|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
79-1404 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 900.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 79 PVDNAGLFSCMTFSWLSPLARIAHKKgELLMEDVWSLSKHESSEVNCRRLERLWQEELHEVGPddaSLRRVVWTFCRTRL 158
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKR-PLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKP---WLLRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 159 ILSIVCLMITQLAGFSGPaFVVKHLLEYTQDTESNLQ---YSLLlvlglllteIVRSWSLALTWALNY-----RTGVRLR 230
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGP-LLLNLLLESMQNGEPAWIgyiYAFS---------IFVGVVLGVLCEAQYfqnvmRVGFRLR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 231 GAILTMAFKKILKLKNIKEK--SVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFLGSAVFILF 308
Cdd:PLN03130 374 STLVAAVFRKSLRLTHEGRKkfTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLM 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 309 YPAMMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSITVGVAPIV 388
Cdd:PLN03130 454 FPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSI 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 389 MVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIQKKPASPHI- 467
Cdd:PLN03130 534 PVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGLp 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 468 TIEMKNATLAWDSShsslqnspkltpktkkdkraargkkekvrqlqptehqavlaeqkghllldsDERPspeeeegkhth 547
Cdd:PLN03130 614 AISIKNGYFSWDSK---------------------------------------------------AERP----------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 548 lgnlrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQM-SLLEGSIAVNGTFAYVAQQAWILNATLRDNILFGK 626
Cdd:PLN03130 632 --------TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGS 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 627 EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSA 706
Cdd:PLN03130 704 PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKC 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 707 IQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLL-----LGETppVEINSKKE--- 778
Cdd:PLN03130 784 IKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG---PLFQKLMenagkMEEY--VEENGEEEddq 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 779 TSGSQKKTQ--DKCPKTGSVKKekavKPEEGQ--LVQMEEKGQGSVPWSVYGVYIQAAGGplaFLVILSLFMLNVGSTAF 854
Cdd:PLN03130 858 TSSKPVANGnaNNLKKDSSSKK----KSKEGKsvLIKQEERETGVVSWKVLERYKNALGG---AWVVMILFLCYVLTEVF 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 855 ---SNWWLSYWIKQGSGNTtvtqenrtsvsssmkDNPLmqYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELF 931
Cdd:PLN03130 931 rvsSSTWLSEWTDQGTPKT---------------HGPL--FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAML 993
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 932 RRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNV---ILVFFCVGMIAGVFPWflvAVGPLIILFSILH 1008
Cdd:PLN03130 994 GSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIfqlLSTFVLIGIVSTISLW---AIMPLLVLFYGAY 1070
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1009 IVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAMRWLAVRLDLISIAL 1088
Cdd:PLN03130 1071 LYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLM 1150
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1089 ITTTGLMIVLMHGQI--PPAYA---GLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKSPS 1163
Cdd:PLN03130 1151 IWLTASFAVMQNGRAenQAAFAstmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYID-LPSEAPLVIENNRPP 1229
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1164 SDWPQEGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLA 1243
Cdd:PLN03130 1230 PGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM 1309
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1244 DLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARAL 1323
Cdd:PLN03130 1310 DLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1324 LRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYA 1403
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
.
gi 1814750642 1404 M 1404
Cdd:PLN03130 1470 M 1470
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
79-1404 |
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: 889.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 79 PVDNAGLFSCMTFSWLSPLARIAHKKgELLMEDVWSLSKHESSEVNCRRLERLWQEELHEV---------GPDDA----- 144
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQ-PLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTrkqpvsavyGKKDPskpkg 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 145 ------------------------SLRRVVWTFCRTRLILSIVCLMITQLAGFSGPAfVVKHLLEYTQDTESNLQYSLLL 200
Cdd:TIGR00957 282 ssqldaneevealivksphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQ-ILSLLIRFVNDPMAPDWQGYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 201 VLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAFKKILKLKNIKEKS--VGELINLCSNDGQRMFEAAAVGSLLAG 278
Cdd:TIGR00957 361 TGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSstVGEIVNLMSVDAQRFMDLATYINMIWS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 279 GPVIAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQ 358
Cdd:TIGR00957 441 APLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLD 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 359 SVQKIREEERRMLEKAGYFQSITVGVAPIVMVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPFSVKSL 436
Cdd:TIGR00957 521 KVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVISSI 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 437 SEASVAVDRFKSLFLMEEV--HMIQKKPASP--HITIEMKNATLAWdsshsslqnspkltpktkkdkraargkkekVRQL 512
Cdd:TIGR00957 601 VQASVSLKRLRIFLSHEELepDSIERRTIKPgeGNSITVHNATFTW------------------------------ARDL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 513 QPTehqavlaeqkghllldsderpspeeeegkhthlgnlrlqrtLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMS 592
Cdd:TIGR00957 651 PPT-----------------------------------------LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 593 LLEGSIAVNGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRI 672
Cdd:TIGR00957 690 KVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRV 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 673 SLARALYSDRDIYILDDPLSALDAHVGNHIFNSAI--QKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELM 750
Cdd:TIGR00957 770 SLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 751 NLNGDYATIFNNLLLGE-----------------------------TPPVEINSKKETSGSQKKTQDKCPKTGSVKK-EK 800
Cdd:TIGR00957 850 QRDGAFAEFLRTYAPDEqqghledswtalvsgegkeakliengmlvTDVVGKQLQRQLSASSSDSGDQSRHHGSSAElQK 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 801 A-VKPEEGQLVQMEEKGQGSVPWSVYGVYIQAAGGPLAFLVILsLFMLNVGSTAFSNWWLSYWIKQGSGNTTvtQEN--- 876
Cdd:TIGR00957 930 AeAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIF-LFVCNHVSALASNYWLSLWTDDPMVNGT--QNNtsl 1006
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 877 RTSVSSSMKdnpLMQYYAsIYALSMAVMLilkairgvvfvkGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSK 956
Cdd:TIGR00957 1007 RLSVYGALG---ILQGFA-VFGYSMAVSI------------GGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSK 1070
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 957 DMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSS 1036
Cdd:TIGR00957 1071 ELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNET 1150
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1037 IQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAV 1116
Cdd:TIGR00957 1151 LLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSL 1230
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1117 QLTGLFQFTVRLASETEARFTSVERINHYIKTlSLEAPARIKNKSPSSDWPQEGEVTFENAEMRYQENLPLVLKKVSFTI 1196
Cdd:TIGR00957 1231 QVTFYLNWLVRMSSEMETNIVAVERLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTI 1309
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1197 KPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTED 1276
Cdd:TIGR00957 1310 HGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDE 1389
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1277 QIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFA 1356
Cdd:TIGR00957 1390 EVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE 1469
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|....*...
gi 1814750642 1357 DCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNdSSRFYAM 1404
Cdd:TIGR00957 1470 DCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ-RGIFYSM 1516
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
79-1404 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 854.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 79 PVDNAGLFSCMTFSWLSPLARIAHKKgELLMEDVWSLSKHESSEVNCRRLERLWQEELHEVGPddaSLRRVVWTFCRTRL 158
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRK-PITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKP---WLLRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 159 ILSIVCLMITQLAGFSGPAfVVKHLLEYTQDTES---NLQYSLLLVLGLLLTEIVRSWSLALTWalnyRTGVRLRGAILT 235
Cdd:PLN03232 304 WLGGIFKIGHDLSQFVGPV-ILSHLLQSMQEGDPawvGYVYAFLIFFGVTFGVLCESQYFQNVG----RVGFRLRSTLVA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 236 MAFKKILKLKNIKEKSV--GELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFLGSAVFILFYPAMM 313
Cdd:PLN03232 379 AIFHKSLRLTHEARKNFasGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 314 FVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKA---GYFQSITVGVAPIVMv 390
Cdd:PLN03232 459 LIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAqllSAFNSFILNSIPVVV- 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 391 iaSVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIQKKPASPHI-TI 469
Cdd:PLN03232 538 --TLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGApAI 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 470 EMKNATLAWDSshsslqnspkltpKTKKDkraargkkekvrqlqptehqavlaeqkghllldsderpspeeeegkhthlg 549
Cdd:PLN03232 616 SIKNGYFSWDS-------------KTSKP--------------------------------------------------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 nlrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLE-GSIAVNGTFAYVAQQAWILNATLRDNILFGKEF 628
Cdd:PLN03232 632 ------TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDF 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 629 DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQ 708
Cdd:PLN03232 706 ESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 709 KHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLL-----LGETPPVEINSKKETSGSQ 783
Cdd:PLN03232 786 DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SG---SLFKKLMenagkMDATQEVNTNDENILKLGP 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 784 KKTQD-KCPKTGSVKKEKAVKpeeGQLVQMEEKGQGSVPWSVYGVYIQAAGGPLAFLVILSLFMLNVGSTAFSNWWLSYW 862
Cdd:PLN03232 862 TVTIDvSERNLGSTKQGKRGR---SVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIW 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 863 IKQgsgnttvtqenrtsvSSSMKDNPlmQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFF 942
Cdd:PLN03232 939 TDQ---------------STPKSYSP--GFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFF 1001
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 943 DTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ---NVILVFFCVGMIAGVFPWflvAVGPLIILFSILHIVSRVLIRELK 1019
Cdd:PLN03232 1002 HTNPTGRVINRFSKDIGDIDRNVANLMNMFMNqlwQLLSTFALIGTVSTISLW---AIMPLLILFYAAYLYYQSTSREVR 1078
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1020 RLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLM 1099
Cdd:PLN03232 1079 RLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLR 1158
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1100 HGQIP-----PAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNKSPSSDWPQEGEVTF 1174
Cdd:PLN03232 1159 NGNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID-LPSEATAIIENNRPVSGWPSRGSIKF 1237
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1254
Cdd:PLN03232 1238 EDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ 1317
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1255 EPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1334
Cdd:PLN03232 1318 SPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1335 ATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 1404
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRM 1467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
211-1407 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 678.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 211 RSWSLALTWALNYRTGvrLRGAILTMAFKKILKLKNIKEKSVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYN 290
Cdd:PTZ00243 304 RFYYISIRCGLQYRSA--LNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 291 VIILGPTGFLGSAVFILFYPAMMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRM 370
Cdd:PTZ00243 382 SRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRY 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 371 LEKAGYFQSITVGV---APIVMvIASVvtFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFk 447
Cdd:PTZ00243 462 LRDVQLARVATSFVnnaTPTLM-IAVV--FTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRI- 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 448 SLFL------------MEEVHMIQKK-PASPHITIEMKNAtlawdSSHSSLqnsPKLTPKTKKDKRAARGK--------- 505
Cdd:PTZ00243 538 STFLecdnatcstvqdMEEYWREQREhSTACQLAAVLENV-----DVTAFV---PVKLPRAPKVKTSLLSRalrmlcceq 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 506 -KEKVRQLQPTEHQAVLAE-----QKGHLLLD-----SDERPSPEEEEGKHTHLGN----LRLQRTLYNIDLEIEEGKLV 570
Cdd:PTZ00243 610 cRPTKRHPSPSVVVEDTDYgspssASRHIVEGgtgggHEATPTSERSAKTPKMKTDdffeLEPKVLLRDVSVSVPRGKLT 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 571 GICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAILP 650
Cdd:PTZ00243 690 VVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLG 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 651 NSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLADCD 730
Cdd:PTZ00243 770 GGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRAD 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 731 EVIFMKEGCITERGTHEELMNlngdyATIFNNLLLGETPPVEI-NSKKETSGSQKKTQDKCPKT--GSVKKE-------- 799
Cdd:PTZ00243 850 YVVALGDGRVEFSGSSADFMR-----TSLYATLAAELKENKDSkEGDADAEVAEVDAAPGGAVDhePPVAKQegnaeggd 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 800 -KAVKPEEGQLVQMEEKGQGSVPWSVYGVYIQAAGGPLAFLVILSLFMLNVGSTAFSNWWLSYWikqgsgnttVTQENRT 878
Cdd:PTZ00243 925 gAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMW---------STRSFKL 995
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 879 SVSSsmkdnplmqyYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDM 958
Cdd:PTZ00243 996 SAAT----------YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDI 1065
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 959 DEVDVRLPfqaeMFIQNVILVFF--CVGMIAGVF--PWFLVAVGPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHIT 1034
Cdd:PTZ00243 1066 DILDNTLP----MSYLYLLQCLFsiCSSILVTSAsqPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLE 1141
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1035 SSIQGLATIHAYKKG----QEFLHRyqelLDNNQRPFFLFTCAMRWLAVRLDLIS------IALITTTGLMIVLMHGQIp 1104
Cdd:PTZ00243 1142 EALQGSATITAYGKAhlvmQEALRR----LDVVYSCSYLENVANRWLGVRVEFLSnivvtvIALIGVIGTMLRATSQEI- 1216
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1105 pAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEA-----------------------PARIKNKS 1161
Cdd:PTZ00243 1217 -GLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDmpeldeevdalerrtgmaadvtgTVVIEPAS 1295
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1162 PSSDWP---QEGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS 1238
Cdd:PTZ00243 1296 PTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG 1375
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1239 DIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLC 1318
Cdd:PTZ00243 1376 AYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMC 1455
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1319 IARALLRHCKILIL-DEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:PTZ00243 1456 MARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
1290
....*....|
gi 1814750642 1398 SSRFYAMFAA 1407
Cdd:PTZ00243 1536 QSIFHSMVEA 1545
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
834-1146 |
4.35e-178 |
|
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: 530.98 E-value: 4.35e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 834 GPLAFLVILSLFMLNVGSTAFSNWWLSYWIKQGSGNTTVTQENRTSVSSSMKDNPLMQYYASIYALSMAVMLILKAIRGV 913
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 914 VFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWF 993
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 994 LVAVGPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCA 1073
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1074 MRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1146
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
79-1409 |
2.02e-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: 514.46 E-value: 2.02e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 79 PVDNAGLFSCMTFSWLSPLARIAHKKgELLMEDVWSLSKHESSEVNCRRLERLWQEELHEVGPDDA---SLRRV-VWTFc 154
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQ-KLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKllnALRRCfFWRF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 155 rtrlILSIVCLMITQLAGFSGPAFVVKHLLEYTQDTESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAIL 234
Cdd:TIGR01271 83 ----VFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 235 TMAFKKILKLKNIK--EKSVGELINLCSNDGQRMFEAAAVGSLLAGGP--VIAILGMIYNviILGPTGFLGSAVFILFYP 310
Cdd:TIGR01271 159 SLIYKKTLKLSSRVldKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPlqVILLMGLIWE--LLEVNGFCGLGFLILLAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 311 AMMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAG---YFQSITVGVAPI 387
Cdd:TIGR01271 237 FQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAylrYFYSSAFFFSGF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 388 VMVIASVVTFSVHMTLgfdlTAAQAFTvvTVFNSMTFALKVT---PFSVKSLSEASVAVDRFKSLFLMEEVHMIQKKPAS 464
Cdd:TIGR01271 317 FVVFLSVVPYALIKGI----ILRRIFT--TISYCIVLRMTVTrqfPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 465 PHItiEMKNATLAWDSSHSSLqnspkltpktkkdkraargkKEKVRQlqptehqavlaeqkghlllDSDERPSPEEEEGk 544
Cdd:TIGR01271 391 TEV--EMVNVTASWDEGIGEL--------------------FEKIKQ-------------------NNKARKQPNGDDG- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 545 hTHLGNLRLQRT--LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWILNATLRDNI 622
Cdd:TIGR01271 429 -LFFSNFSLYVTpvLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNI 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHI 702
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 703 FNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIF-------------NNLLLGET- 768
Cdd:TIGR01271 588 FESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerRNSILTETl 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 769 ------------------------PPVEINSKKETS------GSQKK---TQDKCPKTGSVKKEKAV-KPEEGQ--LVQM 812
Cdd:TIGR01271 668 rrvsidgdstvfsgpetikqsfkqPPPEFAEKRKQSiilnpiASARKfsfVQMGPQKAQATTIEDAVrEPSERKfsLVPE 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 813 EEKGQGSVP----------------------------------------------------------------------- 821
Cdd:TIGR01271 748 DEQGEESLPrgnqyhhglqhqaqrrqsvlqlmthsnrgenrreqlqtsfrkkssitqqnelaseldiysrrlskdsvyei 827
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 822 -------------------------WSVYGVYIqAAGGPLAFLVILSL--FMLNVGSTAfsnwwLSYWIKQGSGNTTVTQ 874
Cdd:TIGR01271 828 seeineedlkecfaderenvfetttWNTYLRYI-TTNRNLVFVLIFCLviFLAEVAASL-----LGLWLITDNPSAPNYV 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 875 ENRTSVSSSMKD------NPLMQYYA-SIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPT 947
Cdd:TIGR01271 902 DQQHANASSPDVqkpviiTPTSAYYIfYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKA 981
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 948 GRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLIILFSILHIVSRVLIRELKRLDNITQS 1027
Cdd:TIGR01271 982 GRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARS 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1028 PFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHgQIPPAY 1107
Cdd:TIGR01271 1062 PIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTN-QDGEGE 1140
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1108 AGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI-------------KTLSLEAPARIKNKSPSSDWPQEGEVTF 1174
Cdd:TIGR01271 1141 VGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIdlpqeeprpsgggGKYQLSTVLVIENPHAQKCWPSGGQMDV 1220
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKLSIIPQ 1254
Cdd:TIGR01271 1221 QGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE-IQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1255 EPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1334
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1335 ATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMFAAAE 1409
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAMSAAD 1453
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
160-446 |
2.96e-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: 414.27 E-value: 2.96e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 160 LSIVCLMITQLAGFSGPAFVVKHLLEYTQDTESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAFK 239
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 240 KILKLKNIKEKSVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRIT 319
Cdd:cd18592 81 KILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 320 AYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSITVGVAPIVMVIASVVTFSV 399
Cdd:cd18592 161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1814750642 400 HMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRF 446
Cdd:cd18592 241 HVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1170-1390 |
3.63e-134 |
|
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: 411.50 E-value: 3.63e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1170 GEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1249
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1329
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1330 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 1390
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
892-1407 |
7.29e-115 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 373.35 E-value: 7.29e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 892 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 971
Cdd:COG1132 62 LLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 972 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLIILFSILHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQ 1050
Cdd:COG1132 142 LVRSVVTLIGALVVLFVIDWRLaLIVLLVLPLLLLVLRLFGR-RLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1051 EFLHRYQELLDNNQRPFFLFTCAMRWLAVRLDLI---SIALITTTGLMIVLmHGQIPPAYAGLAISYAVQLTGLFQFTVR 1127
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLgnlGLALVLLVGGLLVL-SGSLTVGDLVAFILYLLRLFGPLRQLAN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1128 LASETEARFTSVERINHYiktlsLEAPARIKNKS-PSSDWPQEGEVTFENAEMRYQENLPlVLKKVSFTIKPKEKIGIVG 1206
Cdd:COG1132 300 VLNQLQRALASAERIFEL-----LDEPPEIPDPPgAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1207 RTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALE 1283
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAK 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1284 RTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI 1363
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1814750642 1364 AHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFAA 1407
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVEQGTHEELLARG-GLYARLYRL 574
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
556-738 |
6.40e-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: 6.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWILNATLRDNILFGKEFDEERYNS 635
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 636 VLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQKHLK-SK 714
Cdd:cd03250 100 VIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLnNK 179
|
170 180
....*....|....*....|....
gi 1814750642 715 TVLFITHQLQYLADCDEVIFMKEG 738
Cdd:cd03250 180 TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
838-1146 |
2.44e-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: 333.70 E-value: 2.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 838 FLVILSLFMLNVGSTAFSNWWLSYWikqgsgnttvtqenrTSVSSSMKDNPLMQYYASIYALSMAVMLILKAIRGVVFVK 917
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWW---------------SSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 918 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 997
Cdd:cd18580 66 AGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 998 GPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAMRWL 1077
Cdd:cd18580 146 PPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1078 AVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1146
Cdd:cd18580 226 GLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
891-1406 |
9.06e-98 |
|
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: 330.26 E-value: 9.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 891 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVR 964
Cdd:COG2274 190 QDLSTLWVLAIGLLLallfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 965 LPFQAEMFIQNVILVFFCVGMIAGVFPWF----LVAVGPLIILFSILHIVSRVLIRELKRLDNITQSpflsHITSSIQGL 1040
Cdd:COG2274 269 LTGSLLTALLDLLFVLIFLIVLFFYSPPLalvvLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQS----LLVETLRGI 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1041 ATIHAYKKGQEFLHRYQEL----LDNNQRpfflftcaMRWLAVRLDLISIAL--ITTTGLMIV----LMHGQIPP----- 1105
Cdd:COG2274 345 ETIKALGAESRFRRRWENLlakyLNARFK--------LRRLSNLLSTLSGLLqqLATVALLWLgaylVIDGQLTLgqlia 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1106 --AYAGLAISYAVQLTGLFQftvRLAsetEARfTSVERINHYIKtLSLEAPARIKNKSPSsdwPQEGEVTFENAEMRYQE 1183
Cdd:COG2274 417 fnILSGRFLAPVAQLIGLLQ---RFQ---DAK-IALERLDDILD-LPPEREEGRSKLSLP---RLKGDIELENVSFRYPG 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1184 NLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTV 1263
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTI 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1340
Cdd:COG2274 566 RENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 1341 TETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFA 1406
Cdd:COG2274 644 AETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK-GLYAELVQ 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1166-1390 |
1.53e-97 |
|
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: 311.27 E-value: 1.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1166 WPQEGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL 1245
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1246 RSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALerthmkeciaqlplklesEVMENGDNFSVGERQLLCIARALLR 1325
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1326 HCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 1390
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, ... |
838-1145 |
2.46e-89 |
|
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: 292.07 E-value: 2.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 838 FLVILSLFMLNVGSTAFSNWWLSYWIKQGSGNTTVTQENRTsvsssmkdnplmqYYASIYALSMAVMLILKAIRGVVFVK 917
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRD-------------YRLGVYGALGLGQAIFVFLGSLALAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 918 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 997
Cdd:cd18603 68 GCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 998 GPLIILFsilHIVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAM 1074
Cdd:cd18603 148 IPLAILY---FFIQRFYVatsRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSN 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1075 RWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1145
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 ... |
838-1145 |
4.51e-88 |
|
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: 288.22 E-value: 4.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 838 FLVILSLFMLNVGSTAFSNWWLSYWikqgsgnttvtQENRTSVSSSMkdnplmqyYASIYALSMAVMLILKAIRGVVFVK 917
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFW-----------TEDFFGLSQGF--------YIGIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 918 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 997
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 998 GPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAMRWL 1077
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1078 AVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1145
Cdd:cd18606 222 AIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
838-1146 |
4.68e-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: 274.41 E-value: 4.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 838 FLVILSLFMLNVGSTAFSNWWLSYWIKQgsgnttvtqenrTSVSSSMKDNPLMQYYASIYALSMAVMLILKAIRGVVFVK 917
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSH------------SNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 918 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVilvFFCVGMIAGV---FPWFL 994
Cdd:cd18605 69 GGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL---FGLLGYLVVIcyqLPWLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 995 VAVGPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAM 1074
Cdd:cd18605 146 LLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1075 RWLAVRLDLISIALITTTGLMIVLMH---GQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1146
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; ... |
838-1146 |
8.13e-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: 273.57 E-value: 8.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 838 FLVILSLFMLNVGSTAFSNWWLSYWIKQGSGNTTVTQENRTsvsssmkdnplMQYYASIYALSMAVMLILKAIRGVVFVK 917
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVS-----------VLYYLGIYALISLLSVLLGTLRYLLFFF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 918 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVav 997
Cdd:cd18604 70 GSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 998 gPLIILFSILHIVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAM 1074
Cdd:cd18604 148 -PAVVLAALYVYIGRLYLrasRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1075 RWLAVRLDLISIALITTTGLMIVLMHGqIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1146
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) ... |
834-1145 |
8.36e-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: 263.03 E-value: 8.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 834 GPLAFLVILSLFMLNVGSTAFSNWWLSYWiKQGSGNTTVTQENRTSVSSSMKDNPLMQ--YYASIYALSMAVMLILKAIR 911
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYW-ANLEEKLNDTTDRVQGENSTNVDIEDLDrdFNLGIYAGLTAATFVFGFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 912 GVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFP 991
Cdd:cd18601 80 SLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 992 WFLVAVGPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFT 1071
Cdd:cd18601 160 WVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1072 CAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1145
Cdd:cd18601 240 ATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1153-1401 |
9.11e-78 |
|
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: 257.91 E-value: 9.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1153 APARIKNKSPSSDWPQEGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKI 1232
Cdd:cd03288 1 AIASISGSSNSGLVGLGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1233 DGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVG 1312
Cdd:cd03288 81 DGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1313 ERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1392
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPEN 240
|
....*....
