqqaWiLNATLRDniLFGKEFDEER------Y 654
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA------------W-LGKDLLG--MKDDEWRAVRsdiqmiF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 655 NSVLNSccLRPDLAI-----------LPNSDLTEIGERGANL------------------SGGQRQRISLARALYSDRSI 705
Cdd:PRK15079 105 QDPLAS--LNPRMTIgeiiaeplrtyHPKLSRQEVKDRVKAMmlkvgllpnlinryphefSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 706 YILDDPLSALDAHVGNHIFNsaIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 770
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVN--LLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1209-1406 |
1.46e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDG--VRISDIGLADlRSKLTIIPQE--- 1275
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKV-----LSGvyphgsyeGEILFDGevCRFKDIRDSE-ALGIVIIHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1276 -PVLfsgTVRSNLDPFNQYTEEQI--WDALERtHMKECIAQLPLKlesevmENGD----NFSVGERQLLCIARALLRHCK 1348
Cdd:NF040905 90 iPYL---SIAENIFLGNERAKRGVidWNETNR-RARELLAKVGLD------ESPDtlvtDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1349 ILILDEATAAMDtETD---LLiqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1406
Cdd:NF040905 160 LLILDEPTAALN-EEDsaaLL--DLLLELKAqGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
941-1121 |
1.65e-06 |
|
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: 51.33 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 941 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVFPWFLVAVGPL 1020
Cdd:cd18575 66 RVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLF-ITSPKLTLLVLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1021 LILFSVLHIVsrVLIRELKRLDNITQSPFL---SHITSSIQGLATIHAYNKRQEFLHRYQELLDDNqapfflFTCAMRWL 1097
Cdd:cd18575 145 VIPLVVLPII--LFGRRVRRLSRASQDRLAdlsAFAEETLSAIKTVQAFTREDAERQRFATAVEAA------FAAALRRI 216
|
170 180
....*....|....*....|....*
gi 16758936 1098 AVRLDLISIA-LITTTGLMIVLMHG 1121
Cdd:cd18575 217 RARALLTALViFLVFGAIVFVLWLG 241
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1209-1424 |
1.99e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmaLFRLVEL--SGGCIKIDGVRISDIGLADL---RSKLTiiPQEPVLFsgtv 1283
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTL---LARMAGLlpGSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 rsNLDPFnQY---------TEEQIWDALERthmkecIAQLpLKLESEVMENGDNFSVGERQ-------LLCIARALLRHC 1347
Cdd:PRK03695 83 --AMPVF-QYltlhqpdktRTEAVASALNE------VAEA-LGLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1348 KILILDEATAAMD----TETDLLIQETIREAFAdctMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTP-SVLLSNDSSRF 1421
Cdd:PRK03695 153 QLLLLDEPMNSLDvaqqAALDRLLSELCQQGIA---VVMSSHDLnHTLRHADRVWLLKQGKLLASGRRdEVLTPENLAQV 229
|
...
gi 16758936 1422 YAM 1424
Cdd:PRK03695 230 FGV 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1208-1406 |
2.02e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.55 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK--------LTIIP--- 1273
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1274 -QEPVLFSGTVRSNLDpfnQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1352
Cdd:PRK10584 105 aLENVELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1353 DEATAAMDTET-----DLLIQETIREAfadCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1406
Cdd:PRK10584 171 DEPTGNLDRQTgdkiaDLLFSLNREHG---TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
581-770 |
2.24e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.61 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 581 IDLEIEEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAVSGTFAY--------VAQQAWIL--------NATL 639
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpieVRREVGMVfqypnpfpHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNILFG----------KEFDEeRYNSVLNSCCLRPDLAilpnsdlTEIGERGANLSGGQRQRISLARALYSDRSIYILD 709
Cdd:PRK14267 103 YDNVAIGvklnglvkskKELDE-RVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 710 DPLSALDAhVGNHIFNSAIRKRLKSKTVLFVTHQ-LQYLVDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK14267 175 EPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
559-759 |
2.57e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 559 PEEEEGKQIHagsmrlqR------TLYNIDLeIEEGKLVGICGSVGSGKTSLISAILGQMT------------------- 613
Cdd:PRK13409 72 PEELEEEPVH-------RygvngfKLYGLPI-PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyeeepswdevlkrf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 614 -----------LLEGSIAVSGTFAYVAQQAWILNATLRDnILfgKEFDE----ERYNSVLNscclrpdlailpnsdLTEI 678
Cdd:PRK13409 144 rgtelqnyfkkLYNGEIKVVHKPQYVDLIPKVFKGKVRE-LL--KKVDErgklDEVVERLG---------------LENI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 679 GERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDahVGNHIfNSA--IRKRLKSKTVLFVTHQ---LQYLVDCDE 752
Cdd:PRK13409 206 LDRDiSELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRL-NVArlIRELAEGKYVLVVEHDlavLDYLADNVH 282
|
....*..