gi 1814750642 1393 LLSNDSSRF 1401
Cdd:cd03288 241 LLAQEDGVF 249
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
838-1145 |
8.07e-76 |
|
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: 254.07 E-value: 8.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 838 FLVILSLFMLNVGSTAFSNWWLSYWikqgSGNTTVTQENRTSVSSSMKDNPLMQYYASIYALSMAVMLILKAIRGVVFVK 917
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADW----TEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 918 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 997
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 998 GPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCAMRWL 1077
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1078 AVRLDLISiALITTTGLMIVL---MHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 1145
Cdd:cd18602 237 GIRLDYLG-AVIVFLAALSSLtaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
897-1397 |
2.29e-75 |
|
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: 262.00 E-value: 2.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 897 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV---R-LP-- 966
Cdd:COG4988 60 LLGLLLAVLLLRALlawlRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfaRyLPql 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 967 FQAeMFIQNVILVF-FCVGMIAGVFpwfLVAVGPLIILFSIL-HIVSRVLIRelKRLDNITQspfLS-HITSSIQGLATI 1043
Cdd:COG4988 140 FLA-ALVPLLILVAvFPLDWLSGLI---LLVTAPLIPLFMILvGKGAAKASR--RQWRALAR---LSgHFLDRLRGLTTL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1044 HAY-----------KKGQEFLHRYQELLdnnqRPFFLFTCAMRWLAVrldlISIALIT-TTGLMivLMHGQIPPAyAGLA 1111
Cdd:COG4988 211 KLFgrakaeaeriaEASEDFRKRTMKVL----RVAFLSSAVLEFFAS----LSIALVAvYIGFR--LLGGSLTLF-AALF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1112 IsyaVQLTGLFQFTVR-LASETEARFTSV---ERInhyIKTLSLEAPARIKNKSPSSdWPQEGEVTFENAEMRYQENLPl 1187
Cdd:COG4988 280 V---LLLAPEFFLPLRdLGSFYHARANGIaaaEKI---FALLDAPEPAAPAGTAPLP-AAGPPSIELEDVSFSYPGGRP- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 1267
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1268 DPFN-QYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLL 1346
Cdd:COG4988 432 RLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1347 IQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:COG4988 512 ILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
919-1406 |
9.85e-70 |
|
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: 245.45 E-value: 9.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 919 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD-----VRLPFqaemfIQNVILVFFCVGMIAGVFPWF 993
Cdd:COG4987 83 TLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrVLLPL-----LVALLVILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 994 --LVAVGPLIILFSILHIVSRV---LIRELKRLdnitQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRpff 1068
Cdd:COG4987 158 alVLALGLLLAGLLLPLLAARLgrrAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA--- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1069 lftcAMRWLAvRLDLISIALIT-TTGLMIVLM---------HGQIPPAYAG------LAISYAVQ-LTGLFQFTVRLASe 1131
Cdd:COG4987 231 ----AQRRLA-RLSALAQALLQlAAGLAVVAVlwlaaplvaAGALSGPLLAllvlaaLALFEALApLPAAAQHLGRVRA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1132 tearftSVERINHyiktlSLEAPARIKNKSPSSDWPQEGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSG 1211
Cdd:COG4987 305 ------AARRLNE-----LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1212 KSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMK 1288
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1289 ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLH 1368
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
490 500 510
....*....|....*....|....*....|....*...
gi 1814750642 1369 TVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFA 1406
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1170-1394 |
1.26e-68 |
|
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: 230.58 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1170 GEVTFENAEMRYQENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1249
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFSGTVRSNLDPFNQY-TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1328
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 1329 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLL 1394
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
142-761 |
1.43e-64 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 230.82 E-value: 1.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 142 DDASLRRVVWTFCRT---RLILSIVCLMITQLAGFSGPaFVVKHLLEY---TQDTESNLQYSLLLVLGLLLTEIVRSWSL 215
Cdd:COG1132 4 SPRKLLRRLLRYLRPyrgLLILALLLLLLSALLELLLP-LLLGRIIDAllaGGDLSALLLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 216 ALTWALNYRTGVRLRGAI------LTMAFKKilklknikEKSVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIY 289
Cdd:COG1132 83 YLLARLAQRVVADLRRDLfehllrLPLSFFD--------RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 290 NVIILGPTgfLGSAVFILFyPAMMFVSRITAYFRRKCVTITDDRVQKMNEVLT-YIKFIKMyawVKAFSQ---SVQKIRE 365
Cdd:COG1132 155 VLFVIDWR--LALIVLLVL-PLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQeSLSGIRV---VKAFGReerELERFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 366 EERRMLEKAGYFQSITVGVAPIVMVIAS-----VVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEAS 440
Cdd:COG1132 229 ANEELRRANLRAARLSALFFPLMELLGNlglalVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 441 VAVDRFKSLflMEEVHMIQKKPASPHIT-----IEMKNATLAWDsshsslqnspkltpktkkdkraargkkekvrqlqpt 515
Cdd:COG1132 309 ASAERIFEL--LDEPPEIPDPPGAVPLPpvrgeIEFENVSFSYP------------------------------------ 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 516 ehqavlaeqkghllldsDERPspeeeegkhthlgnlrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLE 595
Cdd:COG1132 351 -----------------GDRP-------------------VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 596 GSIAVNGT-------------FAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERG 661
Cdd:COG1132 395 GRILIDGVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERG 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 662 ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNsAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCIT 741
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
650 660
....*....|....*....|
gi 1814750642 742 ERGTHEELMNLNGDYATIFN 761
Cdd:COG1132 554 EQGTHEELLARGGLYARLYR 573
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1172-1405 |
2.64e-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: 215.56 E-value: 2.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1251
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1326
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1327 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMF 1405
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMW 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1172-1383 |
8.52e-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: 8.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1251
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILI 1331
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1332 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQ 1383
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1172-1404 |
1.42e-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: 210.55 E-value: 1.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1251
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1326
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1327 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAM 1404
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGG--VYAK 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
893-1411 |
1.45e-61 |
|
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: 221.90 E-value: 1.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 893 YASIYALSMAVMLILKAIRGvvfvkgtlrassrlhdELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 972
Cdd:TIGR02203 72 FVSTYLLSWVSNKVVRDIRV----------------RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 973 IQNVILVFFCVGMIAgVFPWFLVAVgpLIILFSILHIVSRVLIRELKRLDNITQSPF--LSHITS-SIQGLATIHAYKkG 1049
Cdd:TIGR02203 136 VRETLTVIGLFIVLL-YYSWQLTLI--VVVMLPVLSILMRRVSKRLRRISKEIQNSMgqVTTVAEeTLQGYRVVKLFG-G 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1050 QEF-LHRYQELldnNQRpfflftcaMRWLAVRLD------------LISIALITTtgLMIVLMHGQIPPAYAGLAISYAV 1116
Cdd:TIGR02203 212 QAYeTRRFDAV---SNR--------NRRLAMKMTsagsisspitqlIASLALAVV--LFIALFQAQAGSLTAGDFTAFIT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1117 QLTGLFQFTVRLA---SETEARFTSVERINHYIKT-LSLEAPARIKNKSpssdwpqEGEVTFENAEMRYQENLPLVLKKV 1192
Cdd:TIGR02203 279 AMIALIRPLKSLTnvnAPMQRGLAAAESLFTLLDSpPEKDTGTRAIERA-------RGDVEFRNVTFRYPGRDRPALDSI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1193 SFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DP 1269
Cdd:TIGR02203 352 SLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1270 fNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQE 1349
Cdd:TIGR02203 432 -EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQA 510
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1350 TIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAMFAAAENK 1411
Cdd:TIGR02203 511 ALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG--LYAQLHNMQFR 570
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
556-738 |
2.38e-60 |
|
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: 206.41 E-value: 2.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVN-----------------GTFAYVAQQAWILNATL 618
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHV 698
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1814750642 699 GNHIFNSAIQKHLK--SKTVLFITHQLQYLADCDEVIFMKEG 738
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1169-1386 |
5.30e-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: 5.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1169 EGEVTFENAEMRYQENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSK 1248
Cdd:COG5265 355 GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARAL 1323
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1324 LRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1386
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
554-754 |
4.58e-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: 208.07 E-value: 4.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRD 620
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVG 699
Cdd:COG4988 430 NLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 700 NHIFNsAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNG 754
Cdd:COG4988 510 AEILQ-ALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
160-445 |
6.51e-56 |
|
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: 196.17 E-value: 6.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 160 LSIVCLMITQLAGFSGPaFVVKHLLEYTQD-TESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAF 238
Cdd:cd18579 1 LAGLLKLLEDLLSLAQP-LLLGLLISYLSSyPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 239 --KKILKLKNIKEKSVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVS 316
Cdd:cd18579 80 rkALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 317 RITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSITVGVAPIVMVIASVVT 396
Cdd:cd18579 160 KLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLAT 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1814750642 397 FSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 445
Cdd:cd18579 240 FATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKR 288
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
895-1407 |
6.91e-56 |
|
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: 205.32 E-value: 6.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 895 SIYALSMAVMLILKAIRGVVFVKGTL---RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 971
Cdd:TIGR02204 59 RYFAFLLVVALVLALGTAARFYLVTWlgeRVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSM 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 972 FIQNVILVFFCVGMIAGVFP---WFLVAVGPLIILfSILhivsrVLIRELKRLDNITQSPFLShiTSSIQGlATIHAYKK 1048
Cdd:TIGR02204 139 ALRNALMCIGGLIMMFITSPkltSLVLLAVPLVLL-PIL-----LFGRRVRKLSRESQDRIAD--AGSYAG-ETLGAIRT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1049 GQEFLHRYQELLDNNQRPFFLFTCAMRWLAVRLDLISIAL-ITTTGLMIVL-------MHGQIPPAYAGLAISYAVQLTG 1120
Cdd:TIGR02204 210 VQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIvLVFGAIVGVLwvgahdvIAGKMSAGTLGQFVFYAVMVAG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1121 LFQFTVRLASETEARFTSVERINHYIKTLS-LEAPAriKNKSPSSdwPQEGEVTFENAEMRYQENLP-LVLKKVSFTIKP 1198
Cdd:TIGR02204 290 SIGTLSEVWGELQRAAGAAERLIELLQAEPdIKAPA--HPKTLPV--PLRGEIEFEQVNFAYPARPDqPALDGLNLTVRP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1199 KEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFN-QYTEDQ 1277
Cdd:TIGR02204 366 GETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRpDATDEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1278 IWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD 1357
Cdd:TIGR02204 446 VEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKG 525
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1358 CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSndSSRFYAMFAA 1407
Cdd:TIGR02204 526 RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA--KGGLYARLAR 573
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1172-1397 |
7.78e-55 |
|
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: 191.21 E-value: 7.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQE--NLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1249
Cdd:cd03249 1 IEFKNVSFRYPSrpDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFSGTVRSNL-----DPfnqyTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALL 1324
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1325 RHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
250-762 |
5.17e-54 |
|
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: 202.37 E-value: 5.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 250 KSVGELINlcsndgqRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFLGS---AVFILFYPAMMFVSRITAYFRRKc 326
Cdd:COG2274 250 RSVGDLAS-------RFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPplaLVVLLLIPLYVLLGLLFQPRLRR- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 327 vtiTDDRVQKMN--------EVLTYIKFIKMYA--------WVKAFSQSVqKIREEERRMLEKAGYFQSITVGVAPIVMV 390
Cdd:COG2274 322 ---LSREESEASakrqsllvETLRGIETIKALGaesrfrrrWENLLAKYL-NARFKLRRLSNLLSTLSGLLQQLATVALL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 391 IASVvtFSV---HMTLGfDLTAAQAFtVVTVFNSMT-FALKVTpfsvkSLSEASVAVDRFKSLFLME-EVHMIQKKPASP 465
Cdd:COG2274 398 WLGA--YLVidgQLTLG-QLIAFNIL-SGRFLAPVAqLIGLLQ-----RFQDAKIALERLDDILDLPpEREEGRSKLSLP 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 466 HIT--IEMKNATLawdsshsslqnspkltpktkkdkraargkkekvrqlqptehqavlaeqkghllldsdeRPSPEEEEg 543
Cdd:COG2274 469 RLKgdIELENVSF----------------------------------------------------------RYPGDSPP- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 544 khthlgnlrlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQ 610
Cdd:COG2274 490 ------------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpaslrrqIGVVLQD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 611 AWILNATLRDNILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDD 689
Cdd:COG2274 558 VFLFSGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDE 637
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 690 PLSALDAHvGNHIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 762
Cdd:COG2274 638 ATSALDAE-TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1170-1385 |
1.36e-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: 187.03 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1170 GEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1249
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFSGTVRSNLDPFNQYTEDQ-IWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1328
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1329 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVV 1385
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
557-766 |
2.48e-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: 2.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSV 636
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 637 LNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQKHLKSKTV 716
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1814750642 717 LFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDyatiFNNLLLG 766
Cdd:cd03291 213 ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD----FSSKLMG 258
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1170-1399 |
4.68e-52 |
|
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: 184.67 E-value: 4.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1170 GEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKL 1249
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD-IQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1329
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1330 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSS 1399
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
895-1396 |
6.05e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 193.40 E-value: 6.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 895 SIYALSM--AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 972
Cdd:TIGR00958 203 AIFFMCLlsIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 973 IQNVILVFFCVGMIAGVFPWF----LVAVGPLIILFSILHIVSRVLIRELKrlDNITQSPFLSHitSSIQGLATIHAYKK 1048
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFAA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1049 GQEFLHRYQELLDNnqrpfflftcaMRWLAVRLDLISIALITTTGLM------IVL-------MHGQIPpayAGLAIS-- 1113
Cdd:TIGR00958 359 EEGEASRFKEALEE-----------TLQLNKRKALAYAGYLWTTSVLgmliqvLVLyyggqlvLTGKVS---SGNLVSfl 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1114 -YAVQLTGLFQFTVRLASETEARFTSVERINHYI-KTLSLEAPARIKNKspssdwPQEGEVTFENAEMRY--QENLPlVL 1189
Cdd:TIGR00958 425 lYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdRKPNIPLTGTLAPL------NLEGLIEFQDVSFSYpnRPDVP-VL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1190 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLD- 1268
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAy 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1269 PFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQ 1348
Cdd:TIGR00958 578 GLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1814750642 1349 ETirEAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:TIGR00958 658 ES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1172-1398 |
1.84e-50 |
|
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: 178.83 E-value: 1.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1251
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1328
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1329 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 1398
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
559-757 |
2.87e-50 |
|
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: 188.44 E-value: 2.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNILFG 625
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 K-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFN 704
Cdd:COG4987 433 RpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLA 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 705 sAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:COG4987 513 -DLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
898-1379 |
2.51e-49 |
|
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: 184.41 E-value: 2.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 898 ALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDvrlPFQAEMFI 973
Cdd:TIGR02857 47 LGALALVLLLRAllgwLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALD---GYFARYLP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 974 QNVILVFFCVGMIAGVFP--W----FLVAVGPLIILFSIL--HIVSRVLIRELKRLDNITqspflSHITSSIQGLATIHA 1045
Cdd:TIGR02857 124 QLVLAVIVPLAILAAVFPqdWisglILLLTAPLIPIFMILigWAAQAAARKQWAALSRLS-----GHFLDRLRGLPTLKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1046 YKK-----------GQEFLHRYQELLdnnqRPFFLFTCAMRWLAVrldlISIALITTT-GLMivLMHGQIPPAYAGLAIS 1113
Cdd:TIGR02857 199 FGRakaqaaairrsSEEYRERTMRVL----RIAFLSSAVLELFAT----LSVALVAVYiGFR--LLAGDLDLATGLFVLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1114 YAVQltglFQFTVR-LASETEARFTSVERINHyIKTLsLEAPARIKNKSPSSDWPQEGEVTFENAEMRYqENLPLVLKKV 1192
Cdd:TIGR02857 269 LAPE----FYLPLRqLGAQYHARADGVAAAEA-LFAV-LDAAPRPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1193 SFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DP 1269
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1270 fnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQE 1349
Cdd:TIGR02857 422 --DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
490 500 510
....*....|....*....|....*....|
gi 1814750642 1350 TIREAFADCTMLTIAHRLHTVLGSDRIMVL 1379
Cdd:TIGR02857 500 ALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
930-1397 |
3.76e-48 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 182.14 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 930 LFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD----------VRlpfQAEMFIQNVILVFFcvgmiagvFPWFLVavgp 999
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAssssgalitvVR---EGASIIGLFIMMFY--------YSWQLS---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1000 lIILFSILHIVSrVLIREL-KRLDNIT---QSPfLSHITSS----IQGLATIHAYKkGQEFLHRYQELLDNNQRpfflfT 1071
Cdd:PRK11176 169 -LILIVIAPIVS-IAIRVVsKRFRNISknmQNT-MGQVTTSaeqmLKGHKEVLIFG-GQEVETKRFDKVSNRMR-----Q 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1072 CAMRwlAVRLDLIS---IALITTTGLMIVLMHGQIPPAYAGL-AISYAVQLTGLFQFTVRLASETE--ARFtsvERINHY 1145
Cdd:PRK11176 240 QGMK--MVSASSISdpiIQLIASLALAFVLYAASFPSVMDTLtAGTITVVFSSMIALMRPLKSLTNvnAQF---QRGMAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1146 IKTL----SLEAPariKNKSPSSDWPQEGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFR 1221
Cdd:PRK11176 315 CQTLfailDLEQE---KDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1222 LVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLD--PFNQYTEDQIWDALERTHMKECIAQLPLKLE 1299
Cdd:PRK11176 392 FYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLD 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1300 SEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVL 1379
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551
|
490
....*....|....*...
gi 1814750642 1380 AQGQVVEFDTPSVLLSND 1397
Cdd:PRK11176 552 EDGEIVERGTHAELLAQN 569
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1169-1407 |
6.24e-46 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 175.92 E-value: 6.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1169 EGEVTFENAEMRYqENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSK 1248
Cdd:PRK13657 332 KGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQEPVLFSGTVRSNL-----DPfnqyTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARAL 1323
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1324 LRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE---FDTpsvlLSNDSSR 1400
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGR 562
|
....*..
gi 1814750642 1401 FYAMFAA 1407
Cdd:PRK13657 563 FAALLRA 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
935-1405 |
5.08e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 172.98 E-value: 5.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 935 LRSPMKFFDTTPTGRILNRFSKDMdEVdVRlpfqaEMFIQNVILVFFCVGMIAGVfpwfLVAVGPL--------IILFSI 1006
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDT-EV-IR-----DLYVTVVATVLRSAALIGAM----LVAMFSLdwrmalvaIMIFPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1007 LHIV-------SRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYKKGQEFLHRYQElldnNQRPFFLftcaMR 1075
Cdd:PRK10790 178 VLVVmviyqrySTPIVRRVRA--------YLADINDgfneVINGMSVIQQFRQQARFGERMGE----ASRSHYM----AR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1076 WLAVRLD------LISI--ALITTtGLMivLMHGQIPPAYAGLAISYA-VQLTG-----LFQFTVRLASETEArFTSVER 1141
Cdd:PRK10790 242 MQTLRLDgfllrpLLSLfsALILC-GLL--MLFGFSASGTIEVGVLYAfISYLGrlnepLIELTTQQSMLQQA-VVAGER 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1142 InhyiktlsLEAPARIKNKSPSSDWP-QEGEVTFENAEMRYQENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALF 1220
Cdd:PRK10790 318 V--------FELMDGPRQQYGNDDRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLM 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1221 RLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLES 1300
Cdd:PRK10790 389 GYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYT 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1301 EVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLA 1380
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLH 548
|
490 500
....*....|....*....|....*
gi 1814750642 1381 QGQVVEFDTPSVLLSNdSSRFYAMF 1405
Cdd:PRK10790 549 RGQAVEQGTHQQLLAA-QGRYWQMY 572
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1169-1384 |
8.78e-45 |
|
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: 161.87 E-value: 8.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1169 EGEVTFENAEMRYQeNLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR 1246
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1247 SKLSIIPQEPVLFSGTVRSNLD-PFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLR 1325
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1326 HCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1384
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
919-1367 |
2.27e-44 |
|
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: 169.85 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 919 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR--LPfqaemfiqnvILVFFCVGMIA-GVFPW 992
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyVRviVP----------AGVALVVGAAAvAAIAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 993 FLVAVGPL--IILFSILHIVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYKKGQEFLHRYQ----ELLDNN 1063
Cdd:TIGR02868 151 LSVPAALIlaAGLLLAGFVAPLVSLRAARAAEQALArlrGELAAQLTDALDGAAELVASGALPAALAQVEeadrELTRAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1064 QRpfflftcAMRWLAVRLDLISIALITTTGLMIVL-----MHGQIPPAYagLAISYAVQLT---GLFQFTVRLASETEAR 1135
Cdd:TIGR02868 231 RR-------AAAATALGAALTLLAAGLAVLGALWAggpavADGRLAPVT--LAVLVLLPLAafeAFAALPAAAQQLTRVR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1136 fTSVERINHYIKTLSLEAPARIKNKSPSSdwPQEGEVTFENAEMRYQENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSL 1215
Cdd:TIGR02868 302 -AAAERIVEVLDAAGPVAEGSAPAAGAVG--LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1216 GMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIA 1292
Cdd:TIGR02868 378 LATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1293 QLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL 1367
Cdd:TIGR02868 456 ALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
552-738 |
7.50e-44 |
|
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: 157.16 E-value: 7.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 552 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATL 618
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNILfgkefdeerynsvlnscclrpdlailpnsdlteigerganlSGGQRQRISLARALYSDRDIYILDDPLSALDAHV 698
Cdd:cd03228 93 RENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1814750642 699 GNHIFNsAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEG 738
Cdd:cd03228 132 EALILE-ALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1189-1412 |
1.10e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 168.87 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG-----GCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTV 1263
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSL------LNALLGflpyqGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1340
Cdd:PRK11174 440 RDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1341 TETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE---FDTpsvlLSNDSSRFYAMFAAAENKI 1412
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAHRQEEI 588
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
557-757 |
2.35e-43 |
|
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: 158.16 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNIL 623
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAhVGNHI 702
Cdd:cd03251 98 YGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ESERL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 703 FNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:cd03251 177 VQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
557-761 |
1.78e-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: 155.47 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNATLRDNIL 623
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGYNIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKE--FDEERYNSVLnSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:cd03253 97 YGRPdaTDEEVIEAAK-AAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTERE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 702 IFNsAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 761
Cdd:cd03253 176 IQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
889-1395 |
3.17e-42 |
|
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: 166.29 E-value: 3.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 889 LMQYYASIYALSMAvMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKdMDEVDVRLpfq 968
Cdd:TIGR03797 175 LVQIALALLAAAVG-AAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRIL--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 969 AEMFIQNVILVFFC----VGMIAGVFPWFLVAVGPLIILFSILHIVSRVLIRELKRLDNItQSPFLSHITSSIQGLATIH 1044
Cdd:TIGR03797 250 SGSTLTTLLSGIFAllnlGLMFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLEL-SGKISGLTVQLINGISKLR 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1045 AYKKGQEFLHRYQELLDNNQRPFFLFTCAMRWLAVrldLISIALITTTGLMIVLMHGQIppAYAGLAISYAVQLTGLF-Q 1123
Cdd:TIGR03797 329 VAGAENRAFARWAKLFSRQRKLELSAQRIENLLTV---FNAVLPVLTSAALFAAAISLL--GGAGLSLGSFLAFNTAFgS 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1124 FTVRLASETEARFTSVERINHYIKTLS-LEAPARIK-NKSPssdwPQE--GEVTFENAEMRYQENLPLVLKKVSFTIKPK 1199
Cdd:TIGR03797 404 FSGAVTQLSNTLISILAVIPLWERAKPiLEALPEVDeAKTD----PGKlsGAIEVDRVTFRYRPDGPLILDDVSLQIEPG 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1200 EKIGIVGRTGSGKSSLgmalFRLveLSG------GCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQY 1273
Cdd:TIGR03797 480 EFVAIVGPSGSGKSTL----LRL--LLGfetpesGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPL 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1274 TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliQETIRE 1353
Cdd:TIGR03797 554 TLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSE 629
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1814750642 1354 AFA--DCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 1395
Cdd:TIGR03797 630 SLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
559-762 |
1.24e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 159.63 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLlEGSIAVNGT-------------FAYVAQQAWILNATLRDNILFG 625
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIelreldpeswrkhLSWVGQNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 K-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIfN 704
Cdd:PRK11174 447 NpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV-M 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 705 SAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 762
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
556-754 |
2.18e-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: 149.30 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNI 622
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:cd03254 98 RLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 702 IfNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNG 754
Cdd:cd03254 178 I-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
509-735 |
4.24e-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: 157.06 E-value: 4.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 509 VRQLQPTEH---QAVLAEQKGHLLLDSDERPSPEEEEGKHTHLGNLRLQ----------RTLYNIDLEIEEGKLVGICGS 575
Cdd:TIGR02857 277 LRQLGAQYHaraDGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSgvsvaypgrrPALRPVSFTVPPGERVALVGP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 576 VGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNATLRDNILFGK-EFDEERYNSVLNSCC 641
Cdd:TIGR02857 357 SGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 642 LRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIfNSAIQKHLKSKTVLFITH 721
Cdd:TIGR02857 437 LDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTH 515
|
250
....*....|....
gi 1814750642 722 QLQYLADCDEVIFM 735
Cdd:TIGR02857 516 RLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
556-740 |
3.04e-39 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 145.81 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNI 622
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:cd03245 99 TLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1814750642 702 IFnSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCI 740
Cdd:cd03245 179 LK-ERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1137-1404 |
4.09e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 154.98 E-value: 4.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1137 TSVERINHYIktlslEAPARIKNKSPSSDWPQEGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLG 1216
Cdd:PRK11160 309 ASARRINEIT-----EQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1217 MALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMkECIAQ 1293
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGL-EKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1294 LPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGS 1373
Cdd:PRK11160 461 DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF 540
|
250 260 270
....*....|....*....|....*....|.
gi 1814750642 1374 DRIMVLAQGQVVEFDTPSVLLSNDsSRFYAM 1404
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLAQQ-GRYYQL 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
932-1403 |
4.58e-39 |
|
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: 156.82 E-value: 4.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 932 RRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemfIQNVIL-VFFCVGMIAGVfPWFLVAVGPLIILFSILHIV 1010
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDA---------LASTILsLFLDMWILVIV-GLFLVRQNMLLFLLSLLSIP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1011 SRVLI-----RELKRLDN---ITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCA---MRWLAV 1079
Cdd:TIGR01193 307 VYAVIiilfkRTFNKLNHdamQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAdqgQQAIKA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1080 RLDLISIALITTTGLMIVLMH----GQIPpAYAGLaISYavqLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEapa 1155
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGkltlGQLI-TFNAL-LSY---FLTPLENIINLQPKLQAARVANNRLNEVYLVDSEF--- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1156 rIKNKSPSSDWPQEGEVTFENAEMRYQENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV 1235
Cdd:TIGR01193 459 -INKKKRTELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1236 RISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQ--YTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGE 1313
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1314 RQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREaFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1393
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
490
....*....|
gi 1814750642 1394 LsnDSSRFYA 1403
Cdd:TIGR01193 696 L--DRNGFYA 703
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1180-1384 |
4.89e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.57 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1180 RYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLF 1259
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1260 SGTVRSNLD-PFN----QYTEDQIWDALERthmkeciaqlpLKLESEVME-NGDNFSVGERQLLCIARALLRHCKILILD 1333
Cdd:COG4619 87 GGTVRDNLPfPFQlrerKFDRERALELLER-----------LGLPPDILDkPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1334 EATAAMDTETDLLIQETIREAFADC--TMLTIAH------RLhtvlgSDRIMVLAQGQV 1384
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
822-1146 |
6.71e-39 |
|
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: 148.41 E-value: 6.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 822 WSVYGVYIQAAGGPLAFLV-ILSLFMLNVGSTAFSNWWLSYWIKQGSGNTTVTQENRTSVSSSMKDNplmQYYASIYALS 900
Cdd:cd18600 3 WNTYLRYITSHKSLIFVLIlCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSS---YYVFYIYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 901 MAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF 980
Cdd:cd18600 80 ADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 981 FCVGMIAGVFPWFLVAVGPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELL 1060
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1061 DNNQRPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQiPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVE 1140
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVS 318
|
....*.