gi 16758936 753 VIFMKEG 759
Cdd:PRK13409 283 IAYGEPG 289
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
580-755 |
2.59e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAVSGTFAY---------------VAQQAWILNATL 639
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYapdvdpvevrrrigmVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNILFGK-------EFDE--ERynsvlnscCLRPdlAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:PRK14243 108 YDNIAYGAringykgDMDElvER--------SLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 711 PLSALDAhvgnhIFNSAIR---KRLKSK-TVLFVTHQLQ------------------------YLVDCD--EVIF 755
Cdd:PRK14243 178 PCSALDP-----ISTLRIEelmHELKEQyTIIIVTHNMQqaarvsdmtaffnveltegggrygYLVEFDrtEKIF 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1188-1405 |
2.62e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.65 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1188 QEGEITFENAEMRYReNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiglADLRS 1267
Cdd:PRK15056 3 QQAGIVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1268 KLTIIPQE-------PVLFSGTVRSN-------LDPFNQYTEEQIWDALERTHMkeciaqlplkLESEVMENGDnFSVGE 1333
Cdd:PRK15056 79 LVAYVPQSeevdwsfPVLVEDVVMMGryghmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1334 RQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVV 1405
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
580-753 |
2.80e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFA--YVAQQAWI--------L--NATLRDNIL 644
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvRIRspRDAIALGIgmvhqhfmLvpNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 FGKEfdeerynsvlNSCCLRPDLAILpNSDLTEIGER-G---------ANLSGGQRQRISLARALYSDRSIYILDDPLSA 714
Cdd:COG3845 103 LGLE----------PTKGGRLDRKAA-RARIRELSERyGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16758936 715 LDAHVGNHIFnsAIRKRLKS--KTVLFVTHQLqylvdcDEV 753
Cdd:COG3845 172 LTPQEADELF--EILRRLAAegKSIIFITHKL------REV 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1417 |
2.96e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEP--VLFSGTVRS 1285
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1286 NL--DPFN-----QYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 1358
Cdd:PRK13652 99 DIafGPINlgldeETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1359 MDTETdllIQETIR--EAFADCTMLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSND 1417
Cdd:PRK13652 168 LDPQG---VKELIDflNDLPETYGMTVIFSTHQLdlvpEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
575-754 |
3.10e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.11 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGTF--AYVAQQAWiLNATLRDNIlfgkefdeE 652
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLY-LDTTLPLTV--------N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 653 RYNSvlnsccLRPDLA---ILPNSDLTE----IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD--AHVGNHI 723
Cdd:PRK09544 88 RFLR------LRPGTKkedILPALKRVQaghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQVALYD 161
|
170 180 190
....*....|....*....|....*....|..
gi 16758936 724 FNSAIRKRLKSkTVLFVTHQLQY-LVDCDEVI 754
Cdd:PRK09544 162 LIDQLRRELDC-AVLMVSHDLHLvMAKTDEVL 192
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
580-772 |
3.39e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.03 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVAQQAWIL-NATLRDNIL 644
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFrKLTVEDNIL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 645 -------FGKEFDEERYNSVLNscclrpDLailpnsDLTEIGE-RGANLSGGQRQRISLARALYSDRSIYILD------D 710
Cdd:COG1137 101 avlelrkLSKKEREERLEELLE------EF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDepfagvD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 711 PLSALDahvgnhifnsaIRK---RLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 772
Cdd:COG1137 169 PIAVAD-----------IQKiirHLKERgiGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1209-1403 |
4.24e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS--------DIGLADLRSKLTIIPQEPV--- 1277
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQLTIaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1278 LFSGtvRSNLDPFNQ------YTEEqiwDALerthmkecIAQLPLKLESEVMEnGDnFSVGERQLLCIARALLRHCKILI 1351
Cdd:PRK10762 100 IFLG--REFVNRFGRidwkkmYAEA---DKL--------LARLNLRFSSDKLV-GE-LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1352 LDEATAAM-DTETDLLIQeTIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 1403
Cdd:PRK10762 165 MDEPTDALtDTETESLFR-VIRELKSqGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
922-1162 |
4.36e-06 |
|
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: 50.17 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 922 AVMLILKAIRGVVFV-------KGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdVRLPFQAEMFIQ 994
Cdd:cd18543 43 LLLLALGVAEAVLSFlrrylagRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 995 NVILVFFCVGMIAGVFPWF-LVAVGPLLILFsvlhIVSRVLIRELKRLDNITQS---PFLSHITSSIQGLATIHAYNKRQ 1070
Cdd:cd18543 122 NLLTLVVGLVVMLVLSPPLaLVALASLPPLV----LVARRFRRRYFPASRRAQDqagDLATVVEESVTGIRVVKAFGRER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1071 EFLHRYQELLDDnqapffLFTCAMRwlAVRLDLISIALITT---TGLMIVL-------MHGQIpSAYAGLA-ISYAVQLT 1139
Cdd:cd18543 198 RELDRFEAAARR------LRATRLR--AARLRARFWPLLEAlpeLGLAAVLalggwlvANGSL-TLGTLVAfSAYLTMLV 268
|
250 260
....*....|....*....|...