gi 1814750642 1141 RINHYI 1146
Cdd:cd18600 319 RIFKFI 324
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
160-445 |
9.37e-39 |
|
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: 146.83 E-value: 9.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 160 LSIVCLMITQLAGFSGPaFVVKHLLEYTQDTESNlqyslllvlgLLLTEIVRSWSLAL---------TWALNY------R 224
Cdd:cd18597 1 LAGLLKLLADVLQVLSP-LLLKYLINFVEDAYLG----------GPPPSIGYGIGYAIglfllqllsSLLLNHffyrsmL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 225 TGVRLRGAILTMAFkkilklknikEKS------------VGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVI 292
Cdd:cd18597 70 TGAQVRAALTKAIY----------RKSlrlsgksrhefpNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 293 ILGPTGFLGSAVFILFYPAMMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLE 372
Cdd:cd18597 140 NLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 373 KAGYFQSITVGVAPIVMVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 445
Cdd:cd18597 220 KLQILRSILTAVAFSLPVLASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKR 292
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
557-757 |
5.01e-38 |
|
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: 142.68 E-value: 5.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNIL 623
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKE--FDEERyNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVgNH 701
Cdd:cd03249 99 YGKPdaTDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES-EK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 702 IFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
160-445 |
4.82e-37 |
|
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: 142.25 E-value: 4.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 160 LSIVCLMITQLAGFSGPAFVvKHLLEY-TQDTESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRgAILTMA- 237
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFL-NRLLRYlEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLR-AILTQLi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 238 ---------------------FKKILKLKNIKEKSVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGP 296
Cdd:cd18596 79 fekalrrrdksgssksseskkKDKEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 297 TGFLGSAVFILFYPAMMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGY 376
Cdd:cd18596 159 SALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 377 FQSITVGVAPIVMVIASVVTFSVH-MTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 445
Cdd:cd18596 239 LDLLLSLLWFLIPILVTVVTFATYtLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDR 308
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
160-445 |
1.12e-36 |
|
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: 140.68 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 160 LSIVCLMITQLAGFSGPaFVVKHLLEYTQDTESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAI------ 233
Cdd:cd18595 1 LAALLKLLSDILLFASP-QLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALtsaiyr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 234 --LTMAfkkilkLKNIKEKSVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFLGSAVFILFYPA 311
Cdd:cd18595 80 kaLRLS------NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 312 MMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSITV---GVAPiv 388
Cdd:cd18595 154 NAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSflwTCAP-- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 389 mVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 445
Cdd:cd18595 232 -FLVSLATFATYVLSDPDnvLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKR 289
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
556-761 |
1.90e-36 |
|
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: 146.79 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNI 622
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladytlaslrrqVALVSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFGK--EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGN 700
Cdd:TIGR02203 427 AYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 701 HIfNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 761
Cdd:TIGR02203 507 LV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1188-1387 |
2.36e-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: 137.64 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvR 1264
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP-------M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLDPfnQYT-EDQIWDALE--RTHMKECIAQLPLKLESEVMENGDN--------FSVGERQLLCIARALLRHCKILILD 1333
Cdd:cd03257 93 SSLNP--RMTiGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEEvlnrypheLSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1334 EATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 1387
Cdd:cd03257 171 EPTSALDVSVqaqilDLLKK--LQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
557-757 |
1.05e-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: 136.08 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNATLRDNIL 623
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKE-FDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHvGNHI 702
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE-SEHA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 703 FNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:cd03252 177 IMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
557-745 |
1.56e-35 |
|
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: 134.93 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNATLRDNIL 623
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIf 703
Cdd:cd03244 100 PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALI- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1814750642 704 NSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGT 745
Cdd:cd03244 179 QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
649-1379 |
3.08e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 147.10 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 649 LPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDaHVGNHIFNSAIQ--KHLKSKTVLFITHQLQYL 726
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 727 ADCDEVIFM----------------------------------------------KEGC-ITERGTHEELM-NLNGDYAT 758
Cdd:PTZ00265 644 RYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinNAGSyIIEQGTHDALMkNKNGIYYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 759 IFNNLllgetppvEINSKKETSGSQKKTQDKcpKTGSVK-KEKAVKPEEGQLVQMEEKGQGSVPWSVYGVYIQA----AG 833
Cdd:PTZ00265 724 MINNQ--------KVSSKKSSNNDNDKDSDM--KSSAYKdSERGYDPDEMNGNSKHENESASNKKSCKMSDENAsennAG 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 834 GPLAFL----------------VILSLFML--NVGSTAFSnwwlsywIKQGSGNTTVTQENRTSVSSSMKDNPLMQYYA- 894
Cdd:PTZ00265 794 GKLPFLrnlfkrkpkapnnlriVYREIFSYkkDVTIIALS-------ILVAGGLYPVFALLYAKYVSTLFDFANLEANSn 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 895 --SIYALSMAV-MLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDT---TPtGRILNRFSKDMDEVDVRLPFQ 968
Cdd:PTZ00265 867 kySLYILVIAIaMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNN 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 969 AEMFIQNVILvfFCVGMIAGVFPWFLVA---VGPLIILFSILHIVSRVLIR---ELKRL------------DNITQSP-F 1029
Cdd:PTZ00265 946 IVIFTHFIVL--FLVSMVMSFYFCPIVAavlTGTYFIFMRVFAIRARLTANkdvEKKEInqpgtvfaynsdDEIFKDPsF 1023
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1030 LshITSSIQGLATIHAYKKGQEFLHRYQELLD--NNQRPFFLFTCAMRW---LAVRLDLISIA-----LITTTGLMIV-- 1097
Cdd:PTZ00265 1024 L--IQEAFYNMNTVIIYGLEDYFCNLIEKAIDysNKGQKRKTLVNSMLWgfsQSAQLFINSFAywfgsFLIRRGTILVdd 1101
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1098 LMHGQIPPAYAGlaiSYAVQLtglfqftVRLASETEARFTSVERINHYIKTLSL-----EAPARIKNKSPSsdwpqEGEV 1172
Cdd:PTZ00265 1102 FMKSLFTFLFTG---SYAGKL-------MSLKGDSENAKLSFEKYYPLIIRKSNidvrdNGGIRIKNKNDI-----KGKI 1166
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1173 TFENAEMRY--QENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL------------------------- 1225
Cdd:PTZ00265 1167 EIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgd 1245
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1226 -----------------------------SGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDpFNQ--YT 1274
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedAT 1324
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1275 EDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREA 1354
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
890 900
....*....|....*....|....*..
gi 1814750642 1355 --FADCTMLTIAHRLHTVLGSDRIMVL 1379
Cdd:PTZ00265 1405 kdKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1189-1337 |
4.76e-35 |
|
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: 131.23 E-value: 4.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSG-TVRSNL 1267
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1268 -------DPFNQYTEDQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 1337
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1175-1384 |
1.14e-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: 130.80 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1254
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1255 EPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILILDE 1334
Cdd:cd03246 84 DDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1335 ATAAMDTETDLLIQETIREA-FADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1384
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1172-1386 |
1.20e-34 |
|
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: 130.90 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI 1251
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmenGDNFSVGERQLLCIARALLRHCKILI 1331
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1332 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1386
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
557-756 |
5.81e-34 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 139.08 E-value: 5.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI-------------AVNGTFAYVAQQAWILNATLRDNIL 623
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHI 702
Cdd:PRK10789 411 LGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 703 FNSaIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDY 756
Cdd:PRK10789 491 LHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1146-1386 |
1.77e-33 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 137.92 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1146 IKTLSLEAPARIKNKSPSSDwpQEGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL 1225
Cdd:PRK10789 290 IRAMLAEAPVVKDGSEPVPE--GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1226 SGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEV 1302
Cdd:PRK10789 368 SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1303 MENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQG 1382
Cdd:PRK10789 446 GERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHG 525
|
....
gi 1814750642 1383 QVVE 1386
Cdd:PRK10789 526 HIAQ 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1152-1396 |
5.43e-33 |
|
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: 135.42 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1152 EAPARIKNKSPSSDWPQEGE--VTFENAEMRYQENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS 1226
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1227 GGCIKIDGVRISDIG---LADLRSKLSIIPQEPVlfsgtvrSNLDPFnqYT-EDQIWDALE------RTHMKECIAQLpL 1296
Cdd:COG1123 319 SGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPY-------SSLNPR--MTvGDIIAEPLRlhgllsRAERRERVAEL-L 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1297 K---LESEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHR 1366
Cdd:COG1123 389 ErvgLPPDLADrYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL----DVSVQAQILNLLRDlqrelgLTYLFISHD 464
|
250 260 270
....*....|....*....|....*....|.
gi 1814750642 1367 LHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:COG1123 465 LAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1169-1387 |
8.25e-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: 135.65 E-value: 8.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1169 EGEVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSK 1248
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1328
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1329 ILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVVEF 1387
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
251-446 |
2.27e-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: 128.13 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 251 SVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFLGSAVFILFYPAMMFVSRITAYFRRKCVTIT 330
Cdd:cd18594 94 TTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 331 DDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSITVGVAPIVMVIASVVTFSVHMTLGFDLTAA 410
Cdd:cd18594 174 DERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTAR 253
|
170 180 190
....*....|....*....|....*....|....*...
gi 1814750642 411 QAFTVVTVFNS--MTFALKVtPFSVKSLSEASVAVDRF 446
Cdd:cd18594 254 KVFTVISLLNAlrMTITRFF-PESIQTLSESRVSLKRI 290
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
557-757 |
2.34e-32 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 134.38 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKtSLISSILGQM-SLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNI 622
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGK-STIANLLTRFyDIDEGEILLDGHdlrdytlaslrnqVALVSQNVHLFNDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFGKEfdeERYNsvlnscclRPDL--------AI-----LPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDD 689
Cdd:PRK11176 438 AYART---EQYS--------REQIeeaarmayAMdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 690 PLSALDAHvGNHIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:PRK11176 507 ATSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
838-1122 |
3.01e-31 |
|
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: 124.29 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 838 FLVILSLFMLNVGSTAFSNWWLSYWIKQGSGNttvtqenrtsvsSSMKDNPLMQYYAsIYALSMAVMLILKAIRGVVFVK 917
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPD------------GDPETQALNVYSL-ALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 918 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVIlVFFCVGMIAGVFPWFL--- 994
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLA-TIVGGIIVMFYYGWKLtlv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 995 -VAVGPLIILFSIlhIVSRVLiRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFFLFTCA 1073
Cdd:pfam00664 147 lLAVLPLYILVSA--VFAKIL-RKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1074 MRWLAVRLDLI---SIALITTTGlMIVLMHGQIPPAYAGLAISYAVQLTGLF 1122
Cdd:pfam00664 224 NGLSFGITQFIgylSYALALWFG-AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1172-1396 |
5.30e-31 |
|
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: 129.25 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDIGLADLRSK 1248
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQEPvlfsgtvRSNLDPFNqyTEDQIWDALE-----RTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIAR 1321
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALEnlglsRAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1322 ALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
554-757 |
1.42e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 128.79 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRD 620
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGK-EFDEERYNSVLNscclRPDLAILPNSDL---TEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:PRK11160 433 NLLLAApNASDEALIEVLQ----QVGLEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 697 HVGNHIFnSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:PRK11160 509 ETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
221-445 |
1.56e-30 |
|
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: 123.50 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 221 LNYRTGVRLRGAILTMAF----KKILKLKNIKEKSVGELINLCSNDGQRMFEAAAVGSLLAGGP--VIAILGMIYNViiL 294
Cdd:cd18591 79 IVIREGIRLKTALQAMIYekalRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPlkIIVGLILLYLK--L 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 295 GPTGFLGSAVFILFYPAMMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKA 374
Cdd:cd18591 157 GVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKD 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 375 GYFQSITVGVAPIVMVIASVVTFSVHMTL-GFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 445
Cdd:cd18591 237 AVYWSLMTFLTQASPILVTLVTFGLYPYLeGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
557-757 |
2.14e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 129.84 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNIL 623
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKEF-DEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHI 702
Cdd:TIGR00958 577 YGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 703 FNSaiqKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
554-723 |
5.84e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 126.32 E-value: 5.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNATLRD 620
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVG 699
Cdd:TIGR02868 428 NLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|....
gi 1814750642 700 NHIFnSAIQKHLKSKTVLFITHQL 723
Cdd:TIGR02868 508 DELL-EDLLAALSGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
554-744 |
6.97e-30 |
|
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: 117.41 E-value: 6.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------------FAYVAQQAWILNATLRDN 621
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 IlfgkefdeerynsvlnscclrpdlailpnsdlteigerGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:cd03247 95 L--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1814750642 702 IFnSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERG 744
Cdd:cd03247 137 LL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
557-757 |
1.08e-29 |
|
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: 126.47 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG------TFAY-------VAQQAWILNATLRDNIL 623
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvTQASlraaigiVPQDTVLFNDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGK-EFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVgnhi 702
Cdd:COG5265 454 YGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT---- 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 703 fNSAIQKHLKS----KTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:COG5265 530 -ERAIQAALREvargRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1173-1383 |
1.71e-29 |
|
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: 115.42 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1173 TFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSII 1252
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1253 PQepvlfsgtvrsnldpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILIL 1332
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1333 DEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTV-LGSDRIMVLAQGQ 1383
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
554-757 |
2.02e-29 |
|
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: 125.20 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRD 620
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVdlrqldpaelrarMALVPQDPVLFAASVME 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGK--EFDEERYNSVLNScclRPDLAI--LPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:TIGR02204 433 NIRYGRpdATDEEVEAAARAA---HAHEFIsaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 697 HvGNHIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYA 569
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1174-1383 |
2.57e-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: 116.80 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1174 FENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1253
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1254 QEP--VLFSGTVRSNL--DPFN-QYTEDQIW----DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1324
Cdd:cd03225 82 QNPddQFFGPTVEEEVafGLENlGLPEEEIEerveEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1325 RHCKILILDEATAAMDTETDLLIQETIREaFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQ 1383
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
557-757 |
3.72e-29 |
|
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: 125.63 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWI---LNATLRDNILFGKEFDEery 633
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLrrqMGVVLQENVLFSRSIRD--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 634 nsvlNSCCLRPDLAI------------------LPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:TIGR01846 550 ----NIALCNPGAPFehvihaaklagahdfiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 696 AHvGNHIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:TIGR01846 626 YE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1172-1383 |
5.15e-29 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 115.64 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQEN---LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsK 1248
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1328
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1329 ILILDEATAAMDTET-DLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQ 1383
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
507-762 |
6.78e-29 |
|
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: 124.85 E-value: 6.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 507 EKVRQLQPTEHQAVLAEQKGH--LLLDSDERPSPEEEEgKHTHLGNLRLQRTLY----------NIDLEIEEGKLVGICG 574
Cdd:TIGR01193 429 ENIINLQPKLQAARVANNRLNevYLVDSEFINKKKRTE-LNNLNGDIVINDVSYsygygsnilsDISLTIKMNSKTTIVG 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 575 SVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNILFG--KEFDEERYNSVLNS 639
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILENLLLGakENVSQDEIWAACEI 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 640 CCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQkhLKSKTVLFI 719
Cdd:TIGR01193 588 AEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN--LQDKTIIFV 665
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1814750642 720 THQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 762
Cdd:TIGR01193 666 AHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
557-751 |
8.87e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.34 E-value: 8.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------FAYVAQQA---WILNATLRDNILFG 625
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 --------KEFDEERYNSVLNScclrpdLAILpnsDLTE-----IGErganLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEA------LERV---GLEDladrpIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 693 ALDAHVGNHIFnsAIQKHLKS--KTVLFITHQLQYLAD-CDEVIFMKEGCITErGTHEELMN 751
Cdd:COG1121 169 GVDAATEEALY--ELLRELRRegKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
557-736 |
1.06e-28 |
|
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: 115.32 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------FAYVAQQA---WILNATLRDNIL-- 623
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 ------FGKEFDEERYNSVLNScclrpdLAILpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERV---GLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1814750642 697 HvGNHIFNSAIQK-HLKSKTVLFITHQLQYLAD-CDEVIFMK 736
Cdd:cd03235 166 K-TQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
251-445 |
2.41e-28 |
|
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: 116.55 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 251 SVGELINLCSNDGQRMFEAAAVGSLLAGGPV--IAILGMIYNVIilGPTGFLGSAVFILFYPAMMFVSRITAYFRRKCVT 328
Cdd:cd18593 95 TVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLqlIAVIYILWFEI--GWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 329 ITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSITVGVAPIVMVIASVVTFSVHMTLGFDLT 408
Cdd:cd18593 173 RTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILT 252
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1814750642 409 AAQAFTVVTVFNS----MTFALkvtPFSVKSLSEASVAVDR 445
Cdd:cd18593 253 AERVFVTMALYNAvrltMTLFF---PFAIQFGSELSVSIRR 290
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1188-1395 |
5.34e-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: 114.13 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPvlfsgtvRSNL 1267
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP-------YASL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1268 DPF---------------NQYTEDQIWDALERTHMKECIA-QLPLKLesevmengdnfSVGERQLLCIARALLRHCKILI 1331
Cdd:COG1124 93 HPRhtvdrilaeplrihgLPDREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1332 LDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1395
Cdd:COG1124 162 LDEPTSALDVSVqaeilNLL--KDLREER-GLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
554-738 |
7.01e-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: 110.80 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTfayvaQQAWILNATLRDNILFgkefdeery 633
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGY--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 634 nsvlnscclRPDLailpnsdlteigerganlSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGnHIFNSAIQKHLKS 713
Cdd:cd00267 78 ---------VPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAEE 129
|
170 180
....*....|....*....|....*..
gi 1814750642 714 -KTVLFITHQLQYLAD-CDEVIFMKEG 738
Cdd:cd00267 130 gRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
559-751 |
1.10e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.85 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------------FAYVAQQAWI-LNATLRDNILF- 624
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALyPDLTVRENLRFf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 ------GKEFDEERYNSVLNSCclrpdlailpnsDLTE-IGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAh 697
Cdd:COG1131 98 arlyglPRKEARERIDELLELF------------GLTDaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 698 VGNHIFNSAIQKHLKS-KTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:COG1131 165 EARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
521-750 |
1.15e-27 |
|
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: 119.76 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 521 LAEQKGHLLLDS-DERPSPEEeegkhthlgnlrlQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIA 599
Cdd:TIGR01842 310 LPEPEGHLSVENvTIVPPGGK-------------KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 600 VNG-------------TFAYVAQQAWILNATLRDNIL-FGKEFDEErynSVLNSCCLRP--DLAI-LPNSDLTEIGERGA 662
Cdd:TIGR01842 377 LDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPE---KIIEAAKLAGvhELILrLPDGYDTVIGPGGA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 663 NLSGGQRQRISLARALYSDRDIYILDDPLSALDAhVGNHIFNSAIqKHLKSK--TVLFITHQLQYLADCDEVIFMKEGCI 740
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-EGEQALANAI-KALKARgiTVVVITHRPSLLGCVDKILVLQDGRI 531
|
250
....*....|
gi 1814750642 741 TERGTHEELM 750
Cdd:TIGR01842 532 ARFGERDEVL 541
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
545-751 |
1.53e-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: 112.97 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 545 HTHLGNLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQ- 610
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQDp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 611 ----------AWILNATLRdniLFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYS 680
Cdd:COG1124 89 yaslhprhtvDRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL----------DRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 681 DRDIYILDDPLSALDAHVGNHIFN--SAIQKHLKSkTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNllKDLREERGL-TYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
528-757 |
2.25e-27 |
|
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: 120.05 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 528 LLLDSDERPSPEEEEGK---HTHLGNL-----RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI 598
Cdd:TIGR03796 457 LLEEPEGSAATSEPPRRlsgYVELRNItfgysPLEPPLIeNFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 599 AVNG-------------TFAYVAQQAWILNATLRDNI-LFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANL 664
Cdd:TIGR03796 537 LFDGipreeiprevlanSVAMVDQDIFLFEGTVRDNLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 665 SGGQRQRISLARALYSDRDIYILDDPLSALDAHVgnhifNSAIQKHLKSK--TVLFITHQLQYLADCDEVIFMKEGCITE 742
Cdd:TIGR03796 617 SGGQRQRLEIARALVRNPSILILDEATSALDPET-----EKIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQ 691
|
250
....*....|....*
gi 1814750642 743 RGTHEELMNLNGDYA 757
Cdd:TIGR03796 692 RGTHEELWAVGGAYA 706
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
557-757 |
2.56e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 118.91 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISsilgqmsLLE-------GSIAVNGT-------------FAYVAQQAWILNA 616
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLIN-------LLQrvfdpqsGRILIDGTdirtvtraslrrnIAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 TLRDNILFGKE--FDEERYNSVLNSCCLrpDLaILPNSD--LTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:PRK13657 424 SIEDNIRVGRPdaTDEEMRAAAERAQAH--DF-IERKPDgyDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 693 ALDAHVGNHIfNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:PRK13657 501 ALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
548-740 |
8.87e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.52 E-value: 8.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 548 LGNLRLQRT----LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQ 610
Cdd:COG4619 3 LEGLSFRVGgkpiLSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 611 AWILNATLRDNILF-----GKEFDEERYNSVLNSCCLRPDLAilpNSDLTEigerganLSGGQRQRISLARALYSDRDIY 685
Cdd:COG4619 83 PALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDIL---DKPVER-------LSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 686 ILDDPLSALDAHvgN-HIFNSAIQKHLKSK--TVLFITHQLQYLAD-CDEVIFMKEGCI 740
Cdd:COG4619 153 LLDEPTSALDPE--NtRRVEELLREYLAEEgrAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
544-744 |
9.09e-27 |
|
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: 109.90 E-value: 9.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 544 KHTHLGNLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT----------------FAYV 607
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 608 AQQA-----------WILNATLRDN-ILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISL 674
Cdd:cd03257 88 FQDPmsslnprmtigEQIAEPLRIHgKLSKKEARKEAVLLLLVGVGLPEEVLnRYPHE-----------LSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 675 ARALYSDRDIYILDDPLSALDAHVGNHIFNsaIQKHLKSK---TVLFITHQLQYLAD-CDEVIFMKEGCITERG 744
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILD--LLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
556-738 |
9.63e-27 |
|
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: 109.48 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------------FAYVAQQawILNATL 618
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkvglvFQNPDDQ--FFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNILFGKE---FDEERYNSVLNSCCLRPDLAILPNSDLteigergANLSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:cd03225 94 EEEVAFGLEnlgLPEEEIEERVEEALELVGLEGLRDRSP-------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1814750642 696 AHVGNHIFnsAIQKHLKS--KTVLFITHQLQYLAD-CDEVIFMKEG 738
Cdd:cd03225 167 PAGRRELL--ELLKKLKAegKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1188-1397 |
1.01e-26 |
|
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: 110.52 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVL-FSGTVR-- 1264
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRel 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 ------SNLDPFNQYTED---QIWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:COG1120 96 valgryPHLGLFGRPSAEdreAVEEALERTGLEH-LADRPV----------DELSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1336 TAAMDTETDLLIQETIRE--AFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:COG1120 165 TSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTPE 229
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
557-760 |
1.38e-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: 116.53 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNIL 623
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIdintvtreslrksIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKE--FDEERYNSVLNSCCLRPDLAILPNSDlTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:TIGR01192 431 LGREgaTDEEVYEAAKAAAAHDFILKRSNGYD-TLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEAR 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 702 IFNsAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIF 760
Cdd:TIGR01192 510 VKN-AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
557-740 |
3.89e-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: 106.53 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNIL 623
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 fgkefdeerynsvlnscclrpdlailpnsdlteigerganlSGGQRQRISLARALYSDRDIYILDDPLSALDaHVGNHIF 703
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 1814750642 704 NSAIQkHLKSK--TVLFITHQLQYLADCDEVIFMKEGCI 740
Cdd:cd03246 136 NQAIA-ALKAAgaTRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1174-1397 |
7.73e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1174 FENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1253
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1254 QEPvlfsgtvrsnlDpfNQY----TEDQIWDALE-----RTHMKECIAQLPLKLEsevMEN-----GDNFSVGERQLLCI 1319
Cdd:PRK13632 90 QNP-----------D--NQFigatVEDDIAFGLEnkkvpPKKMKDIIDDLAKKVG---MEDyldkePQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1320 ARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
537-751 |
8.17e-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: 114.07 E-value: 8.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 537 SPEEEEGkhTHL----GNLRLQR-----------TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVN 601
Cdd:COG4618 315 VPAEPER--MPLprpkGRLSVENltvvppgskrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 602 GT-------------FAYVAQQAWILNATLRDNI-LFGkEFDEERynsVLNSCclrpDLA-----I--LPNSDLTEIGER 660
Cdd:COG4618 393 GAdlsqwdreelgrhIGYLPQDVELFDGTIAENIaRFG-DADPEK---VVAAA----KLAgvhemIlrLPDGYDTRIGEG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 661 GANLSGGQRQRISLARALYSDRDIYILDDPLSALDAhVGNHIFNSAIQkHLKS--KTVLFITHQLQYLADCDEVIFMKEG 738
Cdd:COG4618 465 GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAALAAAIR-ALKArgATVVVITHRPSLLAAVDKLLVLRDG 542
|
250
....*....|...