gi 16758936 1140 GLFQFTVRLASETEARFTSVERI 1162
Cdd:cd18543 269 WPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1209-1404 |
4.68e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI--------GLA---DLRSKLTIIPQEPV 1277
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaneainhGFAlvtEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1278 LFSGTVrSNLDpfnQYTEEqiWDALERTHMKE----CIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILD 1353
Cdd:PRK10982 344 GFNSLI-SNIR---NYKNK--VGLLDNSRMKSdtqwVIDSMRVKTPGHRTQIG-SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1354 EATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 1404
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
563-759 |
5.12e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 563 EGKQIHAGSMRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMT--LLEGSIAVSG------TFAYVA---QQ 631
Cdd:PLN03140 882 EMKEQGVTEDRLQ-LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkqeTFARISgycEQ 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 632 AWILN--ATLRDNILFG------KEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGanLSGGQRQRISLARALYSDR 703
Cdd:PLN03140 961 NDIHSpqVTVRESLIYSaflrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 704 SIYILDDPLSALDAHVGNhIFNSAIRKRLKS-KTVLFVTHQ--LQYLVDCDEVIFMKEG 759
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAA-IVMRTVRNTVDTgRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
576-759 |
5.46e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 576 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVAQQA-WILNATLR 640
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 641 DNILFGkefdeeRYNS----VLNSCCLRPDLAILPNSDL-TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK10982 92 DNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIdIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758936 716 DAHVGNHIFNsaIRKRLKSK--TVLFVTHQLQYLVD-CDEVIFMKEG 759
Cdd:PRK10982 166 TEKEVNHLFT--IIRKLKERgcGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
575-759 |
6.47e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 575 QRTLYN-IDLEIEEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSIAVSG---------TFAYVAQQAWIL-NATLRD 641
Cdd:PLN03211 80 ERTILNgVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNrkptkqilkRTGFVTQDDILYpHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILF------GKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16758936 716 DAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLV--DCDEVIFMKEG 759
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEG 283
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
887-1082 |
6.66e-06 |
|
Six-transmembrane helical domain 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: 350002 [Multi-domain] Cd Length: 312 Bit Score: 49.97 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 887 SGNSTVFEGNRSSVSDS------MRDNpfLQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMK 960
Cdd:cd18558 31 NGGMTNITGNSSGLNSSagpfekLEEE--MTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 961 FFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLLILFSVL--HIVSR 1032
Cdd:cd18558 109 WFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGtgFIIGFIRG---WkltlVILAISPVLGLSAVVwaKILSG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758936 1033 VLIRELKRLDNITQSPflshiTSSIQGLATIHAYNKRQEFLHRYQELLDD 1082
Cdd:cd18558 186 FTDKEKKAYAKAGAVA-----EEVLEAFRTVIAFGGQQKEETRYAQNLEI 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1212-1406 |
6.83e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL---------RSKLTIIPQEP------ 1276
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdglrm 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1277 -VLFSGTVRSNLDPF--NQYTE--EQIWDALERTHMKEC-IAQLPlklesevmengDNFSVGERQLLCIARALLRHCKIL 1350
Cdd:PRK11701 105 qVSAGGNIGERLMAVgaRHYGDirATAGDWLERVEIDAArIDDLP-----------TTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1351 ILDEATAAMDTET-----DLLiQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVE 1406
Cdd:PRK11701 174 FMDEPTGGLDVSVqarllDLL-RGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
566-770 |
6.83e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.14 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 566 QIHAGSMRLQ----RTLYNIDLEIEEGKLVGICGSVGSGKTSLISaILGQMTLLEGSIAVSGTFAYVAQQAW-------- 633
Cdd:PRK14247 3 KIEIRDLKVSfgqvEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFkmdvielr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 634 ------------ILNATLRDNILFGKEFD---------EERYNSVLNSCCLRPDLAilpnsdlTEIGERGANLSGGQRQR 692
Cdd:PRK14247 82 rrvqmvfqipnpIPNLSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 693 ISLARALYSDRSIYILDDPLSALDAHvgnhifNSAIRKRL-----KSKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGT 766
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPE------NTAKIESLflelkKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGP 228
|
....
gi 16758936 767 HEEL 770
Cdd:PRK14247 229 TREV 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
573-744 |
7.22e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 573 RLQRTLYnidleieEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-----TFAYVAQ------QAWIL--NATL 639
Cdd:TIGR01257 948 RLNITFY-------ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietNLDAVRQslgmcpQHNILfhHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNILF-----GKEFDEERYNSVlnscclrpdlAILPNSDLT-EIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 713
Cdd:TIGR01257 1021 AEHILFyaqlkGRSWEEAQLEME----------AMLEDTGLHhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190
....*....|....*....|....*....|.
gi 16758936 714 ALDAHVGNHIFNSAIRKRlKSKTVLFVTHQL 744
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHM 1120
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
685-770 |
7.67e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN-SAIRKRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 762
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
|
....*...
gi 16758936 763 ERGTHEEL 770
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
930-1041 |
9.25e-06 |
|
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: 49.23 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 930 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF-FCVGMIag 1008
Cdd:cd18784 55 IRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIgVIVFMF-- 132
|
90 100 110
....*....|....*....|....*....|...
gi 16758936 1009 VFPWFLVAVgpLLILFSVLHIVSRVLIRELKRL 1041
Cdd:cd18784 133 KLSWQLSLV--TLIGLPLIAIVSKVYGDYYKKL 163
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
581-763 |
1.05e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 581 IDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGtfAYVAQQAW-----ILNATLRDNILF-------GKE 648
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPedyrkLFSAVFTDFHLFdqllgpeGKP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 649 FDEERYNSVLNSCCLrpdlailpNSDLTEIGERGAN--LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNS 726
Cdd:PRK10522 420 ANPALVEKWLERLKM--------AHKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 16758936 727 AIRKRLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITE 763
Cdd:PRK10522 491 VLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1211-1422 |
1.48e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.01 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1211 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsDIGLADLRSKLTIIPQEPVLFSGTVRSNLDPF 1290
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1291 NQYTEEQIWD--ALERTHMKECIAqlplkLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQ 1368
Cdd:TIGR01257 1027 YAQLKGRSWEeaQLEMEAMLEDTG-----LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1369 ETIREAFADCTMLTIAHRLHT--VLGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFY 1422
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEadLLG-DRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
686-770 |
1.53e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 686 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI----------FNSAIrkrlksktvLFVTHQLQYLVD-CDEVI 754
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQImtllnelkreFNTAI---------IMITHDLGVVAGiCDKVL 233
|
90
....*....|....*.
gi 16758936 755 FMKEGCITERGTHEEL 770
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
918-1119 |
1.61e-05 |
|
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: 48.35 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 918 ALSMAVML--ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFsKDMDEVDVRLPFQAEMFIQN 995
Cdd:cd18566 47 GVVIAILLesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 996 VILVFFCVGMIAgVFPWFLVAV----GPLLILFSVL-HIVSRVLIRELKRLDNITQspflSHITSSIQGLATIHAYNKRQ 1070
Cdd:cd18566 126 LPFVLIFLGLIW-YLGGKLVLVplvlLGLFVLVAILlGPILRRALKERSRADERRQ----NFLIETLTGIHTIKAMAMEP 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16758936 1071 EFLHRYQELLDDnqapfflftCAMRWLAVRlDLISIALITTTGLMIVLM 1119
Cdd:cd18566 201 QMLRRYERLQAN---------AAYAGFKVA-KINAVAQTLGQLFSQVSM 239
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
580-770 |
1.71e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQM----TLLEGSIAVSGTFAYVAQQAWILNATLRDNilfgkefDEERYN 655
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRGRKIATIMQN-------PRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 656 SVLN-------SCCLR---PDLAILPNSdLTEIG----ERGANL-----SGGQRQRISLARALYSDRSIYILDDPLSALD 716
Cdd:PRK10418 94 PLHTmhthareTCLALgkpADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 717 AHVGNHIFN---SAIRKRlkSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 770
Cdd:PRK10418 173 VVAQARILDlleSIVQKR--ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
685-772 |
1.78e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKRLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITE 763
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*....
gi 16758936 764 RGTHEELMN 772
Cdd:PRK14271 243 EGPTEQLFS 251
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
578-770 |
2.06e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.15 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-TFAYVAQQawILNATLRDNILFGKEFDEERYNS 656
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYDKKS--LLEVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 657 VLNSCCLRPDLAILPNSD--------LTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 722
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEvekrvkeaLKAVGMEGfenkppHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16758936 723 IFNSAIRKRLKSKTVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13639 176 IMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
685-772 |
2.18e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKRLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGC 760
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL--QLLRELQQElnmGLLFITHNLSIVRKlADRVAVMQNGR 234
|
90
....*....|..
gi 16758936 761 ITERGTHEELMN 772
Cdd:PRK15134 235 CVEQNRAATLFS 246
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
568-718 |
2.40e-05 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 47.43 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 568 HAGSMRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVS---------------------GTFA 626
Cdd:COG4778 18 LQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 627 YVAQqawILNATLRDNIL-----------FGKEFDEERYNSVLNSCCLRPDLAILPNsdlteigergANLSGGQRQRISL 695
Cdd:COG4778 97 YVSQ---FLRVIPRVSALdvvaepllergVDREEARARARELLARLNLPERLWDLPP----------ATFSGGEQQRVNI 163
|
170 180
....*....|....*....|...
gi 16758936 696 ARALYSDRSIYILDDPLSALDAH 718
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
931-1082 |
2.44e-05 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain] Cd Length: 289 Bit Score: 47.72 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 931 RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILvffCVGMIAgvf 1010
Cdd:cd18590 56 RGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK---TLGMLG--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1011 pwFLVAVGPLLILFSVLHIVSRVLI--------RELKR--LDNITQSPFLshITSSIQGLATIHAYNKRQEFLHRYQELL 1080
Cdd:cd18590 130 --FMLSLSWQLTLLTLIEMPLTAIAqkvyntyhQKLSQavQDSIAKAGEL--AREAVSSIRTVRSFKAEEEEACRYSEAL 205
|
..
gi 16758936 1081 DD 1082
Cdd:cd18590 206 ER 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
580-762 |
2.48e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT--------------FAYVAQ----QAWILNATLRD 641
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDMSVAE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 642 NILFGkEFDEERYNS--VLNSCCLRpDLA--------ILPNSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILDDP 711
Cdd:COG3845 356 NLILG-RYRRPPFSRggFLDRKAIR-AFAeelieefdVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 712 LSALDahVGNhIfnSAIRKRL-----KSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 762
Cdd:COG3845 430 TRGLD--VGA-I--EFIHQRLlelrdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
584-749 |
2.87e-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: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 584 EIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-TFAYVAQQAwilnatlrdnilfgkefdeerynsvlnscc 662
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQYI------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 663 lrpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKRLK--SKTVLFV 740
Cdd:cd03222 71 ---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEegKKTALVV 128
|
170
....*....|..
gi 16758936 741 THQL---QYLVD 749
Cdd:cd03222 129 EHDLavlDYLSD 140
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1208-1433 |
3.10e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 47.29 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLTIIPQEPVLFSGTVRSNL 1287
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1288 DPFNQYTEEQI---W-----DALERTHMKECIAQLPLklesevmENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1359
Cdd:PRK10253 102 VARGRYPHQPLftrWrkedeEAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1360 DT--ETDL--LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND-SSRFYAM-CAAAENKV 1432
Cdd:PRK10253 175 DIshQIDLleLLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAElIERIYGLrCMIIDDPV 252
|
.
gi 16758936 1433 A 1433
Cdd:PRK10253 253 A 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1212-1408 |
3.47e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1212 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLTIIPQEP----VLFSGTVRSN 1286
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 -----LDPFNqYTEEQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1361
Cdd:PRK10762 351 msltaLRYFS-RAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758936 1362 ETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 1408
Cdd:PRK10762 429 GAKKEIYQLINQFKAEgLSIILVSSEMPEVLGmSDRILVMHEGRISgEFT 478
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
578-770 |
3.65e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.11 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG-------------TFAYVAQQA--WILNATLRDN 642
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFGK---EFDEE----RYNSVLNSCCLRPDLAILPNsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:PRK13652 100 IAFGPinlGLDEEtvahRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 716 DAHVGNHI--FNSAIRKRLkSKTVLFVTHQLQYLVDCDEVIF-MKEGCITERGTHEEL 770
Cdd:PRK13652 169 DPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEI 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
580-773 |
3.69e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 580 NIDLEIEEGKLVGICGSVGSGKTSLISAILGQ--------MTLLEG--------SIAVSGTFAYVA----QQAWILNATL 639
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygrnisgTVFKDGkevdvstvSDAIDAGLAYVTedrkGYGLNLIDDI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNI----LFG----------KEFDE-ERYnsvlnscclRPDLAILPNSDLTEIGergaNLSGGQRQRISLARALYSDRS 704
Cdd:NF040905 358 KRNItlanLGKvsrrgvidenEEIKVaEEY---------RKKMNIKTPSVFQKVG----NLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 705 IYILDDPLSALDahVGN--HIFnsAIRKRLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEELMNL 773
Cdd:NF040905 425 VLILDEPTRGID--VGAkyEIY--TIINELAAegKGVIVISSELPELLGmCDRIYVMNEGRITgelprEEASQERIMRL 499
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
680-777 |
5.98e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 680 ERGAN-LSGGQRQRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVLFVTHQLQYLVDCDEVIFM 756
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100 110
....*....|....*....|....*....|.