gi 1814750642 739 CITERGTHEELMN 751
Cdd:COG4618 543 RVQAFGPRDEVLA 555
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
559-744 |
8.43e-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: 8.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQqawILNATlrdnilfg 625
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ---ALELL-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 kefdeerynsvlnscclrpdlailpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFN 704
Cdd:cd03214 86 ---------------------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1814750642 705 SAIQ-KHLKSKTVLFITHQL----QYladCDEVIFMKEGCITERG 744
Cdd:cd03214 139 LLRRlARERGKTVVMVLHDLnlaaRY---ADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
554-732 |
1.09e-25 |
|
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: 106.02 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------------FAYVAQQ-AWILNATLR 619
Cdd:COG4133 14 ERLLFsGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHAdGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILF-----GKEFDEERYNSVLnscclrpdlAILpnsDLTEIGER-GANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:COG4133 94 ENLRFwaalyGLRADREAIDEAL---------EAV---GLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1814750642 694 LDAHvGNHIFNSAIQKHLKS-KTVLFITHQLQYLADCDEV 732
Cdd:COG4133 162 LDAA-GVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
557-738 |
2.48e-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: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------FAYVAQQA----WilnATLRDNILF 624
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpW---LTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 G-------KEFDEERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRDIYILDDPLSALDA- 696
Cdd:COG1116 104 GlelrgvpKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1814750642 697 ---HVGNHIFNsaIQKHLKsKTVLFITHQLQ---YLAdcDEVIFMKEG 738
Cdd:COG1116 173 treRLQDELLR--LWQETG-KTVLFVTHDVDeavFLA--DRVVVLSAR 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
559-751 |
3.49e-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: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWI-LNATLRDNILF 624
Cdd:COG1120 19 DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEPPApFGLTVRELVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 G-----------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:COG1120 99 GryphlglfgrpSAEDREAVEEALERT------------GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 693 ALDAHvgnHIFnsAIQKHLKS------KTVLFITHQL----QYladCDEVIFMKEGCITERGTHEELMN 751
Cdd:COG1120 167 HLDLA---HQL--EVLELLRRlarergRTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1192-1390 |
3.54e-25 |
|
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: 107.83 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGVRISDIGLADLR----SKLSIIPQEPVlfsgtvr 1264
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLDPFnqYT-EDQIWDALeRTH-------MKECIAQLpLKL-----ESEVMengDN----FSVGERQLLCIARALLRHC 1327
Cdd:COG0444 97 TSLNPV--MTvGDQIAEPL-RIHgglskaeARERAIEL-LERvglpdPERRL---DRypheLSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 1328 KILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTP 1390
Cdd:COG0444 170 KLLIADEPTTALDVTIqaqilNLLKD--LQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelFENP 242
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
559-755 |
3.60e-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: 105.71 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGtFAYVAQQAWILNA--------------TLRDNI-L 623
Cdd:COG4555 19 DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQigvlpderglydrlTVRENIrY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FG---KEFDEERYNSVLNscclrpdlaILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRDIYILDDPLSALDAhVG 699
Cdd:COG4555 98 FAelyGLFDEELKKRIEE---------LIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 700 NHIFNSAIQKHLKS-KTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMNLNGD 755
Cdd:COG4555 168 RRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
557-735 |
5.27e-25 |
|
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: 104.86 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------FAYVAQQA----WilnATLRDNILF 624
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 GkefdeerynsvlnscclrPDLAILPNSDLTEIGER---------GAN-----LSGGQRQRISLARALYSDRDIYILDDP 690
Cdd:cd03293 97 G------------------LELQGVPKAEARERAEEllelvglsgFENayphqLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1814750642 691 LSALDAHVGNHIFN--SAIQKHLKsKTVLFITHqlqylaDCDEVIFM 735
Cdd:cd03293 159 FSALDALTREQLQEelLDIWRETG-KTVLLVTH------DIDEAVFL 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1188-1393 |
5.39e-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: 104.96 E-value: 5.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRISDIGLAD--LRSKLSIIPQEPVLFS 1260
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegeVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1261 GTVRSNLDpfnqYTeDQIWDALERTHMKECIAQLpLK---LESEVME--NGDNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:cd03260 95 GSIYDNVA----YG-LRLHGIKLKEELDERVEEA-LRkaaLWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1336 TAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVL 1393
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
559-751 |
6.42e-25 |
|
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: 110.76 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGqmsLLE---GSIAVNGT----------------FAYVAQ----QawiLN 615
Cdd:COG1123 283 DVSLTLRRGETLGLVGESGSGKSTLARLLLG---LLRptsGSILFDGKdltklsrrslrelrrrVQMVFQdpysS---LN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 616 A--TLRDNILFG--------KEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLARALYSDRDIY 685
Cdd:COG1123 357 PrmTVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDLA----------DRYPHELSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 686 ILDDPLSALDAHVGNHIFN--SAIQKHLKsKTVLFITHQL---QYLadCDEVIFMKEGCITERGTHEELMN 751
Cdd:COG1123 427 ILDEPTSALDVSVQAQILNllRDLQRELG-LTYLFISHDLavvRYI--ADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
554-740 |
6.76e-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: 104.14 E-value: 6.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------FAYVAQQaWIL--NATLRD 620
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD-YALfpHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFG----KEFDEERYNSVLNScclrpdLAILpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:cd03259 92 NIAFGlklrGVPKAEIRARVREL------LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 696 AHVgnhifNSAIQKHLKS------KTVLFITH-QLQYLADCDEVIFMKEGCI 740
Cdd:cd03259 163 AKL-----REELREELKElqrelgITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1172-1404 |
7.39e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLSI 1251
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQE-------PVlfsgTVR----SNLDP----FNQYTE---DQIWDALERTHMKE----CIAQLplklesevmengdnf 1309
Cdd:COG1121 80 VPQRaevdwdfPI----TVRdvvlMGRYGrrglFRRPSRadrEAVDEALERVGLEDladrPIGEL--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1310 SVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 1387
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHG 220
|
250
....*....|....*..
gi 1814750642 1388 DTPSVLLSNDSSRFYAM 1404
Cdd:COG1121 221 PPEEVLTPENLSRAYGG 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
557-740 |
7.96e-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: 102.48 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVngtfayvaqqawilnatlrdnilFGKEFDEERyNSV 636
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 637 LNSCCLRPDLAILPnSDLTeiGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAhVGNHIFNSAIQKHLKS-KT 715
Cdd:cd03230 72 KRRIGYLPEEPSLY-ENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRELKKEgKT 147
|
170 180
....*....|....*....|....*.
gi 1814750642 716 VLFITHQLQYLAD-CDEVIFMKEGCI 740
Cdd:cd03230 148 ILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1175-1385 |
1.52e-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: 102.13 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1254
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1255 epvlfsgtvrsnldpfnqytedqiwdALERT---HMKEC-IAQLplklesevmengdnfSVGERQLLCIARALLRHCKIL 1330
Cdd:cd03214 81 --------------------------ALELLglaHLADRpFNEL---------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1331 ILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRL-HTVLGSDRIMVLAQGQVV 1385
Cdd:cd03214 120 LLDEPTSHLDiahqIELLELLRRLARE--RGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
554-768 |
1.61e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 110.19 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNATLRD 620
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVgn 700
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-- 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 701 hifNSAIQKHL----KSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNLLLGET 768
Cdd:PRK10790 512 ---EQAIQQALaavrEHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
559-692 |
3.66e-24 |
|
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: 100.03 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNA-TLRDNILF 624
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPRlTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 625 GKEFdEERYNSVLNScclRPDLAI--LPNSDL--TEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:pfam00005 83 GLLL-KGLSKREKDA---RAEEALekLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1175-1391 |
3.89e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.94 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1254
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1255 EP-VLFSG-TVRSNLD--------PFNQYTEdQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1324
Cdd:PRK13635 89 NPdNQFVGaTVQDDVAfglenigvPREEMVE-RVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1325 RHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPS 1391
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1118-1380 |
4.59e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 110.50 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1118 LTGLFQFTVRLASETEarftsverinhYIKtlSLEAPA---RIKNKSPSSDWPQEGE-------VTFENAEMRYQENLPL 1187
Cdd:PTZ00265 332 LISMFMLTIILPNITE-----------YMK--SLEATNslyEIINRKPLVENNDDGKklkdikkIQFKNVRFHYDTRKDV 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 -VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKI-DGVRISDIGLADLRSKLSIIPQEPVLFSGTVRS 1265
Cdd:PTZ00265 399 eIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKN 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NLDPF-----------NQYTED--------------------------QIWDALERTHMK-------------------- 1288
Cdd:PTZ00265 479 NIKYSlyslkdlealsNYYNEDgndsqenknkrnscrakcagdlndmsNTTDSNELIEMRknyqtikdsevvdvskkvli 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1289 -ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLT--IAH 1365
Cdd:PTZ00265 559 hDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAH 638
|
330
....*....|....*
gi 1814750642 1366 RLHTVLGSDRIMVLA 1380
Cdd:PTZ00265 639 RLSTIRYANTIFVLS 653
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
839-1146 |
1.14e-23 |
|
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: 103.06 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 839 LVILSLFMLNVGSTAFSNWWLSYWIKQgSGNTTVTQEnrtsvsssmkdnplmQYYASIYALSMAVMLILKAIRGVVFVKG 918
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDD-PVNGPQEHG---------------QVYLSVLGALAILQGITVFQYSMAVSIG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 919 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF---IQNVILVFFcvgMIAGVFPWFLV 995
Cdd:cd18559 66 GIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWmgpLQNVIGLYL---LILLAGPMAAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 996 AVgPLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRyQELLDNNQRPFFLFTCAMR 1075
Cdd:cd18559 143 GI-PLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQ-VDAKRDNELAYLPSIVYLR 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1076 WLAVRLDLISIALITTTGLMIVLMHGQIpPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 1146
Cdd:cd18559 221 ALAVRLWCVGPCIVLFASFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
550-744 |
1.16e-23 |
|
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: 100.83 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 NLRLQRTLYNIDLEIE---EGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------------FAYVAQ 609
Cdd:cd03297 3 CVDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 610 QAWIL-NATLRDNILFGKEFDEERYNSVlnscclRPDlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYIL 687
Cdd:cd03297 83 QYALFpHLNVRENLAFGLKRKRNREDRI------SVD-ELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 688 DDPLSALDAHVGNHIFN--SAIQKHLKsKTVLFITH---QLQYLadCDEVIFMKEGCITERG 744
Cdd:cd03297 156 DEPFSALDRALRLQLLPelKQIKKNLN-IPVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
553-745 |
1.18e-23 |
|
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: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 553 LQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNATLR 619
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNI-LFGKEFDEERYNSVlnscclrpdlailpnsdltEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHV 698
Cdd:cd03369 100 SNLdPFDEYSDEEIYGAL-------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1814750642 699 gNHIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGT 745
Cdd:cd03369 161 -DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1189-1386 |
1.19e-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: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlFSG---- 1261
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 -TV-----------RSNLDPfnQYTEDQIWDALERTHmkeciaqlplkLESEVM-----EngdnFSVGERQLLCIARALL 1324
Cdd:COG4172 379 mTVgqiiaeglrvhGPGLSA--AERRARVAEALEEVG-----------LDPAARhryphE----FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1325 RHCKILILDEATAAMdtetDLLIQETIREAFADC------TMLTIAHRLHTV--LgSDRIMVLAQGQVVE 1386
Cdd:COG4172 442 LEPKLLVLDEPTSAL----DVSVQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1172-1383 |
1.34e-23 |
|
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: 99.18 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG--LADLRSKL 1249
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFSG-TVRSNLdpfnqytedqiwdalerthmkeciaQLPLklesevmengdnfSVGERQLLCIARALLRHCK 1328
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------------------ALGL-------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1329 ILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQ 1383
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
547-749 |
1.36e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 547 HLGNLRLqrtLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGqmslLE----GSIAVNGT--F----------AYVAQQ 610
Cdd:COG1118 11 RFGSFTL---LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGRdlFtnlpprerrvGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 611 AwilnA-----TLRDNILFGkefdeerynsvlnscclrpdLAILPNS---------------DLTEIGER-GANLSGGQR 669
Cdd:COG1118 84 Y----AlfphmTVAENIAFG--------------------LRVRPPSkaeirarveellelvQLEGLADRyPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 670 QRISLARALYSDRDIYILDDPLSALDAHVgnhifnsaiQKHLKSK----------TVLFITH-QLQYLADCDEVIFMKEG 738
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKV---------RKELRRWlrrlhdelggTTVFVTHdQEEALELADRVVVMNQG 210
|
250
....*....|.
gi 1814750642 739 CITERGTHEEL 749
Cdd:COG1118 211 RIEQVGTPDEV 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1174-1382 |
1.59e-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: 100.30 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1174 FENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLSIIP 1253
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1254 QE-------PVLFSGTVRSNLDP----FNQYTEDQ---IWDALERTHMKE----CIAQLplklesevmengdnfSVGERQ 1315
Cdd:cd03235 75 QRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSEladrQIGEL---------------SGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1316 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGS-DRIMVLAQG 1382
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLLNRT 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
557-750 |
1.75e-23 |
|
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: 100.48 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG------TFAYVAQQAWIL---------NATLRDN 621
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRKVGLVfqnpddqlfAPTVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFG-------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:COG1122 97 VAFGpenlglpREEIRERVEEALELV------------GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 694 LDAHVGNHIFNsAIQK-HLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELM 750
Cdd:COG1122 165 LDPRGRRELLE-LLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
554-751 |
3.20e-23 |
|
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: 99.88 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT----------------FAYVAQQAWILNA- 616
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 TLRDNILF-----GKEFDEERYNSV---LNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRDIYILD 688
Cdd:cd03261 93 TVFENVAFplrehTRLSEEEIREIVlekLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 689 DPLSALDAhVGNHIFNSAI---QKHLKSkTVLFITHQLQ-YLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIrslKKELGL-TSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
544-738 |
4.75e-23 |
|
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: 99.10 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 544 KHTHLGNLRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------------FAY 606
Cdd:cd03255 8 KTYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 607 VAQQAWILNA-TLRDNILFGKEF-------DEERYNSVLNSCCLRPDLAILPNsdlteigergaNLSGGQRQRISLARAL 678
Cdd:cd03255 87 VFQSFNLLPDlTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 679 YSDRDIYILDDPLSALDAHVGNHIFNsAIQK--HLKSKTVLFITHQLQYLADCDEVIFMKEG 738
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVME-LLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1134-1366 |
5.20e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.27 E-value: 5.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1134 ARFTS-VERINHYIKtlSLEAPARIKNKSPSSDWPQEGEVTFENAEMRYQENLPLVlKKVSFTIKPKEKIGIVGRTGSGK 1212
Cdd:COG4178 326 AEWRAtVDRLAGFEE--ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1213 SSLgmalFRLveLSG------GCIKI-DGVRISdigladlrsklsIIPQEPVLFSGTVRSNL---DPFNQYTEDQIWDAL 1282
Cdd:COG4178 403 STL----LRA--IAGlwpygsGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1283 ERTHMKECIAQLplkleSEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLT 1362
Cdd:COG4178 465 EAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVIS 539
|
....
gi 1814750642 1363 IAHR 1366
Cdd:COG4178 540 VGHR 543
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1172-1396 |
6.90e-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: 98.81 E-value: 6.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGVRISDIGLADL 1245
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGlerpTSGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1246 ---RSKLSIIPQEPVLFSG-TVRSNLD-PFnqytedQIWdALERTHMKECIAQLpLK---LESEVMENGDNFSVGERQLL 1317
Cdd:cd03258 78 rkaRRRIGMIFQHFNLLSSrTVFENVAlPL------EIA-GVPKAEIEERVLEL-LElvgLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1318 CIARALLRHCKILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1391
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETtqsilALLRD--INREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 1814750642 1392 VLLSN 1396
Cdd:cd03258 227 EVFAN 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1175-1384 |
8.02e-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: 96.70 E-value: 8.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSIIPQ 1254
Cdd:cd03230 4 RNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1255 EPVLFSG-TVRSNLDpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILILD 1333
Cdd:cd03230 81 EPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1334 EATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 1384
Cdd:cd03230 121 EPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
557-749 |
9.54e-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: 98.42 E-value: 9.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSIlgqmSLLE----GSIAVNGT----------------FAYVAQQAWILNA 616
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI----NGLErptsGSVLVDGTdltllsgkelrkarrrIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 -TLRDNILF-------GKEFDEERYNSVLNscclrpdlailpnsdLTEIGERG----ANLSGGQRQRISLARALYSDRDI 684
Cdd:cd03258 97 rTVFENVALpleiagvPKAEIEERVLELLE---------------LVGLEDKAdaypAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 685 YILDDPLSALDAHVGNHIFN--SAIQKHLKSkTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:cd03258 162 LLCDEATSALDPETTQSILAllRDINRELGL-TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
557-738 |
1.79e-22 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 96.10 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTfayvaqqawilnaTLRDNILFGKEFdEERYNSV 636
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-------------DLTDLEDELPPL-RRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 637 LNSCCLRPDLAILPNsdlteIGERganLSGGQRQRISLARALYSDRDIYILDDPLSALDAhvgnhIFNSAIQKHLKS--- 713
Cdd:cd03229 82 FQDFALFPHLTVLEN-----IALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDP-----ITRREVRALLKSlqa 148
|
170 180
....*....|....*....|....*....
gi 1814750642 714 ---KTVLFITHQLQYLAD-CDEVIFMKEG 738
Cdd:cd03229 149 qlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
555-751 |
2.30e-22 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 102.67 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILG---QMSLLEGSIAVNGT-------------FAYVAQQAWI-LN-A 616
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMTqLNpV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 TLRDNILFGKEFD----EERYNSVLnscclrpdlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:COG1123 100 TVGDQIAEALENLglsrAEARARVL---------ELLEAVGLERRLDRYpHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 692 SALDAHVGNHIFnsAIQKHLKS---KTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:COG1123 171 TALDVTTQAEIL--DLLRELQRergTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1192-1386 |
2.66e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.81 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvRSNLD 1268
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-------YASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1269 PfnQYT-EDQIWDALE------RTHMKECIAQLPLK--LESEVM-----EngdnFSVGERQLLCIARALLRHCKILILDE 1334
Cdd:COG4608 110 P--RMTvGDIIAEPLRihglasKAERRERVAELLELvgLRPEHAdryphE----FSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1335 ATAAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRL----HTvlgSDRIMVLAQGQVVE 1386
Cdd:COG4608 184 PVSAL----DVSIQaqvlnllEDLQDEL-GLTYLFISHDLsvvrHI---SDRVAVMYLGKIVE 238
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
557-740 |
6.20e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 96.00 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNATLRDNIL 623
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FG---KEFDE-----ERYNSVLNscclrpdLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:cd03248 110 YGlqsCSFECvkeaaQKAHAHSF-------ISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1814750642 696 AHvGNHIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCI 740
Cdd:cd03248 183 AE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
555-749 |
1.29e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.22 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGqmslLE----GSIAVNGT-----------FAYVAQQaWIL--NAT 617
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG----LEdptsGEILIGGRdvtdlppkdrnIAMVFQS-YALypHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFG-------KEFDEERYNSVLnscclrpdlAILpnsDLTEIGER-GANLSGGQRQRISLARALYSDRDIYILDD 689
Cdd:COG3839 92 VYENIAFPlklrkvpKAEIDRRVREAA---------ELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 690 PLSALDAHVGNH----IfnSAIQKHLKSkTVLFITH-QLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:COG3839 160 PLSNLDAKLRVEmraeI--KRLHRRLGT-TTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
557-742 |
1.51e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.73 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISsILGqmsLL----EGSIAVNGT-----------------FAYVAQQAWIL- 614
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILG---GLdrptSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 615 NATLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRD 683
Cdd:COG1136 100 ELTALENVALplllagvSRKERRERARELL---------------ERVGLGDRLdhrpSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 684 IYILDDPLSALDAHVGNHIFNsAIQKHLKS--KTVLFITHQLQYLADCDEVIFMKEGCITE 742
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLE-LLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1188-1400 |
1.94e-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: 94.88 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLSIIPQEPVLFSG-TV 1263
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMGMLFQSGALFDSlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSNLD-PFNQYTEDQIWDALERThmKECIAQLPLKLESEVMEngDNFSVGERQLLCIARALLRHCKILILDEATAAMD-- 1340
Cdd:cd03261 95 FENVAfPLREHTRLSEEEIREIV--LEKLEAVGLRGAEDLYP--AELSGGMKKRVALARALALDPELLLYDEPTAGLDpi 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1341 --TETDLLIQeTIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1400
Cdd:cd03261 171 asGVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1188-1386 |
2.29e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.71 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPQEPVLFSG-TVR 1264
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDA-QAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLdpF--NQYTEDQI--WDALERThMKECIAQL--PLKLESEVMEngdnFSVGERQLLCIARALLRHCKILILDEATAA 1338
Cdd:COG1129 98 ENI--FlgREPRRGGLidWRAMRRR-ARELLARLglDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1339 M-DTETDLLIqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:COG1129 171 LtEREVERLF-RIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1188-1385 |
2.41e-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: 92.11 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsklsiipqEPVLFSGtvrsnl 1267
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFAS------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1268 dpfnqytedqIWDALErtHMKECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAM-DTETDLL 1346
Cdd:cd03216 69 ----------PRDARR--AGIAMVYQL---------------SVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1814750642 1347 IqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:cd03216 122 F-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
159-446 |
3.01e-21 |
|
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: 95.70 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 159 ILSIVCLMItqlaGFSGPaFVVKHLLEYTQDTESNLQYSLLLVLGLLLTEIVRS-WSLALTWALNyRTGVRLRGAILTMA 237
Cdd:cd18598 4 LLKLLADVL----GFAGP-LLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGAlLSSHYNFQMN-KVSLKVRAALVTAV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 238 F--KKILKLKNIKEKSVGELINLCSNDGQRMfeAAAVGSL--LAGGPV-IAI-LGMIY---NVIILGPTGFLGSAVFILF 308
Cdd:cd18598 78 YrkALRVRSSSLSKFSTGEIVNLMSTDADRI--VNFCPSFhdLWSLPLqIIVaLYLLYqqvGVAFLAGLVFALVLIPINK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 309 YPAmmfvSRITAYFRRKcVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEE------RRMLEKA-GYFQSIT 381
Cdd:cd18598 156 WIA----KRIGALSEKM-MKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKElkalkgRKYLDALcVYFWATT 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 382 vgvaPIVMviaSVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRF 446
Cdd:cd18598 231 ----PVLI---SILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
555-751 |
3.23e-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: 94.33 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFA-----------YVAQQ-AWILNATLRDNI 622
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFGKEFDEERYnsvlnscclRPDLA--------ILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:cd03296 96 AFGLRVKPRSE---------RPPEAeirakvheLLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 694 LDAHVGNHIFNSAIQKHLK-SKTVLFITH-QLQYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDElHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1172-1384 |
6.03e-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: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE-LSGGCIKIDGV---RISDIGLADL 1245
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTdisKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1246 R-SKLSIIPQEPVLFSG-TVRSNLD-------PFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQL 1316
Cdd:cd03255 80 RrRHIGFVFQSFNLLPDlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1317 LCIARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1384
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1188-1396 |
7.15e-21 |
|
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: 92.88 E-value: 7.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEPVLFSG-TVRS 1265
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NL--------DPFNQYTEDQIWDALERthMKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEATA 1337
Cdd:cd03224 95 NLllgayarrRAKRKARLERVYELFPR--LKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1338 ----AMDTEtdllIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:cd03224 162 glapKIVEE----IFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
555-757 |
9.76e-21 |
|
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: 98.88 E-value: 9.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI-------------AVNGTFAYVAQQAWILNATLRDN 621
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqdlagldvqAVRRQLGVVLQNGRLMSGSIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALD----AH 697
Cdd:TIGR03797 547 IAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDnrtqAI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 698 VgnhifnSAIQKHLKSkTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYA 757
Cdd:TIGR03797 627 V------SESLERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
554-749 |
1.08e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSIlgqmSLLE---------GSIAVNGTFAYVAQQAWILNatLRDNILF 624
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeagtirvGDITIDTARSLSQQKGLIRQ--LRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 -GKEFDEERYNSVLNSCCLRP--------DLAI-LPNSDLTEIGERGAN------LSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK11264 90 vFQNFNLFPHRTVLENIIEGPvivkgepkEEATaRARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 689 DPLSALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1172-1386 |
1.58e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.65 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 1248
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQE-PVLFSGTVRSNL---------DPfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 1318
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgkSR--KEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1319 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREafADCTMLtIA-HRLHTVLGSD-RIMVLAQGQVVE 1386
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsweimELL--EEINR--RGTTVL-IAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
557-749 |
1.65e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------FAYVAQQ-AWILNATLRDNILF 624
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 GKEFDEERYnsvlnscclRPDLAI--------LPNSDLTEIGER-GANLSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:PRK10851 98 GLTVLPRRE---------RPNAAAikakvtqlLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 696 AHVGNHIFNSAIQKHLKSK-TVLFITH-QLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1172-1412 |
3.41e-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: 91.59 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1251
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSG-TVRSN--LDP-FNQYTEDQIwdaleRTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHC 1327
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKI-----RERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1328 KILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEFDTPS 1391
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFK-------------RLQQELGktivfvthdideafrlADRIAIMKNGEIVQVGTPD 221
|
250 260
....*....|....*....|.