gi 16758936 757 KE------GCITERGTHEELMN----LNGDY 777
Cdd:TIGR00630 563 GPgagehgGEVVASGTPEEILAnpdsLTGQY 593
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
559-749 |
7.06e-05 |
|
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: 47.47 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 559 PEEEEGKQIH---AGSMRLqrtlYNIDlEIEEGKLVGICGSVGSGKTSLISAILGQMT---------------------- 613
Cdd:COG1245 72 PEELEEDPVHrygENGFRL----YGLP-VPKKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkrfrgt 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 614 --------LLEGSIAVSGTFAYVAQQAWILNATLRDnILfgKEFDE----ERYNSVLNscclrpdlailpnsdLTEIGER 681
Cdd:COG1245 147 elqdyfkkLANGEIKVAHKPQYVDLIPKVFKGTVRE-LL--EKVDErgklDELAEKLG---------------LENILDR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 682 G-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDahvgnhifnsaIRKRLKS-----------KTVLFVTHQ---LQY 746
Cdd:COG1245 209 DiSELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-----------IYQRLNVarlirelaeegKYVLVVEHDlaiLDY 277
|
...
gi 16758936 747 LVD 749
Cdd:COG1245 278 LAD 280
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1224-1408 |
7.07e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1224 IVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLTIIPQEPVLFSG-TVRSNL----DPFNQYT 1294
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgICLPPEKRRIGYVFQDARLFPHyKVRGNLrygmAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1295 EEQIWDALERTHMkecIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDT--ETDLL--IQET 1370
Cdd:PRK11144 109 FDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprKRELLpyLERL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 16758936 1371 IREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1408
Cdd:PRK11144 175 ARE--INIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1213-1362 |
7.65e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1213 SFTIKPKEKIGIVGRTGSGKSSlgmaLFRLveLSG------GCIKIDGVRISDIGlADLRSKLtiipqepvLFSG----- 1281
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTS----LLRI--LAGlarpdaGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 ----TVRSNLDpFNQ-----YTEEQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILIL 1352
Cdd:PRK13538 86 ktelTALENLR-FYQrlhgpGDDEALWEALAQVGLAG-FEDVPVR----------QLSAGQQRRVALARLWLTRAPLWIL 153
|
170
....*....|
gi 16758936 1353 DEATAAMDTE 1362
Cdd:PRK13538 154 DEPFTAIDKQ 163
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
918-1078 |
7.95e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 46.35 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 918 ALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpFQAEMFI 993
Cdd:cd18564 57 AAALVGIALLRGLasyaGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD---LLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 994 QNVILVFFCVGMIAGVF--PWFL----VAVGPLLiLFSVLHIVSRvlIRELKRldniTQSPFLSHITS----SIQGLATI 1063
Cdd:cd18564 134 PLLTNLLTLVGMLGVMFwlDWQLaliaLAVAPLL-LLAARRFSRR--IKEASR----EQRRREGALASvaqeSLSAIRVV 206
|
170
....*....|....*
gi 16758936 1064 HAYNKRQEFLHRYQE 1078
Cdd:cd18564 207 QAFGREEHEERRFAR 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
566-716 |
8.15e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 566 QIHAGSMRLQ--RTLYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSgtFAYVA-----QQAWILNAT 638
Cdd:PRK10938 5 QISQGTFRLSdtKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--FSHITrlsfeQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 639 LRDN---IL------FGKEFDEERYNSVL-NSCCLRpdLA-ILPNSDLteIGERGANLSGGQRQRISLARALYSDRSIYI 707
Cdd:PRK10938 83 WQRNntdMLspgeddTGRTTAEIIQDEVKdPARCEQ--LAqQFGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
....*....
gi 16758936 708 LDDPLSALD 716
Cdd:PRK10938 159 LDEPFDGLD 167
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1192-1360 |
8.19e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.28 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1192 ITFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS------DIgl 1262
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1263 ADLRSKLTIIPQ--EPVLFSGTVRSNL----DPFNQYTEEQIWDALERTHM----KECIAQLPLKLesevmengdnfSVG 1332
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALvgisESLFEKNPFEL-----------SGG 149
|
170 180
....*....|....*....|....*...
gi 16758936 1333 ERQLLCIARALLRHCKILILDEATAAMD 1360
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1172-1404 |
8.40e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 45.82 E-value: 8.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1172 EAPARIKNKAPphdwpqegeITFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcik 1251
Cdd:PRK11247 2 MNTARLNQGTP---------LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1252 idGVRISDIGLADLRSKLTIIPQEPVLF-------------SGTVRsnldpfnqyteEQIWDALERTHMKECIAQLPLKL 1318
Cdd:PRK11247 68 --ELLAGTAPLAEAREDTRLMFQDARLLpwkkvidnvglglKGQWR-----------DAALQALAAVGLADRANEWPAAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1319 esevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI-----REAFadcTMLTIAHRL-HTVLG 1392
Cdd:PRK11247 135 -----------SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDVsEAVAM 200
|
250
....*....|..
gi 16758936 1393 SDRIMVLAQGQV 1404
Cdd:PRK11247 201 ADRVLLIEEGKI 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1208-1360 |
8.67e-05 |
|
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: 45.18 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLveLSGGCIKIDG-VRISDIGLADLRSKLtiipQEPVLFSG----- 1281
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTL----LRI--LAGLSPPLAGrVLLNGGPLDFQRDSI----ARGLLYLGhapgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1282 ----TVRSNLDPFNQY-TEEQIWDALERTHMK----ECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILIL 1352
Cdd:cd03231 85 kttlSVLENLRFWHADhSDEQVEEALARVGLNgfedRPVAQL---------------SAGQQRRVALARLLLSGRPLWIL 149
|
....*...
gi 16758936 1353 DEATAAMD 1360
Cdd:cd03231 150 DEPTTALD 157
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1208-1410 |
8.75e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.48 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDIGlADLRSKLTIIpQEPVLFSG-T 1282
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV----LRLIagfeTPDSGRIMLDGQDITHVP-AENRHVNTVF-QSYALFPHmT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1283 VRSNLdPF--------NQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDE 1354
Cdd:PRK09452 103 VFENV-AFglrmqktpAAEITPRVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1355 ATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEFDTP 1410
Cdd:PRK09452 171 SLSALDYKLRKQMQNELK-------------ALQRKLGitfvfvthdqeealtmSDRIVVMRDGRIEQDGTP 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
578-759 |
1.21e-04 |
|
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: 44.95 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQmtlLEGSIAVSGTFAYVAQQAWILNATLRDNILFGKEfdEERYNSV 657
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSE--EDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 658 LN-------SCCLRPDLAIlpnsdlteigeRGanLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSaIR- 729
Cdd:cd03233 98 LTvretldfALRCKGNEFV-----------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC-IRt 163
|
170 180 190
....*....|....*....|....*....|...
gi 16758936 730 --KRLKSKTVLFVTHQLQYLVDC-DEVIFMKEG 759
Cdd:cd03233 164 maDVLKTTTFVSLYQASDEIYDLfDKVLVLYEG 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1218-1410 |
1.25e-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: 43.90 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1218 PKEKIGIVGRTGSGKSSLGMALFR-LVELSGGCIKIDGVRISDIGLADLRSKLtiipqepvlfsgtvrsnldpfnqytee 1296
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1297 qiwdalerthmkeciaqlplkleseVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR---- 1372
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16758936 1373 ---EAFADCTMLTIAHRLHTVLgsDRIMVLAQGQVVEFDTP 1410
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
578-770 |
1.25e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.61 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 578 LYNIDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSGT-FAYVAQQawILNatLRDNI-LFGKEFDEERYN 655
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKG--LMK--LRESVgMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 656 -SVLNSCCLRPDLAILPNSDLTEIGERGAN--------------LSGGQRQRISLARALYSDRSIYILDDPLSALDAhVG 720
Cdd:PRK13636 98 aSVYQDVSFGAVNLKLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP-MG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 721 nhifNSAIRKRLKSK------TVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 770
Cdd:PRK13636 177 ----VSEIMKLLVEMqkelglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1191-1417 |
1.69e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.46 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1191 EITFENAEMRYRENLPLVLK---KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI--------------KID 1253
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1254 GVRISDI----------GLADLRSKLTIIPQ--EPVLFSGTVRSNL--DPFNQYTEEQiwDALERThmKECIAQLPLKlE 1319
Cdd:PRK13651 82 KVLEKLViqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRA--AKYIELVGLD-E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1320 SEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD---TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDR 1395
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGK--TIILVTHDLDNVLEwTKR 234
|
250 260
....*....|....*....|...
gi 16758936 1396 IMVLAQGQVV-EFDTPSVLLSND 1417
Cdd:PRK13651 235 TIFFKDGKIIkDGDTYDILSDNK 257
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1208-1417 |
1.71e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLG--MALFRLVELSGGCIKIDGVRISDIGlADLRSKLTIIP--QEPVLFSGTv 1283
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSkvIAGHPAYKILEGDILFKGESILDLE-PEERAHLGIFLafQYPIEIPGV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1284 rSNLD----PFNQYTEEQIWDALERTHMKECIAQ-LPL-KLESEVMENGDN--FSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:CHL00131 100 -SNADflrlAYNSKRKFQGLPELDPLEFLEIINEkLKLvGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAILDET 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758936 1356 TAAMDTETDLLIQETIREAFADCT-MLTIAH--RLHTVLGSDRIMVLAQGQVVEfdTPSVLLSND 1417
Cdd:CHL00131 179 DSGLDIDALKIIAEGINKLMTSENsIILITHyqRLLDYIKPDYVHVMQNGKIIK--TGDAELAKE 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
586-749 |
1.74e-04 |
|
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: 45.05 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 586 EEGKLVGICGSVGSGKTSLISAILGQMT------------------------------LLEGSIAVSGTFAYVAQQAWIL 635
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKpnlgkfddppdwdeildefrgselqnyftkLLEGDVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 636 NATLRDNIlfgKEFDEeryNSVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSAL 715
Cdd:cd03236 104 KGKVGELL---KKKDE---RGKLDELVDQLELRHVLDRNIDQ-------LSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16758936 716 DahVGNHIfNSA--IRKRLK-SKTVLFVTHQ---LQYLVD 749
Cdd:cd03236 171 D--IKQRL-NAArlIRELAEdDNYVLVVEHDlavLDYLSD 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1208-1423 |
1.90e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.48 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDG--VRISDIGLADLrsklTIIPQEPVLF-- 1279
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDGedVTHRSIQQRDI----CMVFQSYALFph 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1280 ---SGTVRSNLDPFNQYTEEQiwdaleRTHMKECIAQLPLklesEVMENG--DNFSVGERQLLCIARALLRHCKILILDE 1354
Cdd:PRK11432 93 mslGENVGYGLKMLGVPKEER------KQRVKEALELVDL----AGFEDRyvDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758936 1355 ATAAMDTETDLLIQETIRE---AFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYA 1423
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRElqqQF-NITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQPASRFMA 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1208-1363 |
1.92e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.56 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDgVRISDIGladlrSKLTIIPQEPVlfsgtvrsnL 1287