gi 1814750642 1392 VLLSNDSSRFYAMFAAAENKI 1412
Cdd:cd03295 222 EILRSPANDFVAEFVGADRLL 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
559-749 |
3.64e-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: 94.01 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------FAYVAQQAwilnA-----TLRDNI 622
Cdd:COG3842 23 DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDY----AlfphlTVAENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFG-------KEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:COG3842 99 AFGlrmrgvpKAEIRARVAELL---------------ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 692 SALDAHVGNH----IFNsaIQKHLKsKTVLFITH-QLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:COG3842 164 SALDAKLREEmreeLRR--LQRELG-ITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
557-749 |
6.27e-20 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 90.32 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISsILGQMSLL------EGSIAVNG---------------TFAYVAQQAWILN 615
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLR-LLNRLNDLipgapdEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 616 ATLRDNILFG--------KEFDEERYNSVLnscclrpDLAILPNsdltEIGER--GANLSGGQRQRISLARALYSDRDIY 685
Cdd:cd03260 95 GSIYDNVAYGlrlhgiklKEELDERVEEAL-------RKAALWD----EVKDRlhALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 686 ILDDPLSALDAhVGNHIFNSAIQKHLKSKTVLFITHQLQYLADC-DEVIFMKEGCITERGTHEEL 749
Cdd:cd03260 164 LLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
554-735 |
8.35e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------FAYVAQQ----AWiLNAtlRDN 621
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadRGVVFQKdallPW-LNV--LDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFGKefdeeRYNSVLNSCCLRPDLAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAhvgn 700
Cdd:COG4525 97 VAFGL-----RLRGVPKAERRARAEELLALVGLADFARRRiWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA---- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1814750642 701 hIFNSAIQKHL------KSKTVLFITHqlqylaDCDEVIFM 735
Cdd:COG4525 168 -LTREQMQELLldvwqrTGKGVFLITH------SVEEALFL 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
550-750 |
1.15e-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: 92.47 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 NLRLQR---TLyNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------------FAYVAQ 609
Cdd:COG4148 6 DFRLRRggfTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 610 QAwILNATL--RDNILFG-----KEFDEERYNSVLnscclrpdlailpnsDLTEIG---ERG-ANLSGGQRQRISLARAL 678
Cdd:COG4148 85 EA-RLFPHLsvRGNLLYGrkrapRAERRISFDEVV---------------ELLGIGhllDRRpATLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 679 YSDRDIYILDDPLSALDAHVGNHI--FNSAIQKHLkSKTVLFITHQL---QYLAdcDEVIFMKEGCITERGTHEELM 750
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEIlpYLERLRDEL-DIPILYVSHSLdevARLA--DHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1188-1388 |
1.16e-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: 89.12 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADLRSKLSIIPQEPVLFSG-TVRSN 1266
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVFQDYALFPHlTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LDpF--------NQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 1338
Cdd:cd03259 93 IA-FglklrgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1339 MDTETDLLIQETIREAFA--DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1388
Cdd:cd03259 161 LDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1172-1353 |
1.27e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 88.69 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI 1251
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSG-TVRSNLDpF------NQYTEDQIWDALERTHMKECiAQLPLKlesevmengdNFSVGERQLLCIARALL 1324
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGL-ADLPVR----------QLSAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*....
gi 1814750642 1325 RHCKILILDEATAAMDTETDLLIQETIRE 1353
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1183-1366 |
1.41e-19 |
|
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: 87.21 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1183 ENLPLV-------LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlRSKLSIIPQE 1255
Cdd:cd03223 4 ENLSLAtpdgrvlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFLPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1256 PVLFSGTVRsnldpfnqyteDQI---WDalerthmkeciaqlplklesevmengDNFSVGERQLLCIARALLRHCKILIL 1332
Cdd:cd03223 73 PYLPLGTLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 1814750642 1333 DEATAAMDTETDLLIQETIREAFAdcTMLTIAHR 1366
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
559-751 |
1.67e-19 |
|
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: 89.28 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWIL-NATLRDNI-- 622
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVEENIal 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 ---LFG--KEFDEERYNSVLNSCCLRPdlailpnsdlTEIGER-GANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:cd03295 99 vpkLLKwpKEKIRERADELLALVGLDP----------AEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 697 hvgnhIFNSAIQ---KHLKS---KTVLFITHQLQ---YLAdcDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03295 169 -----ITRDQLQeefKRLQQelgKTIVFVTHDIDeafRLA--DRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
557-751 |
2.25e-19 |
|
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: 89.63 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------------FAYVAQQ-AWILNATL 618
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrrkkISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNILFG-------KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 692 SALDAHVGNHIFNS--AIQKHLKsKTVLFITHqlqylaDCDEVI-------FMKEGCITERGTHEELMN 751
Cdd:cd03294 189 SALDPLIRREMQDEllRLQAELQ-KTIVFITH------DLDEALrlgdriaIMKDGRLVQVGTPEEILT 250
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
550-755 |
3.33e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.27 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 NLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---TFAYVAQ-------QAWILNA--T 617
Cdd:COG3840 8 TYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAErpvsmlfQENNLFPhlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFGkefdeerynsvlnsccLRPDL-----------AILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRDIY 685
Cdd:COG3840 88 VAQNIGLG----------------LRPGLkltaeqraqveQALERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 686 ILDDPLSALD--------AHVgnhifnSAIQKHLKSkTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMNLNGD 755
Cdd:COG3840 152 LLDEPFSALDpalrqemlDLV------DELCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1188-1397 |
5.24e-19 |
|
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: 87.73 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGL-ADLRSKLSI--IPQEPVLFSG-TV 1263
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLpPHRIARLGIgyVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSNLD--PFNQYTEDQIWDALERTH-----MKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEAT 1336
Cdd:COG0410 96 EENLLlgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1337 AAmdtetdL--LIQETIREAFAD-----CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:COG0410 165 LG------LapLIVEEIFEIIRRlnregVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
223-445 |
5.61e-19 |
|
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: 89.20 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 223 YRTGVRLRGAILTMAFKKILKLKNIKEKS--VGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFL 300
Cdd:cd18559 63 SIGGIFASRAVHLDLYHKALRSPISFFERtpSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 301 GSAVFILFYPAMMFVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSI 380
Cdd:cd18559 143 GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAL 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 381 TVGVAPIVMVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 445
Cdd:cd18559 223 AVRLWCVGPCIVLFASFFAYVSRHSLagLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1172-1395 |
6.40e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.64 E-value: 6.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLP-LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1250
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1251 IIPQepvlfsgtvrsnlDPFNQYT----EDQIWDALE-----RTHMKECIAQlplKLESEVMENGDN-----FSVGERQL 1316
Cdd:PRK13650 85 MVFQ-------------NPDNQFVgatvEDDVAFGLEnkgipHEEMKERVNE---ALELVGMQDFKEreparLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1317 LCIARALLRHCKILILDEATAAMDTETDL-LIQ--ETIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1393
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLeLIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
..
gi 1814750642 1394 LS 1395
Cdd:PRK13650 228 FS 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1188-1384 |
6.59e-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: 86.81 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKLSIIPQEPVLFSG-TVR 1264
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLdpfnqyTEDQIW--------------DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKIL 1330
Cdd:cd03262 95 ENI------TLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1331 ILDEATAAMDTEtdlLIQE---TIREAFAD-CTMLTIAHRlhtvLG-----SDRIMVLAQGQV 1384
Cdd:cd03262 158 LFDEPTSALDPE---LVGEvldVMKDLAEEgMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1188-1396 |
7.54e-19 |
|
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: 87.11 E-value: 7.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDIGlADLRSKLSIIP--QEPVLFSG 1261
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 -TVRSNL----------DPFNQYTEDQIWDALERTHmkECIAQLPLkleSEVM-ENGDNFSVGERQLLCIARALLRHCKI 1329
Cdd:cd03219 90 lTVLENVmvaaqartgsGLLLARARREEREARERAE--ELLERVGL---ADLAdRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1330 LILDEATAAM-DTETDLLIqETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:cd03219 165 LLLDEPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1189-1382 |
7.56e-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: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSK----LSIIPQEPVLFSGTVR 1264
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNL---DPFNQYTEDQIWDALErthMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1341
Cdd:cd03290 97 ENItfgSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1814750642 1342 E-TDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQG 1382
Cdd:cd03290 174 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1175-1391 |
8.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.57 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKL 1249
Cdd:PRK13637 6 ENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEP--VLFSGTVRSNLD--PFN-QYTEDQIWDALERThMKEciaqlpLKLESEVMENGDNF--SVGERQLLCIARA 1322
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAfgPINlGLSEEEIENRVKRA-MNI------VGLDYEDYKDKSPFelSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1323 LLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI--AHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1391
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlvSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
552-741 |
8.82e-19 |
|
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: 86.16 E-value: 8.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 552 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG----------TFAYVAQQAwilnatlrDN 621
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDV--------DY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFGkefdeeryNSVLNSCCLRPDLA---------ILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:cd03226 83 QLFT--------DSVREELLLGLKELdagneqaetVLKDLDLYALKERHpLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 692 SALDAH----VGNHIFNSAIQKhlksKTVLFITHQLQYLAD-CDEVIFMKEGCIT 741
Cdd:cd03226 155 SGLDYKnmerVGELIRELAAQG----KAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1172-1404 |
1.03e-18 |
|
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: 87.45 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSL-GMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1250
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1251 II---------PQEPVL------FSGTVrsnlDPFNQYTEDQI---WDALERTHMKECIAQLPLKLesevmengdnfSVG 1312
Cdd:COG1119 82 LVspalqlrfpRDETVLdvvlsgFFDSI----GLYREPTDEQReraRELLELLGLAHLADRPFGTL-----------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1313 ERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF-D 1388
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAgP 226
|
250
....*....|....*.
gi 1814750642 1389 TPSVLLSNDSSRFYAM 1404
Cdd:COG1119 227 KEEVLTSENLSEAFGL 242
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
893-1334 |
1.05e-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: 91.78 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 893 YASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMD---EVDVRLPFqa 969
Cdd:COG4615 50 LLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 970 emFIQNVILVFFCVGMIAgvfpW-----FLVAVGPLIILFSILHIVSRVLIRELKRLDNiTQSPFLSHITSSIQGLA--T 1042
Cdd:COG4615 128 --LLQSVALVLGCLAYLA----WlspplFLLTLVLLGLGVAGYRLLVRRARRHLRRARE-AEDRLFKHFRALLEGFKelK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1043 IHAyKKGQEFLHRY-----QELLDNNQRPFFLFTCAMRWlavrldlISIALITTTGLmIVLMHGQIPPAYAGLAISYAvq 1117
Cdd:COG4615 201 LNR-RRRRAFFDEDlqptaERYRDLRIRADTIFALANNW-------GNLLFFALIGL-ILFLLPALGWADPAVLSGFV-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1118 LTGLF------QFTVRLASETEARfTSVERINHYikTLSLEAPARIKNKSPSSDWPQE-GEVTFENAEMRY---QENLPL 1187
Cdd:COG4615 270 LVLLFlrgplsQLVGALPTLSRAN-VALRKIEEL--ELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYpgeDGDEGF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFsgtvRSNL 1267
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1268 DPFNQYTEDQIWDALERthmkeciaqlpLKLESEVMENGDNF-----SVGERQLLCIARALLRHCKILILDE 1334
Cdd:COG4615 423 GLDGEADPARARELLER-----------LELDHKVSVEDGRFsttdlSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
557-751 |
1.19e-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: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------FAYVAQQ-AWILNATLRDNILF 624
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 G----KEFDEERYNSVLNsccLRPDLAIlpnsdlTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVG 699
Cdd:cd03299 95 GlkkrKVDKKEIERKVLE---IAEMLGI------DHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 700 NHIFN--SAIQKHLKSkTVLFITHQL-QYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03299 166 EKLREelKKIRKEFGV-TVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1188-1391 |
1.26e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvR 1264
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLDPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMEN-----------GDNFSVGERQLLCIARALLRHCKILILD 1333
Cdd:PRK15134 373 SSLNP--RLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvgldpetrhryPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1334 EATAAMDTETD-----LL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTPS 1391
Cdd:PRK15134 451 EPTSSLDKTVQaqilaLLksLQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVEqgdcervFAAPQ 518
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
556-744 |
1.30e-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: 86.15 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-----------TFAYVAQQ-AWILNATLRDNIL 623
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FG-------KEFDEERYNSVlnscclrpdlailpnSDLTEIGE----RGANLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:cd03301 95 FGlklrkvpKDEIDERVREV---------------AELLQIEHlldrKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 693 ALDAHVGNHIFN--SAIQKHLKsKTVLFITH-QLQYLADCDEVIFMKEGCITERG 744
Cdd:cd03301 160 NLDAKLRVQMRAelKRLQQRLG-TTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1188-1396 |
1.49e-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: 87.02 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISdiGL-ADLRSKLSI-----IPQepv 1257
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDIT--GLpPHRIARLGIartfqNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1258 LFSG-TVRSN-----------------LDPFNQYTE-----DQIWDALERTHMKECIAQLPlklesevmengDNFSVGER 1314
Cdd:COG0411 90 LFPElTVLENvlvaaharlgrgllaalLRLPRARREerearERAEELLERVGLADRADEPA-----------GNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1315 QLLCIARALLRHCKILILDEATAAM-DTETDLLIqETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1390
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTP 237
|
....*.
gi 1814750642 1391 SVLLSN 1396
Cdd:COG0411 238 AEVRAD 243
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
557-733 |
1.55e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.98 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG--TFAYVAQQ---AWILNATLRDNI---LFGKEF 628
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 629 DEERYN----SVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFN 704
Cdd:NF040873 88 LWRRLTrddrAAVDDALERVGLADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....*....
gi 1814750642 705 SAIQKHLKSKTVLFITHQLQYLADCDEVI 733
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
552-750 |
1.65e-18 |
|
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: 89.02 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 552 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------------FAYVAQQAWIL 614
Cdd:TIGR02142 8 RLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 615 -NATLRDNILFGKEF--------DEERYNSVLNsccLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRDIY 685
Cdd:TIGR02142 88 pHLSVRGNLRYGMKRarpserriSFERVIELLG---IGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 686 ILDDPLSALDAHVGNHI--FNSAIQKHLKSKtVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELM 750
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEIlpYLERLHAEFGIP-ILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1172-1385 |
2.72e-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: 85.11 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRSKL 1249
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFSG-TVRSNLDPFNQYTedqiwdALERTHMKECIAQLPLKLE-SEVME-NGDNFSVGERQLLCIARALLRH 1326
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLY------GLKGDELTARLEELADRLGmEELLDrRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1327 CKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
559-751 |
3.90e-18 |
|
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: 85.42 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT----------------FAYVAQQAwilnA-----T 617
Cdd:COG1127 23 GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelrrrIGMLFQGG----AlfdslT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFG-KEF----DEERYNSVLNScclrpdlailpnsdLTEIGERGAN------LSGGQRQRISLARALYSDRDIYI 686
Cdd:COG1127 99 VFENVAFPlREHtdlsEAEIRELVLEK--------------LELVGLPGAAdkmpseLSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 687 LDDPLSALDAHVGNHIFN--SAIQKHLKSkTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:COG1127 165 YDEPTAGLDPITSAVIDEliRELRDELGL-TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1173-1407 |
4.15e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.19 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1173 TFENAEMRYQEnLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlRsKLSII 1252
Cdd:COG3840 3 RLDDLTYRYGD-FPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1253 PQEPVLFSG-TVRSN----LDPFNQYTEDQ---IWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1324
Cdd:COG3840 77 FQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1325 RHCKILILDEATAAMD----TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSS 1399
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*...
gi 1814750642 1400 rfyAMFAA 1407
Cdd:COG3840 224 ---PALAA 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
557-749 |
5.35e-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: 84.93 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT----------------FAYVAQQ-AWILNATLR 619
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGKEfdeeRYNSVLNSCCLRPD-------LAILPNSDLTE-IGERGANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:cd03256 97 ENVLSGRL----GRRSTWRSLFGLFPkeekqraLAALERVGLLDkAYQRADQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 692 SALD---AHVGNHIFNSAIQKHlkSKTVLFITHQLQY-LADCDEVIFMKEGCITERGTHEEL 749
Cdd:cd03256 173 ASLDpasSRQVMDLLKRINREE--GITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1189-1386 |
2.59e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLSIIPQEPVlfsgtvrS 1265
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NLDPfNQYTEDQIWDALeRTH-----------MKECIAQLPLKLEsEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1334
Cdd:PRK10261 413 SLDP-RQTVGDSIMEPL-RVHgllpgkaaaarVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1335 ATAAMDTET-----DLL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:PRK10261 490 AVSALDVSIrgqiiNLLldLQRDFGIAY-----LFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
551-744 |
2.84e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 82.16 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 551 LRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---TFAYVAQQAwiLNATLRDNILFGKE 627
Cdd:cd03298 8 FSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRP--VSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 628 FDEERYnsvlnscclrpDLAILPNSDLTEIgERGA-------------------NLSGGQRQRISLARALYSDRDIYILD 688
Cdd:cd03298 86 TVEQNV-----------GLGLSPGLKLTAE-DRQAievalarvglaglekrlpgELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 689 DPLSALDAHVGNHIFNSAIQKHLKSK-TVLFITHQLQ-YLADCDEVIFMKEGCITERG 744
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKmTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1167-1406 |
2.90e-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: 83.22 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1167 PQEGEVTFENAEMRYQENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDI 1240
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1241 GladlrSKLSIIPQEPVLFs-gTVRSN---------LDPfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfS 1310
Cdd:COG1116 79 G-----PDRGVVFQEPALLpwlTVLDNvalglelrgVPK--AERRERARELLELVGLAGFEDAYPHQL-----------S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1311 VGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAH------RLhtvlgSDRIMVLAQ- 1381
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHdvdeavFL-----ADRVVVLSAr 215
|
250 260 270
....*....|....*....|....*....|.
gi 1814750642 1382 -GQV-----VEFDTPSVLLSNDSSRFYAMFA 1406
Cdd:COG1116 216 pGRIveeidVDLPRPRDRELRTSPEFAALRA 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1172-1399 |
4.02e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.26 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLVLKKVSFTIkPKEK-IGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1250
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNI-PKGQwTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1251 IIPQEPV-LFSGT-----VRSNLDPFNQYTEDqiwdalerthMKECIAQLpLKlESEVMENGDN----FSVGERQLLCIA 1320
Cdd:PRK13648 87 IVFQNPDnQFVGSivkydVAFGLENHAVPYDE----------MHRRVSEA-LK-QVDMLERADYepnaLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1321 RALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 1398
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
.
gi 1814750642 1399 S 1399
Cdd:PRK13648 235 E 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
559-774 |
4.77e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---TFAYVAQ-------QAWIL--NATLRDNILFGK 626
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQrdicmvfQSYALfpHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 627 EF----DEERYNSVlnscclRPDLAILpnsDLTEIGERGAN-LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:PRK11432 104 KMlgvpKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 702 IFNS--AIQKHLkSKTVLFITH-QLQYLADCDEVIFMKEGCITERGTHEEL---------MNLNGDyATIFNNLLLGETp 769
Cdd:PRK11432 175 MREKirELQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELyrqpasrfmASFMGD-ANIFPATLSGDY- 251
|
....*
gi 1814750642 770 pVEIN 774
Cdd:PRK11432 252 -VDIY 255
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
553-759 |
6.89e-17 |
|
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: 82.26 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 553 LQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLR 619
Cdd:cd03288 33 LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlrsrLSIILQDPILFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVG 699
Cdd:cd03288 113 FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 700 NhIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELM-NLNGDYATI 759
Cdd:cd03288 193 N-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
533-722 |
1.05e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 533 DERPSPEEEEGKHTHLGNLRLQ----RTLY-NIDLEIEEGKLVGICGSVGSGKTSLISSILGqmslL----EGSIAV--N 601
Cdd:COG4178 350 EAASRIETSEDGALALEDLTLRtpdgRPLLeDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 602 GTFAYVAQQAWILNATLRDNILF---GKEFDEERYNSVLNSCCLrPDLAilpnSDLTEIGERGANLSGGQRQRISLARAL 678
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHLA----ERLDEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1814750642 679 YSDRDIYILDDPLSALDAHVGNHIFnSAIQKHLKSKTVLFITHQ 722
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALY-QLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
557-770 |
1.14e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT----------------FAYVAQQAWILNATLRD 620
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklvgIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGKEfdeerynsvlnSCCLRP-DLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:PRK13644 98 DLAFGPE-----------NLCLPPiEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 694 LDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEelmnlngdyaTIFNNL---LLGETPP 770
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE----------NVLSDVslqTLGLTPP 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
557-740 |
1.16e-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: 80.27 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSIlgqmSLLE----GSIAVNGTFAYVAQQAWilnATLRDNIlfGKEFdeER 632
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI----NLLEepdsGTIIIDGLKLTDDKKNI---NELRQKV--GMVF--QQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 633 YN-----SVLNSCCLRPDLAI-LPNSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:cd03262 85 FNlfphlTVLENITLAPIKVKgMSKAEAEERALEllekvGladkadaypAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1814750642 693 ALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCI 740
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1189-1385 |
1.46e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLgM-ALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPQEPVLFSG-TVR 1264
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSPRDA-IALGIGMVHQHFMLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNL----DPFNQYTEDqiWDALeRTHMKECIAQLPLKL--ESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAA 1338
Cdd:COG3845 99 ENIvlglEPTKGGRLD--RKAA-RARIRELSERYGLDVdpDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1339 M-DTETDLLIqETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:COG3845 172 LtPQEADELF-EILRR-LAAegKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
559-722 |
1.60e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---TFAYVAQQAWIL---NA-----TLRDNILFGKE 627
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiDDPDVAEACHYLghrNAmkpalTVAENLEFWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 628 FdeerynsvLNSCCLRPD--LAILPNSDLTEIgeRGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHvGNHIFNS 705
Cdd:PRK13539 100 F--------LGGEELDIAaaLEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAE 168
|
170
....*....|....*...
gi 1814750642 706 AIQKHLKSK-TVLFITHQ 722
Cdd:PRK13539 169 LIRAHLAQGgIVIAATHI 186
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
557-738 |
2.65e-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: 78.75 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSL--LEGSIAVNGT----------FAYVAQQ-AWILNATLRDNIL 623
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrkiIGYVPQDdILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FgkefdeerynsvlnSCCLRpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIF 703
Cdd:cd03213 105 F--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1814750642 704 NSAIQKHLKSKTVLFITHQLQYL--ADCDEVIFMKEG 738
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEifELFDKLLLLSQG 188
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1188-1396 |
2.86e-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: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRI--SDIGLADLRSKLSIIPQEPVLFS 1260
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1261 GTV---------------RSNLDpfnqytedqiwDALERThmkeciaqlpLK---LESEV----MENGDNFSVGERQLLC 1318
Cdd:COG1117 106 KSIydnvayglrlhgiksKSELD-----------EIVEES----------LRkaaLWDEVkdrlKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1319 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSV 1392
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGPTEQ 239
|
....
gi 1814750642 1393 LLSN 1396
Cdd:COG1117 240 IFTN 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1188-1385 |
4.00e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSI--IPQEPVLFSG-TVR 1264
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLD---PFNQytedqiwDALERthMKECIAQLPLKLESEVmeNGDNFSVGERQLLCIARALLRHCKILILDEATAAMD- 1340
Cdd:PRK15439 105 ENILfglPKRQ-------ASMQK--MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1814750642 1341 TETDLLIQEtIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:PRK15439 174 AETERLFSR-IRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
555-740 |
4.14e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 79.24 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQM---SLLEGSIAVNGT----------FAYVAQQ-AWILNATLRD 620
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQprkpdqfqkcVAYVRQDdILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILF------GKEFDEERYNSVLNSCCLRpDLAIlpnsdlTEIG-ERGANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:cd03234 101 TLTYtailrlPRKSSDAIRKKRVEDVLLR-DLAL------TRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 694 LDAHVGNHIFNSAIQKHLKSKTVLFITHQLQylADC----DEVIFMKEGCI 740
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPR--SDLfrlfDRILLLSSGEI 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1172-1404 |
5.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLRSKLS 1250
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1251 IIPQEP-VLFSG-TVRSNLdPFNqyTEDQIWDALE-RTHMKECIAQlpLKLESEVMENGDNFSVGERQLLCIARALLRHC 1327
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL-AFG--PENLCLPPIEiRKRVDRALAE--IGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1328 KILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 1404
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1188-1385 |
5.92e-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: 77.59 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIglaDLRSKLSIIPQEPVLFSG-TVR 1264
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLdpfnQYTedqiwdalerthmkeciAQLplklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1344
Cdd:cd03213 101 ETL----MFA-----------------AKL------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1814750642 1345 LLIQETIRE-AFADCTMLTIAHRLHTVLGS--DRIMVLAQGQVV 1385
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1172-1386 |
6.09e-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: 78.28 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrSKL 1249
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFS-GTVRSN--LDPfnqytEDQIWDALE-RTHMKECIAQLPLKlesevmENGDNF----SVGERQLLCIAR 1321
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGL-----ELQGVPKAEaRERAEELLELVGLS------GFENAYphqlSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1322 ALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLH-TVLGSDRIMVLAQ--GQVVE 1386
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
554-755 |
6.56e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGtFAYVAQQAW----------------ILNAT 617
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvfqnpdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:PRK13635 99 VQDDVAFGLE----------NIGVPREEMVERVDQALRQVGmedflnREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 692 SALD----AHVGNHIfnsaiqKHLKSK---TVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGD 755
Cdd:PRK13635 169 SMLDprgrREVLETV------RQLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
543-769 |
6.63e-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: 79.46 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 543 GKHTHlgnlrlQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG----------------TFAY 606
Cdd:TIGR02769 19 GAKQR------APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 607 VAQQA-----------WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLA 675
Cdd:TIGR02769 93 VFQDSpsavnprmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDA----------DKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 676 RALYSDRDIYILDDPLSALDAHVGNHIFnsAIQKHLKSK---TVLFITHQL---QYLadCDEVIFMKEGCITERGTHEEL 749
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVIL--ELLRKLQQAfgtAYLFITHDLrlvQSF--CQRVAVMDKGQIVEECDVAQL 238
|
250 260
....*....|....*....|
gi 1814750642 750 MNLNGDYATIFNNLLLGETP 769
Cdd:TIGR02769 239 LSFKHPAGRNLQSAVLPEHP 258
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
557-751 |
7.23e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 78.24 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYVAQ-QAWILNATLRDN 621
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFG-----KEFDEERYNSVlnscclrpdLAILPNsdLTEI-GERGANLSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:cd03224 96 LLLGayarrRAKRKARLERV---------YELFPR--LKERrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 696 AHVGNHIFNsAIQKhLKSK--TVLFITHQLQY-LADCDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03224 165 PKIVEEIFE-AIRE-LRDEgvTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
557-751 |
9.79e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.88 E-value: 9.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKtSLISSIL-GQMSLLEGSIAVNG------TFAYVAQQAWI---------LNATLRD 620
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGK-STISKILtGLLKPQSGEIKIDGitiskeNLKEIRKKIGIifqnpdnqfIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIGERGA------NLSGGQRQRISLARALYSDRDIYILDDPLSAL 694
Cdd:PRK13632 104 DIAFGLE----------NKKVPPKKMKDIIDDLAKKVGMEDYldkepqNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 695 DAHVGNHI--FNSAIQKHlKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK13632 174 DPKGKREIkkIMVDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
557-738 |
1.42e-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: 75.54 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTfayvaqqawilnatlrdnilfgkefdEERYNSv 636
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 637 lnscclrPDLAIlpnsdlteigERGAN----LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFnsAIQKHLK 712
Cdd:cd03216 69 -------PRDAR----------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF--KVIRRLR 129
|
170 180
....*....|....*....|....*....