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFG-----REASLIDAIGR---------K 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 1288 DPFNQYTEeqiwdALERTHMKEciAQLPLKLESEvmengdnFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1363
Cdd:COG2401 110 GDFKDAVE-----LLNAVGLSD--AVLWLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
946-1144 |
2.48e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 44.83 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 946 LHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNViLVFFCVGMIAGVFPWFLVAVG----PLL 1021
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNV-LTLVGVAIILFSINPKLALLTlipiPFL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1022 ILFSVLH-IVSRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYNKRQEFLHRYQELLDDnqapffLFTCAMRw 1096
Cdd:cd18778 154 ALGAWLYsKKVRPRYRKVRE--------ALGELNAllqdNLSGIREIQAFGREEEEAKRFEALSRR------YRKAQLR- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 1097 lAVRLDLI---SIALITTTGLMIVLMHGqipsayAGLAISYAVQLTGLFQF 1144
Cdd:cd18778 219 -AMKLWAIfhpLMEFLTSLGTVLVLGFG------GRLVLAGELTIGDLVAF 262
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1208-1421 |
2.68e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.07 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLTIIPQEPVLFSG-TVRSN 1286
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1287 LD-----------PFNQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEA 1355
Cdd:PRK10851 95 IAfgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758936 1356 TAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRF 1421
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREPATRF 232
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
929-1082 |
3.31e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 44.55 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 929 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDM----DEVDVRLpfqaEMFIQNVILVFFCVG 1004
Cdd:cd18780 60 FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTqvlqNAVTVNL----SMLLRYLVQIIGGLV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1005 MIaGVFPWFLVAVgpLLILFSVLHIVSRVLIRELKRLDNITQSPfLSHITS----SIQGLATIHAYNKRQEFLHRYQELL 1080
Cdd:cd18780 136 FM-FTTSWKLTLV--MLSVVPPLSIGAVIYGKYVRKLSKKFQDA-LAAASTvaeeSISNIRTVRSFAKETKEVSRYSEKI 211
|
..
gi 16758936 1081 DD 1082
Cdd:cd18780 212 NE 213
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
678-770 |
3.54e-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: 45.39 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 678 IGERGANLSGGQRQRISLARALY---SDRSIYILDDPLSALDAHVGNHIFNsaIRKRLKSK--TVLFVTHQLQYLVDCDE 752
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLE--VLQRLVDKgnTVVVIEHNLDVIKTADY 900
|
90 100
....*....|....*....|....
gi 16758936 753 VIFM------KEGCITERGTHEEL 770
Cdd:TIGR00630 901 IIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
941-981 |
4.80e-04 |
|
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: 43.69 E-value: 4.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 16758936 941 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV 981
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEF 112
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
581-769 |
5.06e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 581 IDLEIEEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAVSG---TFAYVA---------------QQAWILNATLRDN 642
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpiDIRSPRdairagimlcpedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 643 ILFGKefdeeRYNSVLNSCCLRP------------DLAILPNSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILDD 710
Cdd:PRK11288 352 INISA-----RRHHLRAGCLINNrweaenadrfirSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758936 711 PLSALDahVG------NHIFNSAIRKRlkskTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEE 769
Cdd:PRK11288 423 PTRGID--VGakheiyNVIYELAAQGV----AVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
686-744 |
6.67e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 6.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 686 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQL 744
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDlQRDFGIAYLFISHDM 524
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1208-1407 |
8.21e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.71 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1208 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG--GCIKIDGVRISDiglaDLRSKLTIIPQEPVLFSG-TVR 1284
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLDPFNQYTEEQIWDALERTHMKE-CIAQLPL-KLESEVMenGDNF----SVGERQLLCIARALLRHCKILILDEATAA 1358
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAEsVISELGLtKCENTII--GNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758936 1359 MDTETDL-LIQetireafadcTMLTIAHRLHTVLGS------------DRIMVLAQGQVVEF 1407
Cdd:PLN03211 237 LDATAAYrLVL----------TLGSLAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFF 288
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1209-1405 |
9.76e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 42.17 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1209 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD---LRSKLTIIPQEP-VLFSGTVR 1284
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1285 SNLD-PF------NQYTEEQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 1357
Cdd:PRK10908 98 DNVAiPLiiagasGDDIRRRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16758936 1358 AMDTEtdllIQETIREAFAD-----CTMLTIAHRLHTVLGSD-RIMVLAQGQVV 1405
Cdd:PRK10908 167 NLDDA----LSEGILRLFEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
918-1085 |
1.50e-03 |
|
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: 42.48 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 918 ALSMAVMLILKAIRGVVFVKGTLRASSR-LHD---ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemFI 993
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERlLYDlrlRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSE--------LL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 994 QN-----VILVFFCVGMIAGVF----PWFLVA--VGPLLILFSVL-HIVSRVLIRELKrlDNITQSpfLSHITSSIQGLA 1061
Cdd:cd18546 114 QTglvqlVVSLLTLVGIAVVLLvldpRLALVAlaALPPLALATRWfRRRSSRAYRRAR--ERIAAV--NADLQETLAGIR 189
|
170 180
....*....|....*....|....
gi 16758936 1062 TIHAYNKRQEFLHRYQELLDDNQA 1085
Cdd:cd18546 190 VVQAFRRERRNAERFAELSDDYRD 213
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1142-1407 |
1.51e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1142 FQFTVRLASETEARFTSVERINHYIKTLS-----LEAPAriknkapPHDWPQEGEITFENAEMRYRENlPLVLKKVSFTI 1216
Cdd:PLN03073 461 FRYNAKRASLVQSRIKALDRLGHVDAVVNdpdykFEFPT-------PDDRPGPPIISFSDASFGYPGG-PLLFKNLNFGI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1217 KPKEKIGIVGRTGSGKSS-LGMALFRLVELSGGCIKIDGVRISDI------GLaDLRSKltiipqePVLFSgtvrsnLDP 1289
Cdd:PLN03073 533 DLDSRIAMVGPNGIGKSTiLKLISGELQPSSGTVFRSAKVRMAVFsqhhvdGL-DLSSN-------PLLYM------MRC 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1290 FNQYTEEQIwdaleRTHMKECIAQLPLKLESEVMENGdnfsvGERQLLCIARALLRHCKILILDEATAAMDTE-TDLLIQ 1368
Cdd:PLN03073 599 FPGVPEQKL-----RAHLGSFGVTGNLALQPMYTLSG-----GQKSRVAFAKITFKKPHILLLDEPSNHLDLDaVEALIQ 668
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16758936 1369 ETireAFADCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF 1407
Cdd:PLN03073 669 GL---VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVTPF 705
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
270-466 |
1.60e-03 |
|
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: 42.15 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 270 EKSLGELINICSNDgqrmfeAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLG---SAVFILFYPAMMFVSRltaYFRRK 346
Cdd:cd07346 92 RNRTGDLMSRLTSD------VDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNwklTLVALLLLPLYVLILR---YFRRR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 347 CVAATDDRVQKM-------NEVLTYIKFIKMYAWVKAFSQCVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFS 419
Cdd:cd07346 163 IRKASREVRESLaelsaflQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16758936 420 V--HMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 466
Cdd:cd07346 243 YggYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
663-754 |
2.40e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 663 LRPDLAILPNSDLTEIG-ERG-ANLSGGQRQRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKRLKSKTVL 738
Cdd:PRK00635 453 LKSRLSILIDLGLPYLTpERAlATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVL 532
|
90
....*....|....*.
gi 16758936 739 FVTHQLQYLVDCDEVI 754
Cdd:PRK00635 533 LVEHDEQMISLADRII 548
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
640-770 |
2.42e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 640 RDNI-LFGKEFDEERYNSVLnscclRPDlAILPNSDLTEI-GERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 717
Cdd:NF000106 104 RENLyMIGR*LDLSRKDARA-----RAD-ELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 718 HVGNHIFNSAIRKRLKSKTVLFVThqlQYLVDCD----EVIFMKEGCITERGTHEEL 770
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTT---QYMEEAEqlahELTVIDRGRVIADGKVDEL 231
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
910-1041 |
2.53e-03 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 41.43 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 910 LQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMkffDTTPTGRILNRFSkDMDEVD------- 982
Cdd:cd18586 41 LLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPL---ESRPSGYWQQLLR-DLDTLRnfltgps 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758936 983 ----VRLPFqaemFIQNVILVFFcvgmIAGVFPWFLVAVGPLLILFSVL-HIVSRVLIRELKRL 1041
Cdd:cd18586 117 lfafFDLPW----APLFLAVIFL----IHPPLGWVALVGAPVLVGLAWLnHRATRKPLGEANEA 172
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
685-774 |
4.05e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 685 LSGGQRQRISLARALYS---DRSIYILDDPLSAL---DAHVGNHIFNSAIRkrlKSKTVLFVTHQLQYLVDCDEVIFM-- 756
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTH---QGHTVVIIEHNMHVVKVADYVLELgp 886
|
90 100
....*....|....*....|..
gi 16758936 757 ----KEGCITERGTHEELMNLN 774
Cdd:PRK00635 887 eggnLGGYLLASCSPEELIHLH 908
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
581-699 |
5.95e-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: 39.94 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 581 IDLE-IEEGKLVGICGSVGSGKTSLISAI----LGQMTLLEGSIAVSGTFAYVAQQAWILNATLRDNIL------FGKEF 649
Cdd:cd03279 20 IDFTgLDNNGLFLICGPTGAGKSTILDAItyalYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKyrversRGLDY 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 16758936 650 DEERyNSVLnscclrpdlaiLPNSDLTEIGERGA-NLSGGQRQRISLARAL 699
Cdd:cd03279 100 DQFT-RIVL-----------LPQGEFDRFLARPVsTLSGGETFLASLSLAL 138
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
945-1119 |
5.98e-03 |
|
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: 40.49 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 945 RLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVFPWFLVAVgpLLILF 1024
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMF-LLDWVLTLV--TLAVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 1025 SVLHIVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYNKRQEFLHRYQELLDDnqapffLFTCAMRwlAVRL 1101
Cdd:cd18551 147 PLAFLIILPLGRRIRKASKRAQdalGELSAALERALSAIRTVKASNAEERETKRGGEAAER------LYRAGLK--AAKI 218
|
170
....*....|....*...
gi 16758936 1102 DLIsIALITTTGLMIVLM 1119
Cdd:cd18551 219 EAL-IGPLMGLAVQLALL 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
651-718 |
7.28e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 7.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 651 EERYNSVLNSCCLRPDLAIlpnsdlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 718
Cdd:PLN03073 321 EARAASILAGLSFTPEMQV----------KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
685-770 |
7.50e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.11 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 685 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KRLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 762
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElQQKENMALVLITHDLALVAEaAHKIIVMYAGQVV 233
|
....*...
gi 16758936 763 ERGTHEEL 770
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
925-1080 |
7.80e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 40.24 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758936 925 LILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDmDEVDVRLPFQAEMFIQNVILVFFCVG 1004
Cdd:cd18568 56 ILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLG 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758936 1005 MIAgVFPWFL--VAVGpLLILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKRQEFLHRYQELL 1080
Cdd:cd18568 135 LMF-YYNLQLtlIVLA-FIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKF 210
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
911-971 |
9.42e-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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 39.81 E-value: 9.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758936 911 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRIL 971
Cdd:cd18783 36 QSYSTLYVLTIGVVIallfegILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLT 102
|
|
| |