gi 1814750642 713 S--KTVLFITHQLQYLAD-CDEVIFMKEG 738
Cdd:cd03216 130 AqgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
554-751 |
1.67e-15 |
|
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: 77.28 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------FAYVAQQ-AWILNATLRDN 621
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNyALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFG-------KEFDEERYNSVLnscclrpDLAilpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:cd03300 93 IAFGlrlkklpKAEIKERVAEAL-------DLV-----QLEGYANRKpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 694 LDAHVGNHIFN--SAIQKHLKSkTVLFITH-QLQYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03300 161 LDLKLRKDMQLelKRLQKELGI-TFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
557-749 |
1.75e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.35 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSIlgqmSLLE----GSIAVNGT--------------------FayvaQQAW 612
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGVdltalserelraarrkigmiF----QHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 613 ILNA-TLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYS 680
Cdd:COG1135 93 LLSSrTVAENVALpleiagvPKAEIRKRVAELL---------------ELVGLSDKAdaypSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 681 DRDIYILDDPLSALDAHVGNHIFN--SAIQKHLKsKTVLFITHQLqylaD-----CDEVIFMKEGCITERGTHEEL 749
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDllKDINRELG-LTIVLITHEM----DvvrriCDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
554-744 |
2.29e-15 |
|
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: 76.49 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTF------------AYVAQQAWILNATLRDN 621
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrrigALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILF---GKEFDEERYNSVLNSCCLRpdlailpnsdlTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAhV 698
Cdd:cd03268 93 LRLlarLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP-D 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1814750642 699 GNHIFNSAIQKHLKS-KTVLFITHQLQYLAD-CDEVIFMKEGCITERG 744
Cdd:cd03268 161 GIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1188-1410 |
2.89e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 76.99 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGVRIS----DI-GLADLRSKLSIIPQEPVLFSgt 1262
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVL-------LETIAGFIKPDSGKILlngkDItNLPPEKRDISYVPQNYALFP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1263 vrsnldpfNQYTEDQIWDALE-RTHMKEciaqlplKLESEVME-------------NGDNFSVGERQLLCIARALLRHCK 1328
Cdd:cd03299 85 --------HMTVYKNIAYGLKkRKVDKK-------EIERKVLEiaemlgidhllnrKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1329 ILILDEATAAMDTET-DLLIQE--TIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 1404
Cdd:cd03299 150 ILLLDEPFSALDVRTkEKLREElkKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAE 228
|
....*.
gi 1814750642 1405 FAAAEN 1410
Cdd:cd03299 229 FLGFNN 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
552-722 |
3.29e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.86 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 552 RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------------FAYVAQQAWILNA-T 617
Cdd:TIGR01189 10 RGERMLFeGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFGKEFDEERYNSVLNScclrpdlailpnsdLTEIGERG------ANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTIEDA--------------LAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|..
gi 1814750642 692 SALDAHvGNHIFNSAIQKHL-KSKTVLFITHQ 722
Cdd:TIGR01189 156 TALDKA-GVALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
543-742 |
4.01e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 543 GKHTHlgnlrlQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG----------------TFAY 606
Cdd:PRK10419 20 GKHQH------QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 607 VAQQA-----------WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteiGERGANLSGGQRQRISLA 675
Cdd:PRK10419 94 VFQDSisavnprktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL----------DKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 676 RALYSDRDIYILDDPLSALDAHVGNHIFnsAIQKHLKSKT---VLFITHQL---QYLadCDEVIFMKEGCITE 742
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVI--RLLKKLQQQFgtaCLFITHDLrlvERF--CQRVMVMDNGQIVE 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
550-738 |
4.17e-15 |
|
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: 74.78 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 NLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYVA----QQA 611
Cdd:cd03215 9 GLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 612 WILNATLRDNILfgkefdeerynsvlnscclrpdLAILpnsdlteigerganLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:cd03215 89 LVLDLSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1814750642 692 SALDahVG--NHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEG 738
Cdd:cd03215 133 RGVD--VGakAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1172-1396 |
4.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.53 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLV---ELSGGCIKIDGVRISDIGLADLRSK 1248
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQepvlfsgtvrsnlDPFNQY----TEDQIWDALE-----RTHMKECIAQLplkLESEVMEN-----GDNFSVGER 1314
Cdd:PRK13640 86 VGIVFQ-------------NPDNQFvgatVGDDVAFGLEnravpRPEMIKIVRDV---LADVGMLDyidsePANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1315 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1392
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
....
gi 1814750642 1393 LLSN 1396
Cdd:PRK13640 230 IFSK 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
559-749 |
4.62e-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: 76.19 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSIlgqmSLLE----GSIAVNGTfaYVAQQAWILNAtLRDNIlfGKEFdeERYN 634
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCI----NLLEepdsGTITVDGE--DLTDSKKDINK-LRRKV--GMVF--QQFN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 635 -----SVLNSCCLRPdlaI----LPNSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:COG1126 88 lfphlTVLENVTLAP---IkvkkMSKAEAEERAMEllervGladkadaypAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 692 SALD----AHVGNHIfnsaiqKHLKSK--TVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:COG1126 165 SALDpelvGEVLDVM------RDLAKEgmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
561-744 |
4.69e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 75.67 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 561 DLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------FAYVAQQAWIL-NATLRDNILFG--- 625
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 ----KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:TIGR01277 98 glklNAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1814750642 702 IFnsAIQKHL---KSKTVLFITHQLQYLAD-CDEVIFMKEGCITERG 744
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
557-752 |
5.97e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.45 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-TFAYVAQQAWILNA-----------TLRDNILF 624
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 GkefdeerynsvlnsccLRpdLAILPNSD-------------LTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDP 690
Cdd:PRK09452 110 G----------------LR--MQKTPAAEitprvmealrmvqLEEFAQRKpHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 691 LSALDahvgnHIFNSAIQ---KHLKSK---TVLFITH-QLQYLADCDEVIFMKEGCITERGT----HEELMNL 752
Cdd:PRK09452 172 LSALD-----YKLRKQMQnelKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTpreiYEEPKNL 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1188-1392 |
6.46e-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: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRS-KLSIIPQ--------- 1254
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRArHVGFVFQsfqllptlt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1255 --EPVLFSGTVRSNLDPFNQYTEdqiwdALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1332
Cdd:COG4181 107 alENVMLPLELAGRRDARARARA-----LLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1333 DEATAAMDTET-----DLLIQETiREAFAdcTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1392
Cdd:COG4181 171 DEPTGNLDAATgeqiiDLLFELN-RERGT--TLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1175-1395 |
6.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLPL-VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1253
Cdd:PRK13642 8 ENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1254 QEP-VLFSGTVRSNLDPFNQytEDQiwdALERTHMKECI--AQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKIL 1330
Cdd:PRK13642 88 QNPdNQFVGATVEDDVAFGM--ENQ---GIPREEMIKRVdeALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1331 ILDEATAAMD----TETDLLIQEtIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 1395
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHE-IKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
554-735 |
7.36e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.28 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI-----AVNGTFA---YVAQQAWILN-ATLRDNILF 624
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkPVEGPGAergVVFQNEGLLPwRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 GKEF----DEERYNSVLnscclrpdlAILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVG 699
Cdd:PRK11248 94 GLQLagveKMQRLEIAH---------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1814750642 700 NHIFNSAIQK-HLKSKTVLFITHqlqylaDCDEVIFM 735
Cdd:PRK11248 165 EQMQTLLLKLwQETGKQVLLITH------DIEEAVFM 195
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
544-751 |
7.75e-15 |
|
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: 76.43 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 544 KHTHLGNLRLQrtlyNIDLEIEEGKLVGICGSVGSGKTSLISSILgQMSLLEGSIAVNG-------------TFAYVAQQ 610
Cdd:cd03289 11 KYTEGGNAVLE----NISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 611 AWILNATLRDNI-LFGKEFDEERYNsVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDD 689
Cdd:cd03289 86 VFIFSGTFRKNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 690 PLSALDAhVGNHIFNSAIQKHLKSKTVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03289 165 PSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
554-750 |
8.72e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 8.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWI-LNATLR 619
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLsFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGKEFDEERYN-------SVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:PRK09536 96 QVVEMGRTPHRSRFDtwtetdrAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 693 ALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELM 750
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1188-1397 |
9.10e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.96 E-value: 9.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVL-FSGTVRS- 1265
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 ---NLDPFNQ-YTEDQ--IWDALERThmkECIA-------QLplklesevmengdnfSVGERQLLCIARAL--LRHC--- 1327
Cdd:PRK13548 97 vamGRAPHGLsRAEDDalVAAALAQV---DLAHlagrdypQL---------------SGGEQQRVQLARVLaqLWEPdgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1328 -KILILDEATAAMdtetDLLIQETIreafadctmLTIAHR------------LH----TVLGSDRIMVLAQGQVVEFDTP 1390
Cdd:PRK13548 159 pRWLLLDEPTSAL----DLAHQHHV---------LRLARQlaherglavivvLHdlnlAARYADRIVLLHQGRLVADGTP 225
|
....*..
gi 1814750642 1391 SVLLSND 1397
Cdd:PRK13548 226 AEVLTPE 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1138-1415 |
9.42e-15 |
|
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: 79.99 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1138 SVERINHYIKTLSLEaPARIKNKSPSsdwPQEG-EVTFENAEMRYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLG 1216
Cdd:TIGR00957 606 SLKRLRIFLSHEELE-PDSIERRTIK---PGEGnSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLL 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1217 MALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPL 1296
Cdd:TIGR00957 682 SALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPS 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1297 KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI---REAFADCTMLTIAHRLHTVLGS 1373
Cdd:TIGR00957 749 GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQV 828
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1814750642 1374 DRIMVLAQGQVVEFDTPSVLLSNDSS--RFYAMFAAAENKIAVK 1415
Cdd:TIGR00957 829 DVIIVMSGGKISEMGSYQELLQRDGAfaEFLRTYAPDEQQGHLE 872
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
604-751 |
1.32e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.69 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 604 FAYVAQQAWILNATLRDNILFGKE-FDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDR 682
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 683 DIYILDDPLSALDAHVGNHIFNSAIQ-KHLKSKTVLFITHQLQYLADCDEVIFM----KEGCITE-RGTHEELMN 751
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTIVDiKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLS 1452
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
559-751 |
1.59e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 75.26 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------FAYVAQQ------------------AWIL 614
Cdd:COG4167 31 PVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdYKYRCKHirmifqdpntslnprlniGQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 615 NATLRDNILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:COG4167 111 EEPLRLNTDLTAEEREERIFATLRLVGLLPEHAnFYPHM-----------LSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 694 LDAHVGNHIFN--SAIQKHLKSKTVlFITHQLQYLADC-DEVIFMKEGCITERGTHEELMN 751
Cdd:COG4167 180 LDMSVRSQIINlmLELQEKLGISYI-YVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1188-1386 |
1.63e-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: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKLSIIPQE-PVLFSG-- 1261
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 TVRSNL-DPFNQYTEdqiwdaLERTHMKECIAQL--PLKLESEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEATA 1337
Cdd:TIGR02769 106 TVRQIIgEPLRHLTS------LDESEQKARIAELldMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1338 AMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:TIGR02769 180 NLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
885-1142 |
1.97e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 75.66 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 885 KDNPLMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVR 964
Cdd:cd07346 33 GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 965 LPFQAEMFIQNVILVFFCVGMIAgVFPW--FLVAVGPLIILFSILHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLAT 1042
Cdd:cd07346 113 VSSGLLQLLSDVLTLIGALVILF-YLNWklTLVALLLLPLYVLILRYFRR-RIRKASREVRESLAELSAFLQESLSGIRV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1043 IHAYKKGQEFLHRYQELLDNNQRpffLFTCAMRWLAvrLDLISIALITTTGLMIVL-------MHGQIPPAYAGLAISYA 1115
Cdd:cd07346 191 VKAFAAEEREIERFREANRDLRD---ANLRAARLSA--LFSPLIGLLTALGTALVLlyggylvLQGSLTIGELVAFLAYL 265
|
250 260
....*....|....*....|....*..
gi 1814750642 1116 VQLTGLFQFTVRLASETEARFTSVERI 1142
Cdd:cd07346 266 GMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
560-738 |
2.02e-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: 73.85 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 560 IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---------TFAYVAQQAWI-LNATLRDNILF----- 624
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVYlaqlk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 --GKEFDEERYNSVLNscclRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRDIYILDDPLSALDAhVGNHI 702
Cdd:cd03269 99 glKKEEARRRIDEWLE----RLELSEYANKRVEE-------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVEL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1814750642 703 FNSAIQKHL-KSKTVLFITHQLQYLAD-CDEVIFMKEG 738
Cdd:cd03269 167 LKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
555-751 |
2.11e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.47 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------------TFAYVAQQawILN 615
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkkvglVFQYPEYQ--LFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 616 ATLRDNILFGK----EFDEERYNSVLNSCclrpDLAILPNSDLTEigERGANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:PRK13637 99 ETIEKDIAFGPinlgLSEEEIENRVKRAM----NIVGLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 692 SALDAHVGNHIFNSAIQKHLKSK-TVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1188-1383 |
2.29e-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: 74.01 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI-------KIDGVRISDIGLADLRSK--------LSII 1252
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1253 PQ--------EPVLFSGTVRsnldpfnQYTEDQIWDALERTHMKECIAQLPLKlesevmengdNFSVGERQLLCIARALL 1324
Cdd:COG4778 106 PRvsaldvvaEPLLERGVDR-------EEARARARELLARLNLPERLWDLPPA----------TFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1325 RHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQ 1383
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
572-749 |
2.51e-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: 75.99 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 572 ICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-FAYVAQ---------QAWIL--NATLRDNILFG----KEFDEERYNS 635
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdVTNVPPhlrhinmvfQSYALfpHMTVEENVAFGlkmrKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 636 VLnscclrpdlAILPNSDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNS--AIQKHLk 712
Cdd:TIGR01187 81 VL---------EALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLElkTIQEQL- 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 1814750642 713 SKTVLFITH-QLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:TIGR01187 151 GITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1174-1396 |
2.59e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.12 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1174 FENAEmryQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLRSKLSII 1252
Cdd:PRK13633 14 YESNE---ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1253 PQEP------------VLFSgtvRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIA 1320
Cdd:PRK13633 91 FQNPdnqivativeedVAFG---PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1321 RALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1188-1411 |
2.64e-14 |
|
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: 78.41 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLFSGTVRSNL 1267
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1268 DPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDlli 1347
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE--- 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1348 qetiREAFADCTMLTIAHRlhtvlgsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENK 1411
Cdd:TIGR01271 585 ----KEIFESCLCKLMSNK-------TRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
557-752 |
2.91e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFayvaqqAWIL--------NATLRDNILFG--- 625
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALLelgagfhpELTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 ----KEFDEERYNSVLnscclrpdlailpnsDLTEIGE------RgaNLSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 696 AHvgnhiFN----SAIQKHLKS-KTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMNL 752
Cdd:COG1134 179 AA-----FQkkclARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
557-738 |
4.15e-14 |
|
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: 70.94 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAV--NGTFAYVAQqawilnatlrdnilfgkefdeeryn 634
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 635 svlnscclrpdlailpnsdlteigerganLSGGQRQRISLARALYSDRDIYILDDPLSALDahvgnhIFN-SAIQKHLKS 713
Cdd:cd03221 71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD------LESiEALEEALKE 115
|
170 180
....*....|....*....|....*....
gi 1814750642 714 --KTVLFITHQlQYLAD--CDEVIFMKEG 738
Cdd:cd03221 116 ypGTVILVSHD-RYFLDqvATKIIELEDG 143
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
560-744 |
4.25e-14 |
|
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: 73.17 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 560 IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAY-----VAQQAWILNA--------TLRDNILF-- 624
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkepaeARRRLGFVSDstglydrlTARENLEYfa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 ------GKEFdEERYNSVlnscclrpdlailpnSDLTEIGE----RGANLSGGQRQRISLARALYSDRDIYILDDPLSAL 694
Cdd:cd03266 104 glyglkGDEL-TARLEEL---------------ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 695 DAHVGNHIFNsaIQKHLKS--KTVLFITHQLQYLAD-CDEVIFMKEGCITERG 744
Cdd:cd03266 168 DVMATRALRE--FIRQLRAlgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1185-1405 |
4.30e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.23 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1185 LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS----KLSIIPQEPVLFS 1260
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1261 G-TVRSNldpfNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1339
Cdd:PRK10070 120 HmTVLDN----TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1340 D--TETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMF 1405
Cdd:PRK10070 196 DplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1188-1386 |
4.64e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRISDIGLADLRSKLSIIPQEP------ 1256
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1257 VLFS----GTVRSNLDPFNQYTEDQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILIL 1332
Cdd:PRK14247 98 SIFEnvalGLKLNRLVKSKKELQERVRWALEK-------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1333 DEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVE 1386
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1191-1385 |
5.29e-14 |
|
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: 72.71 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1191 KVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLSIIPQEPVLFSG-TVRS 1265
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NL--------DPFNQYTEDQIWDALERTHMKEciaQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 1337
Cdd:cd03297 95 NLafglkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1338 AMDTETDLLIQETIREAFAD--CTMLTIAHRLHTV-LGSDRIMVLAQGQVV 1385
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1188-1386 |
5.79e-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: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLVEL----SGGCIKIDGVRISDI---GLADLRSKLSIIPQEPVLFS 1260
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINLlerpTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1261 G-TVRSNldpfnqytedqiwdalerthmkecIAqLPLKL--------ESEVME---------NGDNF----SVGERQLLC 1318
Cdd:COG1135 96 SrTVAEN------------------------VA-LPLEIagvpkaeiRKRVAEllelvglsdKADAYpsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1319 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETtrsilDLL--KDINREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
557-751 |
6.05e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.46 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAY----------VAQQAWILNATLRDNILFgK 626
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 627 EFDEERYNSVLNSCCLRPDLAI-LPNSDLTE----------IGERG-----ANLSGGQRQRISLARALYSDRDIYILDDP 690
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVLgLSKQEAREravkylakvgIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 691 LSALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLADC-DEVIFMKEGCITERGTHEELMN 751
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1184-1410 |
6.97e-14 |
|
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: 73.74 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1184 NLPL----VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLF 1259
Cdd:cd03291 44 NLCLvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1260 SGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1339
Cdd:cd03291 111 PGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1340 DTETDlliqetiREAFADCTMLTIAHRlhtvlgsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1410
Cdd:cd03291 191 DVFTE-------KEIFESCVCKLMANK-------TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
550-752 |
7.58e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 NLRLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYV----AQQA 611
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVpedrKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 612 WILNATLRDNILFGkefdeeRYNSVLNSCCLRP------------DLAILPNSDLTEIGergaNLSGGQRQRISLARALY 679
Cdd:COG1129 341 LVLDLSIRENITLA------SLDRLSRGGLLDRrreralaeeyikRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 680 SDRDIYILDDPLSALDahVGNHifnSAIQKHLKS-----KTVLFITHQLQ-YLADCDEVIFMKEGCIT-----ERGTHEE 748
Cdd:COG1129 411 TDPKVLILDEPTRGID--VGAK---AEIYRLIRElaaegKAVIVISSELPeLLGLSDRILVMREGRIVgeldrEEATEEA 485
|
....
gi 1814750642 749 LMNL 752
Cdd:COG1129 486 IMAA 489
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1172-1405 |
8.69e-14 |
|
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: 72.27 E-value: 8.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrsklsi 1251
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVlfsGTVRSNLDPFNQYT-EDQIWDALERTHMKECI------AQLPL-KLESEVMENGDNFSVGERQLLCIARAL 1323
Cdd:cd03300 69 PHKRPV---NTVFQNYALFPHLTvFENIAFGLRLKKLPKAEikervaEALDLvQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1324 LRHCKILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEF 1387
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELK-------------RLQKELGitfvfvthdqeealtmSDRIAVMNKGKIQQI 212
|
250
....*....|....*...
gi 1814750642 1388 DTPSVLLSNDSSRFYAMF 1405
Cdd:cd03300 213 GTPEEIYEEPANRFVADF 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
664-751 |
9.78e-14 |
|
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: 75.88 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 664 LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFN--SAIQK--HLkskTVLFITHQLQ---YLadCDEVIFMK 736
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDllRDLQRehGL---AYLFISHDLAvvrAL--AHRVMVMK 500
|
90
....*....|....*
gi 1814750642 737 EGCITERGTHEELMN 751
Cdd:COG4172 501 DGKVVEQGPTEQVFD 515
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
885-1125 |
1.02e-13 |
|
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: 73.58 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 885 KDNPLMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvr 964
Cdd:cd18544 35 GDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 965 lpfqAEMFIQNVILVFFCVGMIAGVF----------PWFLVAVGPLIILFSILH-IVSRVLIRELKRLdnitqspfLSHI 1033
Cdd:cd18544 112 ----NELFTSGLVTLIGDLLLLIGILiamfllnwrlALISLLVLPLLLLATYLFrKKSRKAYREVREK--------LSRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1034 TS----SIQGLATIHAYKKGQEFLHRYQELldnNQRpffLFTCAMRwlAVRLDLI---SIALITTTGLMIVLMHGqippa 1106
Cdd:cd18544 180 NAflqeSISGMSVIQLFNREKREFEEFDEI---NQE---YRKANLK--SIKLFALfrpLVELLSSLALALVLWYG----- 246
|
250
....*....|....*....
gi 1814750642 1107 yAGLAISYAVQLTGLFQFT 1125
Cdd:cd18544 247 -GGQVLSGAVTLGVLYAFI 264
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
559-751 |
1.13e-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: 72.19 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTF--------------AYVAQQAWIL-NATLRDNIL 623
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarlgiGYLPQEASIFrKLTVEENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 -------FGKEFDEERYNSVLNscclrpDLAILPNSDlteigERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:cd03218 98 avleirgLSKKEREEKLEELLE------EFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 697 hvgnhIFNSAIQ---KHLKSKTV-LFIT-HQL-QYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03218 167 -----IAVQDIQkiiKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1183-1384 |
1.47e-13 |
|
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: 70.54 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1183 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPqepvl 1258
Cdd:cd03215 8 RGLsvKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDA-IRAGIAYVP----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1259 fsgtvrsnldpfnqytEDqiwdaleRTHMKeciaqlpLKLESEVMEN---GDNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:cd03215 82 ----------------ED-------RKREG-------LVLDLSVAENialSSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1336 TAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQV 1384
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1188-1400 |
1.83e-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: 71.42 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLaDLRSKLSII--PQEPVLFSG-TVR 1264
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGylPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLDPFNQYTEDQIWDALERThmKECIAQLplKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1344
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEKL--EELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1345 LLIQETIREaFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1400
Cdd:cd03218 170 QDIQKIIKI-LKDRGIgvLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
550-721 |
1.96e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 NLRLQ---RTLY-NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG--TFAYVAQQAWIL-NATLRDNI 622
Cdd:COG0488 3 NLSKSfggRPLLdDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDdDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFG-KEFDE--ERYNSVLNSCCLRPDLAILPNSDLTEIGERGA--------------------------NLSGGQRQRIS 673
Cdd:COG0488 83 LDGdAELRAleAELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 674 LARALYSDRDIYILDDPLSALDAHvgnhifnsAIQ---KHLKS--KTVLFITH 721
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLE--------SIEwleEFLKNypGTVLVVSH 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1189-1388 |
2.04e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRI--SDIGLADLRSKLSIIPQEPVLFSG 1261
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 TVRSNLD---PFNQYTEDQIWDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 1338
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1339 MDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1388
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1188-1387 |
2.29e-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: 70.68 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSIIPQEPVLFSG-TVRSN 1266
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LDPFNqytedqiwdALERTHMKECIAQLPLKLESEVMENGDN-----FSVGERQLLCIARALLRHCKILILDEATAAMDT 1341
Cdd:cd03264 93 LDYIA---------WLKGIPSKEVKARVDEVLELVNLGDRAKkkigsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1814750642 1342 ETDLLIQETIREAFADCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF 1387
Cdd:cd03264 164 EERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
554-751 |
2.60e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.27 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------FAYVAQQAWIL---NA-----TLR 619
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAKRLAILrqeNHinsrlTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGkefdeeRYnsvlnscclrP---------DLAILPNS----DLTEIGERGAN-LSGGQRQRISLARALYSDRDIY 685
Cdd:COG4604 94 ELVAFG------RF----------PyskgrltaeDREIIDEAiaylDLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 686 ILDDPLSALDahvgnhIFNS-AIQKHLKS------KTVLFITHQLQYlADC--DEVIFMKEGCITERGTHEELMN 751
Cdd:COG4604 158 LLDEPLNNLD------MKHSvQMMKLLRRladelgKTVVIVLHDINF-ASCyaDHIVAMKDGRVVAQGTPEEIIT 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1189-1405 |
4.21e-13 |
|
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: 71.14 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS----KLSIIPQEPVLFSG-TV 1263
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSNLdPF--------NQYTEDQIWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:cd03294 120 LENV-AFglevqgvpRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1336 TAAMDTetdlLIQETIREAFADC------TMLTIAHRLHTV--LGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMF 1405
Cdd:cd03294 188 FSALDP----LIRREMQDELLRLqaelqkTIVFITHDLDEAlrLG-DRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
557-733 |
4.37e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNATLRDNIL 623
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 F-----GKEFDEERynsvlnsccLRPDLAI--LPNSDLTEigeRGANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:PRK10247 103 FpwqirNQQPDPAI---------FLDDLERfaLPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1814750642 697 HvGNHIFNSAIQKHLKSK--TVLFITHQLQYLADCDEVI 733
Cdd:PRK10247 171 S-NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
557-751 |
4.71e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.37 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTS---LISSILGQMSLLEGSIAVNGTfAYVAQQAW----------------ILNAT 617
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGI-TLTAKTVWdirekvgivfqnpdnqFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFGKEfdeerynsvlNSCCLRPDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:PRK13640 102 VGDDVAFGLE----------NRAVPRPEMIKIVRDVLADVGmldyidSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 692 SALDAHVGNHIFNsaIQKHLKSK---TVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK13640 172 SMLDPAGKEQILK--LIRKLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
557-744 |
4.90e-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: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGtfayvaQQAWIL--------NATLRDNILFG--- 625
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLglgggfnpELTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 ----KEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAH 697
Cdd:cd03220 112 lglsRKEIDEKIDEII---------------EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 698 vgnhiFNSAIQKHL-----KSKTVLFITHQLQYLAD-CDEVIFMKEGCITERG 744
Cdd:cd03220 177 -----FQEKCQRRLrellkQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1162-1386 |
5.02e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1162 PSSDWPQEGEV-TFENAEMRYQENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---- 1234
Cdd:PRK10261 2 PHSDELDARDVlAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1235 ------VRISDIGLADLR----SKLSIIPQEPVlfsgtvrSNLDPFNQYTEdQIWDALeRTHM----KECIAQLPLKL-- 1298
Cdd:PRK10261 82 rrsrqvIELSEQSAAQMRhvrgADMAMIFQEPM-------TSLNPVFTVGE-QIAESI-RLHQgasrEEAMVEAKRMLdq 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1299 ----ESEVM--ENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTV 1370
Cdd:PRK10261 153 vripEAQTIlsRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVV 232
|
250
....*....|....*..
gi 1814750642 1371 LG-SDRIMVLAQGQVVE 1386
Cdd:PRK10261 233 AEiADRVLVMYQGEAVE 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1192-1396 |
5.17e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLSIIPQEPvLFSGTVRSNL- 1267
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1268 ----DPFNQYTEDqiwdaLERTHMKECIAQLPLK---LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1340
Cdd:PRK15079 119 eiiaEPLRTYHPK-----LSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1341 TETDL----LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:PRK15079 194 VSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
557-751 |
5.55e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.12 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSI--LGQMS---LLEGSIAVNGTFA----------YVAQQAWIL-NATLRD 620
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdLIVDGLKVNDPKVderlirqeagMVFQQFYLFpHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFG--------KEFDEERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:PRK09493 97 NVMFGplrvrgasKEEAEKQARELLAKVGLAERAHHYP-----------SELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 693 ALDAHVGNHIFNsaIQKHLKSK--TVLFITHQLQYLADC-DEVIFMKEGCITERGTHEELMN 751
Cdd:PRK09493 166 ALDPELRHEVLK--VMQDLAEEgmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1180-1395 |
5.95e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1180 RYQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL-----VELSGGCIKIDGVRISDIGLADLR----SKLS 1250
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1251 IIPQEPVLfsgtvrsNLDPFNQyTEDQIWDALE----------RTHMKEC-----IAQLPLKLEsevmENGDNFSVGERQ 1315
Cdd:PRK15134 96 MIFQEPMV-------SLNPLHT-LEKQLYEVLSlhrgmrreaaRGEILNCldrvgIRQAAKRLT----DYPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1316 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSV 1392
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLSIVRKlADRVAVMQNGRCVEQNRAAT 243
|
...
gi 1814750642 1393 LLS 1395
Cdd:PRK15134 244 LFS 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1188-1386 |
7.36e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.79 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS----GGCIKIDGVRISDIGLADLR----SKLSIIPQEPVlf 1259
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1260 sgtvrSNLDPFnqYT-EDQIW-------------------DALERTHMKE---CIAQLPLKLesevmengdnfSVGERQL 1316
Cdd:COG4172 103 -----TSLNPL--HTiGKQIAevlrlhrglsgaaararalELLERVGIPDperRLDAYPHQL-----------SGGQRQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1317 LCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIREAfadctMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVqaqilDLLkdLQRELGMA-----LLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
559-749 |
7.43e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.98 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------FAYVAQQ-AWILNATLRDNILFG- 625
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergVGMVFQSyALYPHLSVAENMSFGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 ------KEFDEERYNSVLnscclrpdlAILPNSDLTEigERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDA--H 697
Cdd:PRK11000 101 klagakKEEINQRVNQVA---------EVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 698 VGNHIFNSAIQKHLKSkTVLFITH-QLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:PRK11000 170 VQMRIEISRLHKRLGR-TMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
559-751 |
7.53e-13 |
|
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: 69.77 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG------------------TFayvaQQAWIL-NATLR 619
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiarlgigrTF----QIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGKEFDEERYNSVLNSCCLRPDL-----AILpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRDIYILDDP 690
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 691 LSALD----AHVGNHIfnsaiqKHLKSK--TVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:cd03219 171 AAGLNpeetEELAELI------RELRERgiTVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
557-740 |
7.70e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.22 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISsILGQMSLlegsiAVNGTFAYVAQQAWILN----ATLRDNiLFGKEFdeER 632
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDK-----PTSGTYRVAGQDVATLDadalAQLRRE-HFGFIF--QR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 633 YNsvlnsccLRPDLAILPNSDLTEI----------------------GER----GANLSGGQRQRISLARALYSDRDIYI 686
Cdd:PRK10535 95 YH-------LLSHLTAAQNVEVPAVyaglerkqrllraqellqrlglEDRveyqPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 687 LDDPLSALDAHVGNHIFnsAIQKHLKSK--TVLFITHQLQYLADCDEVIFMKEGCI 740
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1172-1386 |
7.71e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.37 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGVRI---SDIGL 1242
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLlerpTSGRVLVDGQDLtalSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1243 ADLRSKLSIIPQEPVLFSG-TVRSNldpfnqytedqiwdalerthmkecIAqLPLKL--------ESEVMENGD------ 1307
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSSrTVFDN------------------------VA-LPLELagtpkaeiKARVTELLElvglsd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1308 -------NFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIreafaDCTMLTIAHRLHTVLG- 1372
Cdd:PRK11153 133 kadrypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRi 207
|
250
....*....|....
gi 1814750642 1373 SDRIMVLAQGQVVE 1386
Cdd:PRK11153 208 CDRVAVIDAGRLVE 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1183-1388 |
8.18e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1183 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDI------GLA----DlRSK 1248
Cdd:COG1129 260 EGLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPrdairaGIAyvpeD-RKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQEPVLFSGTVrSNLDPFNQYTedQIWDALERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLR 1325
Cdd:COG1129 339 EGLVLDLSIRENITL-ASLDRLSRGG--LLDRRRERALAEEYIKRLRIKtpsPEQPVG----NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1326 HCKILILDEATAAMD----TEtdllIQETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 1388
Cdd:COG1129 412 DPKVLILDEPTRGIDvgakAE----IYRLIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIVgELD 477
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
557-751 |
8.23e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-----------------TFAYVAQ--QAWILNAT 617
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFG-KEFdeerynsvlnscclrpdlailpNSDLTEIGERGANL------------------SGGQRQRISLARAL 678
Cdd:PRK13646 103 VEREIIFGpKNF----------------------KMNLDEVKNYAHRLlmdlgfsrdvmsqspfqmSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 679 YSDRDIYILDDPLSALDAHVGNHIFNSAIQKHLK-SKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
557-745 |
9.16e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.37 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSIlgqmSLLE----GSIAVNGT----------------FAYVAQQAWILNA 616
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGQdltalsekelrkarrqIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 -TLRDNILF-------GKEFDEERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRDI 684
Cdd:PRK11153 97 rTVFDNVALplelagtPKAEIKARVTELL---------------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 685 YILDDPLSALDAHVGNHIFN--SAIQKHLKSkTVLFITHQLQYLAD-CDEVIFMKEGCITERGT 745
Cdd:PRK11153 162 LLCDEATSALDPATTRSILEllKDINRELGL-TIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1172-1396 |
9.69e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI----SDIGLAD 1244
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1245 LRSKLSIIPQ--EPVLFSGTVRSNLD--PFN-QYTEDQiwdalERTHMKECIAQLPLkleSEVMENGDNF--SVGERQLL 1317
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKNfGFSEDE-----AKEKALKWLKKVGL---SEDLISKSPFelSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1318 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1391
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPK 230
|
....*
gi 1814750642 1392 VLLSN 1396
Cdd:PRK13641 231 EIFSD 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
554-744 |
1.11e-12 |
|
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: 68.76 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGkLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG------------TFAYVAQQ-AWILNATLRD 620
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NIlfgkefdeeRYNSVLNSC----CLRPDLAILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:cd03264 92 FL---------DYIAWLKGIpskeVKARVDEVLELVNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 696 ahVGNHI-FNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERG 744
Cdd:cd03264 163 --PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
559-749 |
1.16e-12 |
|
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: 70.47 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGqmsLLE------GSIAVNGT-----------------FAYVAQQA---- 611
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILG---LLPppgitsGEILFDGEdllklsekelrkirgreIQMIFQDPmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 612 -------WILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAIL---PNsdlteigergaNLSGGQRQRISLARALYSD 681
Cdd:COG0444 100 npvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 682 RDIYILDDPLSALDAHVGNHIFN--SAIQKHLKSkTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAQILNllKDLQRELGL-AILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEEL 238
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1172-1384 |
1.34e-12 |
|
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: 68.59 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 1248
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 LSIIPQEPVLFSG-TVRSNLDPFNQYTEDQIWDALERthMKECIAQLPLKLESEVMENGdnFSVGERQLLCIARALLRHC 1327
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKR--VPAALELVGLSHKHRALPAE--LSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1328 KILILDEATAAMDTET-----DLLiqETIREAFADCTMLTIAHRLHTVLgSDRIMVLAQGQV 1384
Cdd:cd03292 156 TILIADEPTGNLDPDTtweimNLL--KKINKAGTTVVVATHAKELVDTT-RHRVIALERGKL 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1189-1391 |
1.35e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.88 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLADLRSKLSIIPQEP--VLFSGTVR 1264
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLD--PFN-QYTEDQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEATAAMD- 1340
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1341 ---TETDLLIQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVEFDTPS 1391
Cdd:PRK13636 175 mgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPK 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1188-1394 |
1.54e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLAdlRSKLSIIPQEPVL-FSGTVRS 1265
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NLDPFNQYTedqiwdaleRTHMKECIAQLPLKLESEVMENGDNFSV-----GERQLLCIARALLRHCKILILDEATAAMD 1340
Cdd:PRK13536 134 NLLVFGRYF---------GMSTREIEAVIPSLLEFARLESKADARVsdlsgGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1341 TETDLLIQETIREAFA--DCTMLTI-----AHRLhtvlgSDRIMVLAQGQVVEFDTPSVLL 1394
Cdd:PRK13536 205 PHARHLIWERLRSLLArgKTILLTThfmeeAERL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1172-1399 |
1.62e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRsklsI 1251
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDER----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEpvlfSGTVRSNLDPFNQYTedqiwdALE---------RTHMKECIAQLPLKLESEV--MENGDNF----SVGERQL 1316
Cdd:PRK09493 75 IRQE----AGMVFQQFYLFPHLT------ALEnvmfgplrvRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1317 LCIARALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRL---HTVlGSdRIMVLAQGQVVEFDT 1389
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKvmQDLAEegMTMVIVTHEIgfaEKV-AS-RLIFIDKGRIAEDGD 219
|
250
....*....|
gi 1814750642 1390 PSVLLSNDSS 1399
Cdd:PRK09493 220 PQVLIKNPPS 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
260-749 |
1.63e-12 |
|
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: 71.75 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 260 SNDGQRMFEAAAVGSLLAGGPVIAILGMIYnVIILGPTGFLGSAVFI----LFYpaMMFVSRITAYFRRkcVTITDDRVQ 335
Cdd:COG4615 112 TEDVRTISQAFVRLPELLQSVALVLGCLAY-LAWLSPPLFLLTLVLLglgvAGY--RLLVRRARRHLRR--AREAEDRLF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 336 K-MNEVLTYIKFIKM--------YAwvKAFSQSVQKIREEERRmlekAGYFQSITVGVAPIVM--VIASVVTFSVHMtlg 404
Cdd:COG4615 187 KhFRALLEGFKELKLnrrrrrafFD--EDLQPTAERYRDLRIR----ADTIFALANNWGNLLFfaLIGLILFLLPAL--- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 405 FDLTAAQAFTVVTVF----NSMTFALKVTPfsvkSLSEASVAVDRFKSLFLMEEvhmiqkkPASPHITIEmknATLAWDS 480
Cdd:COG4615 258 GWADPAVLSGFVLVLlflrGPLSQLVGALP----TLSRANVALRKIEELELALA-------AAEPAAADA---AAPPAPA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 481 SHSSLQnspkltpktkkdkraargkkekVRQLqptEHQavlaeqkghllldsderpSPEEEEGKHTHLGNlrlqrtlynI 560
Cdd:COG4615 324 DFQTLE----------------------LRGV---TYR------------------YPGEDGDEGFTLGP---------I 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 561 DLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGtfAYVAQQAWilnATLRDNI--------LF------GK 626
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNR---EAYRQLFsavfsdfhLFdrllglDG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 627 EFDEERYNSVLNscclrpDLAIlpnSDLTEIgERGA----NLSGGQRQRISLARALYSDRDIYILD------DPlsalda 696
Cdd:COG4615 427 EADPARARELLE------RLEL---DHKVSV-EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDewaadqDP------ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 697 hVGNHIFNSAIQKHLKS--KTVLFITHQLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:COG4615 491 -EFRRVFYTELLPELKArgKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1172-1385 |
1.65e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQeNLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLG--MALFRLVElsGGCIKIDGVRISDIGLAdlRSKL 1249
Cdd:PRK10771 2 LKLTDITWLYH-HLPM---RFDLTVERGERVAILGPSGAGKSTLLnlIAGFLTPA--SGSLTLNGQDHTTTPPS--RRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1250 SIIPQEPVLFSG-TVRSN----LDP---FNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIAR 1321
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1322 ALLRHCKILILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
557-751 |
1.67e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.11 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIA------------------------------------- 599
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklviqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 600 ----VNGTFAYVAQQawILNATLRDNILFG-------KEFDEERYNSVLNSCCLrpDLAILPNSDLteigergaNLSGGQ 668
Cdd:PRK13651 103 irrrVGVVFQFAEYQ--LFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRSPF--------ELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 669 RQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQY-LADCDEVIFMKEGCITERG-TH 746
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGdTY 250
|
....*
gi 1814750642 747 EELMN 751
Cdd:PRK13651 251 DILSD 255
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
552-722 |
1.81e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 552 RLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNgtfayVAQQAWILNATLRDNILFGKEFDE 630
Cdd:COG2401 40 VVERYVLrDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 631 ERYnsVLNSCCLrpdlailpnSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALD---AHVGNHIFNSAI 707
Cdd:COG2401 115 AVE--LLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLA 183
|
170
....*....|....*
gi 1814750642 708 QKHlkSKTVLFITHQ 722
Cdd:COG2401 184 RRA--GITLVVATHH 196
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1146-1386 |
2.02e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1146 IKTLSLEAP-ARIKNKSPSSDWPQegeVTFENAEMRYQENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 1224
Cdd:PRK10522 299 LNKLALAPYkAEFPRPQAFPDWQT---LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1225 LSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTvrsnLDPFNQYTEDQIWDA-LERTHMKEciaqlplKLEsevM 1303
Cdd:PRK10522 375 PQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAH-------KLE---L 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1304 ENGD----NFSVGERQLLCIARALLRHCKILILDEATAAMDTE------TDLL--IQETIREAFAdctmltIAHRLHTVL 1371
Cdd:PRK10522 441 EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLplLQEMGKTIFA------ISHDDHYFI 514
|
250
....*....|....*
gi 1814750642 1372 GSDRIMVLAQGQVVE 1386
Cdd:PRK10522 515 HADRLLEMRNGQLSE 529
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1188-1396 |
2.15e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID------GVRISDIGLADLRSKLSIIPQEPVLFSG 1261
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 -TVRSNLD-PFNQYTedqIWDALE-RTHMKECIAQLPL--KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1336
Cdd:PRK14246 105 lSIYDNIAyPLKSHG---IKEKREiKKIVEECLRKVGLwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1337 AAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
557-759 |
2.61e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.97 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTfAYVAQQAWILN----------------ATLRD 620
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWNLRrkigmvfqnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGKEFDEERYNSVLNscclRPDLAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGN 700
Cdd:PRK13642 102 DVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 701 HIFNsaIQKHLKSK---TVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMNLNGDYATI 759
Cdd:PRK13642 178 EIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
555-756 |
2.70e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILG----------QMSLLEGSIAVNGTFA-----------YVAQQAWI 613
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirksrantgYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 614 LNA-TLRDNILFGKEFDEERYNSvlnscCLR---PDLAILPNSDLTEIG------ERGANLSGGQRQRISLARALYSDRD 683
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRT-----CFSwftREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 684 IYILDDPLSALDAHVGNHIFNSAIQ-KHLKSKTVLFITHQLQY-LADCDEVIFMKEGCITERGTHEELMNLNGDY 756
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFDH 247
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
562-820 |
3.02e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.45 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 562 LEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTfayvaQQAWILNATLRdnilfgkEFDEERYNSVLNSCC 641
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIAKISDAELR-------EVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 642 LRPDLAILPNSD--------------------LTEIG-ERGAN-----LSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:PRK10070 117 LMPHMTVLDNTAfgmelaginaeerrekaldaLRQVGlENYAHsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 696 AHVGNHIFNSAIQKHLK-SKTVLFITHQL-QYLADCDEVIFMKEGCITERGTHEELMN--LNGDYATIFNNLLLGETPPV 771
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNnpANDYVRTFFRGVDISQVFSA 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1814750642 772 EINSKKETSGSQKKTqdkcPKTGSVKKEKAVKPEEGQLVQMEEKGQGSV 820
Cdd:PRK10070 277 KDIARRTPNGLIRKT----PGFGPRSALKLLQDEDREYGYVIERGNKFV 321
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1192-1410 |
3.23e-12 |
|
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: 69.74 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLSIIPQEPVLFSG-TVRSN 1266
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFPHlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LdpfnQYTEDQIWDALERTHMKECIAQL---PLkLESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1343
Cdd:COG4148 98 L----LYGRKRAPRAERRISFDEVVELLgigHL-LDRRP----ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1344 -----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1410
Cdd:COG4148 169 kaeilPYL--ERLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGS 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
559-749 |
3.36e-12 |
|
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: 67.39 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG------------TFAYVAQQAWILNA-TLRDNI--- 622
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyih 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 --LFGKEFDE--ERYNSVLNSCclrpdlailpnsDLTEIGER-GANLSGGQRQRISLARALYSDRDIYILDDPLSALDAH 697
Cdd:cd03265 98 arLYGVPGAErrERIDELLDFV------------GLLEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 698 VGNHIFnSAIQKHLKSK--TVLFITHQLQYlAD--CDEVIFMKEGCITERGTHEEL 749
Cdd:cd03265 166 TRAHVW-EYIEKLKEEFgmTILLTTHYMEE-AEqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
559-738 |
3.37e-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: 67.53 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG----TFAYVAQQA-----------WILnaTLRDNIL 623
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQSlgycpqfdalfDEL--TVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 F-----GKEFDEERYNSvlnscclrpdLAILPNSDLTEIGERGA-NLSGGQRQRISLARALYSDRDIYILDDPLSALDAH 697
Cdd:cd03263 98 FyarlkGLPKSEIKEEV----------ELLLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1814750642 698 VGNHIFNsAIQKHLKSKTVLFITHQLQyLAD--CDEVIFMKEG 738
Cdd:cd03263 168 SRRAIWD-LILEVRKGRSIILTTHSMD-EAEalCDRIAIMSDG 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
554-749 |
3.39e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.89 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAV------NGT---------------FAYVAQQaw 612
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKknkklkplrkkvgivFQFPEHQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 613 ILNATLRDNILFG-------KEFDEERYNSVLNSCCLRPDLaiLPNSDLteigergaNLSGGQRQRISLARALYSDRDIY 685
Cdd:PRK13634 98 LFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEEL--LARSPF--------ELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 686 ILDDPLSALDAHVGNHIFNSAIQKHL-KSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
554-740 |
3.70e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRT-LYNIDLEIEEGKLVGICGSVGSGKTSLISSILG-----QMSLLEGSIAVngtfayvaqqawilnATLRDNILFgkE 627
Cdd:PRK11247 24 ERTvLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsAGELLAGTAPL---------------AEAREDTRL--M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 628 FDEER---YNSVLNSCCL------RPD-LAILPNSDLTE-IGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:PRK11247 87 FQDARllpWKKVIDNVGLglkgqwRDAaLQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1814750642 697 HVG---NHIFNSAIQKHlkSKTVLFITHQL-QYLADCDEVIFMKEGCI 740
Cdd:PRK11247 167 LTRiemQDLIESLWQQH--GFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
665-778 |
3.86e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.22 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 665 SGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFN--SAIQKHLKSKTVlFITHQL---QYLAdcDEVIFMKEGC 739
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNlmMDLQQELGLSYV-FISHDLsvvEHIA--DEVMVMYLGR 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1814750642 740 ITERGTHEelmnlngdyaTIFNN-------LLLGETPPVEINSKKE 778
Cdd:PRK11308 233 CVEKGTKE----------QIFNNprhpytqALLSATPRLNPDDRRE 268
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1188-1396 |
4.05e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGVRISD--IGLADLRSKLSIIPQEPVLFS 1260
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1261 GTVRSNLdpfnQYTEDQI-W------DALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILD 1333
Cdd:PRK14258 102 MSVYDNV----AYGVKIVgWrpkleiDDIVESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 1334 EATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVL-----------GSDRImvlaqGQVVEFDTPSVLLSN 1396
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrlsdftaffkgNENRI-----GQLVEFGLTKKIFNS 246
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1188-1400 |
4.14e-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: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEPVLFSG-TVRS 1265
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NLDPFNQYTEDQIWdaleRTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDL 1345
Cdd:PRK11614 100 NLAMGGFFAERDQF----QERIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1346 LIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1400
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
548-722 |
4.24e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 548 LGNLRLQRTLY-NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------------FAYVAQQAWI- 613
Cdd:PRK13538 7 LACERDERILFsGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrdeyhqdLLYLGHQPGIk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 614 --LNAtlrdnilfgkefdEE--RYNSVLnSCCLRPDLAIlpnSDLTEIGERG------ANLSGGQRQRISLARALYSDRD 683
Cdd:PRK13538 87 teLTA-------------LEnlRFYQRL-HGPGDDEALW---EALAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1814750642 684 IYILDDPLSALDAHvGNHIFNSAIQKHLKSK-TVLFITHQ 722
Cdd:PRK13538 150 LWILDEPFTAIDKQ-GVARLEALLAQHAEQGgMVILTTHQ 188
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1188-1400 |
4.32e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVL-FSGTVR-- 1264
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 ---------SNLDPFNQYTEDQIWDALERTHMKECIAQlPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:PRK09536 98 vemgrtphrSRFDTWTETDRAAVERAMERTGVAQFADR-PV----------TSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1336 TAAMDTETDLLIQETIRE-------AFADCTMLTIAHRLhtvlgSDRIMVLAQGQVVEFDTPSVLLSNDSSR 1400
Cdd:PRK09536 167 TASLDINHQVRTLELVRRlvddgktAVAAIHDLDLAARY-----CDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
557-742 |
5.22e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.00 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT----------------FAYVAQQAWIL-NATLR 619
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDFRLLpDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILF-----GKEFDE--ERYNSVLnscclrpdlailpnsDLTEIGERG----ANLSGGQRQRISLARALYSDRDIYILD 688
Cdd:COG2884 98 ENVALplrvtGKSRKEirRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 689 DPLSALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLADCDE-VIFMKEGCITE 742
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
548-695 |
5.71e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 548 LGNLRLQrtlynIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------------FAYVAQQ 610
Cdd:PRK11144 10 LGDLCLT-----VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 611 AWIL-NATLRDNILFG-KEFDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK11144 85 ARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMD 153
|
....*..
gi 1814750642 689 DPLSALD 695
Cdd:PRK11144 154 EPLASLD 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1192-1384 |
6.43e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE-LSGGCIKIDG--VRIS------DIGLADL---RSKLSIIPQEPVLF 1259
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRnpqqaiAQGIAMVpedRKRDGIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1260 SGTVrSNLDPFNQYTedQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAM 1339
Cdd:PRK13549 361 NITL-AALDRFTGGS--RIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1340 DT----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 1384
Cdd:PRK13549 437 DVgakyEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1189-1383 |
6.43e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDGVRISDIGLADL-RSKLSIIPQEPVLF 1259
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKV-----LSGvyphgtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1260 SG-TVRSNLDPFNQYTEDQI--WDALERtHMKECIAQLPLKL--ESEVMENGdnfsVGERQLLCIARALLRHCKILILDE 1334
Cdd:PRK13549 95 KElSVLENIFLGNEITPGGImdYDAMYL-RAQKLLAQLKLDInpATPVGNLG----LGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1335 ATAAM-DTETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 1383
Cdd:PRK13549 170 PTASLtESETAVLL-DIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
552-744 |
6.99e-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: 66.97 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 552 RLQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG----------------TFAYVAQQAWILN 615
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrkkflrrigvVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 616 AtlRDNILFGKE---FDEERYNSVLNSCClrpdlailpnsDLTEIGE------RgaNLSGGQRQRISLARALYSDRDIYI 686
Cdd:cd03267 112 V--IDSFYLLAAiydLPPARFKKRLDELS-----------ELLDLEElldtpvR--QLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 687 LDDPLSALDAHVGNHI--FNSAIQKhLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERG 744
Cdd:cd03267 177 LDEPTIGLDVVAQENIrnFLKEYNR-ERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1188-1388 |
7.20e-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: 66.40 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS---DIGLAdLRSKLSIIpqEPVLFSGTVR 1264
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSsllGLGGG-FNPELTGR--ENIYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLDPFNQYTEDQIWDALErthMKECIaQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1344
Cdd:cd03220 113 GLSRKEIDEKIDEIIEFSE---LGDFI-DLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1814750642 1345 LLIQETIREAFADCTMLTIA-HRLHTVLG-SDRIMVLAQGQVVEFD 1388
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
564-747 |
7.26e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 564 IEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGtfAYVAQQAWILNA---------------TLRDNIL-FGKE 627
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARArigvvpqfdnldlefTVRENLLvFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 628 FdeeRYNSvlnscclRPDLAILPNsdLTEIGE-------RGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGN 700
Cdd:PRK13536 142 F---GMST-------REIEAVIPS--LLEFARleskadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1814750642 701 HIFNSAIQKHLKSKTVLFITHQLQYlAD--CDEVIFMKEGC-ITERGTHE 747
Cdd:PRK13536 210 LIWERLRSLLARGKTILLTTHFMEE-AErlCDRLCVLEAGRkIAEGRPHA 258
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1175-1393 |
7.56e-12 |
|
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: 66.62 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDiglaDLRSKLSI 1251
Cdd:cd03265 4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvVREPR----EVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSG-TVRSNLdpfnqYTEDQIWdALERTHMKECIAQLpLKLeSEVMENGD----NFSVGERQLLCIARALLRH 1326
Cdd:cd03265 78 VFQDLSVDDElTGWENL-----YIHARLY-GVPGAERRERIDEL-LDF-VGLLEAADrlvkTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1327 CKILILDEATAAMDTETDLLIQETIR---EAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1393
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
559-749 |
7.72e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.83 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFayvaqqawiLNATLRDNI--LfgkefDEERynsv 636
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---------LDPEDRRRIgyL-----PEER---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 637 lnscCLRPDLAI------------LPNSDLT----------EIGERGA----NLSGGQRQRISLARALYSDRDIYILDDP 690
Cdd:COG4152 81 ----GLYPKMKVgeqlvylarlkgLSKAEAKrradewlerlGLGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 691 LSALDAhVGNHIFNSAIQKHLKS-KTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:COG4152 157 FSGLDP-VNVELLKDVIRELAAKgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
557-749 |
8.12e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 8.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQM---SLLEGSIAVNGT----------FAYVAQQAWILNA-TLRDNI 622
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMpidakemraiSAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFGKEF--------DE--ERYNSVLNscclrpDLAILPNSDlTEIGERGA--NLSGGQRQRISLARALYSDRDIYILDDP 690
Cdd:TIGR00955 121 MFQAHLrmprrvtkKEkrERVDEVLQ------ALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 691 LSALDAHVGNHIFnsAIQKHL--KSKTVLFITHQLQYLADC--DEVIFMKEGCITERGTHEEL 749
Cdd:TIGR00955 194 TSGLDSFMAYSVV--QVLKGLaqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
549-722 |
8.25e-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: 64.87 E-value: 8.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 549 GNLRLQrtlyNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI---AVNGTFaYVAQQAWILNATLRDNIlfg 625
Cdd:cd03223 13 GRVLLK----DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmpEGEDLL-FLPQRPYLPLGTLREQL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 kefdeerynsvlnscclrpdlaILPNSDlteigergaNLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFnS 705
Cdd:cd03223 85 ----------------------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY-Q 132
|
170
....*....|....*..
gi 1814750642 706 AIQKHLksKTVLFITHQ 722
Cdd:cd03223 133 LLKELG--ITVISVGHR 147
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
557-721 |
1.02e-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: 65.89 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT---------FAYVAQQ--------AWILNATLR 619
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRKigvvfqdfRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGKEFDE-------ERYNSVLNSCCLRPDLAILPnsdlteigergANLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:cd03292 97 ENVAFALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*....
gi 1814750642 693 ALDAHVGNHIFNSAIQKHLKSKTVLFITH 721
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
555-751 |
1.04e-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: 69.06 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILG--QMSLLEGSIAVN------------------------GTFAYVA 608
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvgepcpvcgGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 609 QQAWILNATLRDN------ILFGKEF----DEERYNSVLNS---CCLRPDLAILPNSDLTE---IGER----GANLSGGQ 668
Cdd:TIGR03269 94 VDFWNLSDKLRRRirkriaIMLQRTFalygDDTVLDNVLEAleeIGYEGKEAVGRAVDLIEmvqLSHRithiARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 669 RQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQKHLKSKTVLFIT-HQLQYLAD-CDEVIFMKEGCITERGTH 746
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIEDlSDKAIWLENGEIKEEGTP 253
|
....*
gi 1814750642 747 EELMN 751
Cdd:TIGR03269 254 DEVVA 258
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1175-1396 |
1.12e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLplVLKKVSFTIkPKEKI-GIVGRTGSGKSSLGMALFRLVELSGGCiKIDGVRI--------SDIGLADL 1245
Cdd:PRK14243 14 ENLNVYYGSFL--AVKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1246 RSKLSIIPQEPVLFSGTVRSNLD---PFNQYTEDQiwDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARA 1322
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAygaRINGYKGDM--DELVERSLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1323 LLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLH---------------TVLGSDRimvlaQGQVVEF 1387
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQqaarvsdmtaffnveLTEGGGR-----YGYLVEF 240
|
....*....
gi 1814750642 1388 DTPSVLLSN 1396
Cdd:PRK14243 241 DRTEKIFNS 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
554-751 |
1.20e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.60 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSiLGQMSLLEGSIAVNGTFAYVAQQAWI----LNATLRD-NILFGKE- 627
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYErrvnLNRLRRQvSMVHPKPn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 628 -FDEERYNSVLNSCCL---RPDLAI-------LPNSDL-----TEIGERGANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:PRK14258 99 lFPMSVYDNVAYGVKIvgwRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 692 SALDAHVGNHIFNSAIQKHLKSK-TVLFITH---QLQYLADCDEVIFMKEGCIT---ERGTHEELMN 751
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSElTMVIVSHnlhQVSRLSDFTAFFKGNENRIGqlvEFGLTKKIFN 245
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
158-426 |
1.34e-11 |
|
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: 66.90 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 158 LILSIVCLMITQLAGFSGPaFVVKHLLE-YTQDTESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTM 236
Cdd:pfam00664 1 LILAILLAILSGAISPAFP-LVLGRILDvLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 237 AFKKILKLKNI--KEKSVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPT-GFLGSAVFILFYPAMM 313
Cdd:pfam00664 80 LFKKILRQPMSffDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 314 FVSRITAYFRRKCVTITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSITVGVAPIVMVIAS 393
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1814750642 394 VVT--FSVHMTLGFDLTAAQAFTVVTVFNSMTFAL 426
Cdd:pfam00664 240 ALAlwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1181-1351 |
1.41e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1181 YQENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFS 1260
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1261 GTVRSNLD-PFnqytedQIW-DALERTHMKECIAQLPLKlESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 1338
Cdd:PRK10247 95 DTVYDNLIfPW------QIRnQQPDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170
....*....|...
gi 1814750642 1339 MDTETDLLIQETI 1351
Cdd:PRK10247 168 LDESNKHNVNEII 180
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
516-740 |
1.54e-11 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 68.83 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 516 EHQAVLAEQKGHLLLDSDER-------------PSPEEEEGKHthlgnlrlqrtLYNIDLEIEEGKLVGICGSVGSGKTS 582
Cdd:TIGR01194 315 EPELELSDADNVLLLAHDKSvdsielkdvhmnpKAPEGSEGFA-----------LGPIDLRIAQGDIVFIVGENGCGKST 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 583 LISSILGQMSLLEGSIAVNGtfAYVAQQAW-----ILNATLRDNILFGK--EFDEERYNSVLNSCCLRPDLAILPNSDLT 655
Cdd:TIGR01194 384 LAKLFCGLYIPQEGEILLDG--AAVSADSRddyrdLFSAIFADFHLFDDliGPDEGEHASLDNAQQYLQRLEIADKVKIE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 656 EIG-ERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVgNHIFNSAIQKHLK--SKTVLFITHQLQYLADCDEV 732
Cdd:TIGR01194 462 DGGfSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAF-KRFFYEELLPDLKrqGKTIIIISHDDQYFELADQI 540
|
....*...
gi 1814750642 733 IFMKEGCI 740
Cdd:TIGR01194 541 IKLAAGCI 548
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1188-1403 |
1.60e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElsggciKIDGVRIS-DIGLA-----------DLRSKLSIIPQE 1255
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMND------KVSGYRYSgDVLLGgrsifnyrdvlEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1256 PVLFSGTVRSN---------LDPFNQY--------TEDQIWDALerthmKECIAQLPLKLesevmengdnfSVGERQLLC 1318
Cdd:PRK14271 110 PNPFPMSIMDNvlagvrahkLVPRKEFrgvaqarlTEVGLWDAV-----KDRLSDSPFRL-----------SGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1319 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN- 1396
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSp 253
|
250
....*....|
gi 1814750642 1397 ---DSSRFYA 1403
Cdd:PRK14271 254 khaETARYVA 263
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1192-1395 |
1.67e-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: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGG--CIKI--DGVRISDIGLaDLRSK----LSIIPQEPVLFsgTV 1263
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY--PH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSNLDPFNQYTEDQIWDALERthMKECIAQLPLKLESEVMEN-----GDNFSVGERQLLCIARALLRHCKILILDEATAA 1338
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELAR--MKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1339 MDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1395
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
557-751 |
1.85e-11 |
|
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: 65.77 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYVAQQAWIL-NATLRDN 621
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFpSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFG------KEFDEERYNSVLNsccLRPDLAilpnsdlteigER----GANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:COG0410 99 LLLGayarrdRAEVRADLERVYE---LFPRLK-----------ERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 692 SALDAHVGNHIFNsAIqKHLKSK--TVLFITHQLQY-LADCDEVIFMKEGCITERGTHEELMN 751
Cdd:COG0410 165 LGLAPLIVEEIFE-II-RRLNREgvTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1180-1385 |
1.91e-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: 65.21 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1180 RYQEnLPLVLkkvSFTIKPKEKIGIVGRTGSGKSSLG--MALFrLVELSGGcIKIDGVrisDIGLADL-RSKLSIIPQEP 1256
Cdd:cd03298 9 SYGE-QPMHF---DLTFAQGEITAIVGPSGSGKSTLLnlIAGF-ETPQSGR-VLINGV---DVTAAPPaDRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1257 VLFSG-TVRSNLD----PFNQYTEDQ---IWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCK 1328
Cdd:cd03298 80 NLFAHlTVEQNVGlglsPGLKLTAEDrqaIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1329 ILILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:cd03298 149 VLLLDEPFAALDpalrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
557-742 |
1.94e-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: 65.53 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLissiLGQMSLLE----GSIAVNGT--FAyvaqqawiLN----ATLR-DNILFg 625
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTL----LGLLAGLDrptsGTVRLAGQdlFA--------LDedarARLRaRHVGF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 kefdeerynsVLNSCCLRPDLAILPN----------SDLTEI----------GERG----ANLSGGQRQRISLARALYSD 681
Cdd:COG4181 95 ----------VFQSFQLLPTLTALENvmlplelagrRDARARarallervglGHRLdhypAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 682 RDIYILDDPLSALDAHVGNHIFNSAIQKHLKSKTVLFI-THQLQYLADCDEVIFMKEGCITE 742
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLvTHDPALAARCDRVLRLRAGRLVE 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
547-751 |
2.55e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 65.52 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 547 HLGNLRLqrtLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG------------------------ 602
Cdd:COG4559 10 RLGGRTL---LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarrravlpqhssl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 603 TFAYVAQQ-------AWILNATLRDNILfgkefdEErynsvlnscCL-RPDLAILPNSDLTEigerganLSGGQRQRISL 674
Cdd:COG4559 87 AFPFTVEEvvalgraPHGSSAAQDRQIV------RE---------ALaLVGLAHLAGRSYQT-------LSGGEQQRVQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 675 ARAL---YSDRD----IYILDDPLSALD-AHVgNHIFNSAiqKHLKSK--TVLFITHQL----QYladCDEVIFMKEGCI 740
Cdd:COG4559 145 ARVLaqlWEPVDggprWLFLDEPTSALDlAHQ-HAVLRLA--RQLARRggGVVAVLHDLnlaaQY---ADRILLLHQGRL 218
|
250
....*....|.
gi 1814750642 741 TERGTHEELMN 751
Cdd:COG4559 219 VAQGTPEEVLT 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1174-1388 |
2.57e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1174 FENAEMRYQEnlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLV----ELSGGCIKID-GVRIsdigladlrsk 1248
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRI----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1249 lSIIPQEPVLFSG-TVRSN-LDPFNQYteDQIWDALERTHMKECIAQLPLKLESEVME-----NG--------------- 1306
Cdd:COG0488 64 -GYLPQEPPLDDDlTVLDTvLDGDAEL--RALEAELEELEAKLAEPDEDLERLAELQEefealGGweaearaeeilsglg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1307 ----------DNFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLLIQEtireafaDCTMLTIAH-R--LH 1368
Cdd:COG0488 141 fpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY-------PGTVLVVSHdRyfLD 213
|
250 260
....*....|....*....|
gi 1814750642 1369 TVlgSDRIMVLAQGQVVEFD 1388
Cdd:COG0488 214 RV--ATRILELDRGKLTLYP 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
548-722 |
2.77e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.44 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 548 LGNLRLQRTLYN-IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------------FAYVAQQAWIL 614
Cdd:cd03231 6 LTCERDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 615 NA-TLRDNILFGKEFDEEryNSVLNScclrpdlaiLPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:cd03231 86 TTlSVLENLRFWHADHSD--EQVEEA---------LARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 1814750642 693 ALDAHvGNHIFNSAIQKHL-KSKTVLFITHQ 722
Cdd:cd03231 155 ALDKA-GVARFAEAMAGHCaRGGMVVLTTHQ 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1187-1372 |
3.01e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1187 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvriSDIGLADLRSKLSII----PQEPVLfsgT 1262
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLghrnAMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1263 VRSNLD---PFNQYTEDQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAM 1339
Cdd:PRK13539 90 VAENLEfwaAFLGGEELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|...
gi 1814750642 1340 DTETDLLIQETIREAFADCTMLTIAhrLHTVLG 1372
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAA--THIPLG 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
555-745 |
3.15e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-TFAYVAQQAWILNATLRDNILFgkEFDEERY 633
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKVGVVF--QFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 634 --NSVLNSCCLRPDLAILPNSDLTEIGERGAN---------------LSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:PRK13643 98 feETVLKDVAFGPQNFGIPKEKAEKIAAEKLEmvgladefwekspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1814750642 697 HVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGT 745
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1188-1402 |
3.17e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGL-ADLRSKLSIIPQEPVLFSG-TVRS 1265
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NLDPFNQYTEDqiwdaLERTHMKECIAQLPLKLESEVMEN--GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1343
Cdd:PRK10895 98 NLMAVLQIRDD-----LSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1344 DLLIQETIrEAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDS-SRFY 1402
Cdd:PRK10895 173 VIDIKRII-EHLRDSGLgvLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEHvKRVY 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
556-751 |
3.51e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG------TFAYVAQQAWIL---------NATLRD 620
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitddNFEKLRKHIGIVfqnpdnqfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGKE-----FDE--ERYNSVLNscclrpDLAILPNSDlteigERGANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:PRK13648 104 DVAFGLEnhavpYDEmhRRVSEALK------QVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 694 LDAHVGNHIFNsaIQKHLKSK---TVLFITHQLQYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK13648 173 LDPDARQNLLD--LVRKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1171-1390 |
4.12e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.43 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1171 EVTFENAEMRYQENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIdGVRISDIG-----L 1242
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1243 ADLRSKLSIIPQ--EPVLFSGTVRSNL--DPFNQYTEDQiwDALERThmKECIAQlpLKLESEVMENGD-NFSVGERQLL 1317
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDIcfGPMNFGVSEE--DAKQKA--REMIEL--VGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1318 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1390
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1195-1378 |
4.49e-11 |
|
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: 64.74 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1195 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGVrisDIGLAdlRSKLSIIPQE-PVLFSGTVRSNLdpfnqy 1273
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTF-------IKMLAGVLKPDEG---DIEIE--LDTVSYKPQYiKADYEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1274 tEDQIWDALERTHMKECIAQlPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE 1353
Cdd:cd03237 83 -SSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*....
gi 1814750642 1354 aFA---DCTMLTIAHRLHTV-LGSDRIMV 1378
Cdd:cd03237 161 -FAennEKTAFVVEHDIIMIdYLADRLIV 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
662-751 |
4.80e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 662 ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFnsAIQKHLKSK---TVLFITHQLQYL-ADCDEVIFMKE 737
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL--ALLKSLQQKhqlAYLFISHDLHVVrALCHQVIVLRQ 501
|
90
....*....|....
gi 1814750642 738 GCITERGTHEELMN 751
Cdd:PRK15134 502 GEVVEQGDCERVFA 515
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
559-751 |
5.37e-11 |
|
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: 64.34 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEG-SIAVNGT-------------FAYV--AQQAWIL-NATLRDN 621
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkrIGLVspALQLRFPrDETVLDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 IL---FG-----KEFDEERYNSVLNScclrpdLAILpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:COG1119 101 VLsgfFDsiglyREPTDEQRERAREL------LELL---GLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 693 ALDAHvGNHIFNSAIQK--HLKSKTVLFITHQLQYLADC-DEVIFMKEGCITERGTHEELMN 751
Cdd:COG1119 172 GLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1189-1395 |
5.75e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdIGLADLRS-KLSIIPQEPV---------- 1257
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1258 -LFSGTVRSNLDPFNQYTEDQIWDALERTHM-KECIAQLPLKLESevmengdnfsvGERQLLCIARALLRHCKILILDEA 1335
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1336 TAAMDTETD-------LLIQETIREAFADCTMlTIAHRLHTvlgSDRIMVLAQGQVVEF-DTPSVLLS 1395
Cdd:PRK15112 177 LASLDMSMRsqlinlmLELQEKQGISYIYVTQ-HLGMMKHI---SDQVLVMHQGEVVERgSTADVLAS 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
547-696 |
6.28e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.65 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 547 HLGNLRLQRT----LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSL---LEGSIAVNGT-----------FAYVA 608
Cdd:COG4136 3 SLENLTITLGgrplLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRrltalpaeqrrIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 609 QQAWiLNATL--RDNILFG---KEFDEERYNSVLNScclrpdlaiLPNSDLTEIGERG-ANLSGGQRQRISLARALYSDR 682
Cdd:COG4136 83 QDDL-LFPHLsvGENLAFAlppTIGRAQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLRALLAEP 152
|
170
....*....|....
gi 1814750642 683 DIYILDDPLSALDA 696
Cdd:COG4136 153 RALLLDEPFSKLDA 166
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
561-759 |
6.85e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.83 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 561 DLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---TFAYVAQQ-AWIL--------NATLRDNILFGkef 628
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRpVSMLfqennlfsHLTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 629 deerynsvlnsccLRPDL-----------AILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:PRK10771 96 -------------LNPGLklnaaqreklhAIARQMGIEDLLARlPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 697 HVGNHIFN----SAIQKHLkskTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMNLNGDYATI 759
Cdd:PRK10771 163 ALRQEMLTlvsqVCQERQL---TLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1192-1386 |
7.32e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLSIIPQEPVlfsgtvrSNLD 1268
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEAQKLLRQKIQIVFQNPY-------GSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1269 PfNQYTEDQIWDALE----------RTHMKECIAQLPLKLESEV----MengdnFSVGERQLLCIARALLRHCKILILDE 1334
Cdd:PRK11308 107 P-RKKVGQILEEPLLintslsaaerREKALAMMAKVGLRPEHYDryphM-----FSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1335 ATAAMDTEtdllIQETIREAFAD------CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:PRK11308 181 PVSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1192-1384 |
9.40e-11 |
|
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: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-GGCIKIDGVRISDIGLAD-LRSKLSIIPQE-------PVLFSG- 1261
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQaIRAGIAMVPEDrkrhgivPILGVGk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 -TVRSNLDPFNQYTedQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMD 1340
Cdd:TIGR02633 359 nITLSVLKSFCFKM--RIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1814750642 1341 T----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 1384
Cdd:TIGR02633 436 VgakyEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
556-749 |
1.03e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 556 TLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTfAYVAQQAW----------------ILNATLR 619
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvfqnpdnqFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGKE-----FDE--ERYNSVLNSCclrpdlailpnsDLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:PRK13650 101 DDVAFGLEnkgipHEEmkERVNEALELV------------GMQDFKEREpARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 692 SALDAHvGNHIFNSAIQKHLKSK--TVLFITHQLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:PRK13650 169 SMLDPE-GRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
557-762 |
1.04e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.90 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSiLGQMSLL------EGSIAVNGTFAY---------------VAQQAWILN 615
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLipgarvEGEILLDGEDIYdpdvdvvelrrrvgmVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 616 ATLRDNILFG---------KEFDE--ERynsvlnscCLRpdLAILPNsdltEIGER----GANLSGGQRQRISLARALYS 680
Cdd:COG1117 106 KSIYDNVAYGlrlhgikskSELDEivEE--------SLR--KAALWD----EVKDRlkksALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 681 DRDIYILDDPLSALDAhvgnhIFNSAIQ---KHLKSK-TVLFITHQLQYLADC-DEVIFMKEGCITERGTHEElmnlngd 755
Cdd:COG1117 172 EPEVLLMDEPTSALDP-----ISTAKIEeliLELKKDyTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQ------- 239
|
....*..
gi 1814750642 756 yatIFNN 762
Cdd:COG1117 240 ---IFTN 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1172-1388 |
1.07e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRL----VELSGGCIKIdGVRIsdigladlrs 1247
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1248 KLSIIPQEpvlfsgtvRSNLDPfnqytEDQIWDALERTHmkeciaqlPLKLESEVME-------NGD-------NFSVGE 1313
Cdd:COG0488 379 KIGYFDQH--------QEELDP-----DKTVLDELRDGA--------PGGTEQEVRGylgrflfSGDdafkpvgVLSGGE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1314 RQLLCIARALLRHCKILILDEATAAMDTETdlliqetiREAFADC------TMLTIAH-R--LHTVlgSDRIMVLAQGQV 1384
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgTVLLVSHdRyfLDRV--ATRILEFEDGGV 507
|
....
gi 1814750642 1385 VEFD 1388
Cdd:COG0488 508 REYP 511
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1188-1386 |
1.20e-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: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIgLADLRSKLSII--PQEPVLFSGtv 1263
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDL-PPEERARLGIFlaFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 rsnldpfnqytedqiwdalerthmkeciaqlpLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1343
Cdd:cd03217 92 --------------------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1814750642 1344 DLLIQETIRE-AFADCTMLTIAH--RLHTVLGSDRIMVLAQGQVVE 1386
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1191-1389 |
1.28e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1191 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDI---GLADLRS-KLSIIPQEPVlfsgtv 1263
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLpekELNKLRAeQISMIFQDPM------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 rSNLDPFNQYTEdQIWDAL-------------ERTHMKECIaQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKIL 1330
Cdd:PRK09473 108 -TSLNPYMRVGE-QLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARKRMKMYPHE-FSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1331 ILDEATAAMDTETD----LLIQETIREaFaDCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEFDT 1389
Cdd:PRK09473 184 IADEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1188-1395 |
1.36e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSG-TVRSN 1266
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 L----DPFNQY-----TEDQ--IWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:PRK11231 97 VaygrSPWLSLwgrlsAEDNarVNQAMEQTRINH-LADRRL----------TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1336 TAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1395
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
557-747 |
1.48e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSilgqMSLLEgsIAVNGTFAyVAQQAWILNAT--------LRDNIlfGKEF 628
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLE--MPRSGTLN-IAGNHFDFSKTpsdkaireLRRNV--GMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 629 deERYN-----SVLNSCCLRP--------------DLAILPNSDLTEIGER-GANLSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK11124 89 --QQYNlwphlTVQQNLIEAPcrvlglskdqalarAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 689 DPLSALDAHVGNHIFNsaIQKHLKSK--TVLFITHQLQYLAD-CDEVIFMKEGCITERGTHE 747
Cdd:PRK11124 167 EPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1189-1390 |
1.66e-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: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrsklsiiPQEPVLFSG------- 1261
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQNysllpwl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 TVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEvmENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1341
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAAD--KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1342 ETDLLIQETIREAFAD--CTMLTIAHRL-HTVLGSDRIMVLAQ------GQVVEFDTP 1390
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEhrVTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEVPFP 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1188-1405 |
1.71e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID-GVRISDIgladlRSKLSIIPQEPVLFSGTVRsn 1266
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYV-----PQKLYLDTTLPLTVNRFLR-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LDPFNQytEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDL- 1345
Cdd:PRK09544 92 LRPGTK--KEDILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVa 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1346 ---LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQgQVVEFDTPSVLLSNdsSRFYAMF 1405
Cdd:PRK09544 159 lydLIDQLRRE--LDCAVLMVSHDLHLVMAkTDEVLCLNH-HICCSGTPEVVSLH--PEFISMF 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1172-1397 |
1.87e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.67 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADL-RSKLS 1250
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRARHaRQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1251 IIPQ----EPVLfsgTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMEngdnFSVGERQLLCIARALLRH 1326
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1327 CKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
554-751 |
1.91e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.87 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSIlGQMSLLEGSIAVNGTFAY---------------------VAQQAW 612
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 613 ILNATLRDNILFGKEFDEERYNSVLNSCCLRpdlAILPNSDLTEIGER----GANLSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK14239 97 PFPMSIYENVVYGLRLKGIKDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 689 DPLSALDAhvgnhIFNSAIQKHL----KSKTVLFITHQLQYLAD-CDEVIFMKEGCITERG-THEELMN 751
Cdd:PRK14239 174 EPTSALDP-----ISAGKIEETLlglkDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNdTKQMFMN 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
555-751 |
1.94e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.49 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGqMSLLEGSIAVNGTFAYVAQ---------------------QAWI 613
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG-LIISETGQTIVGDYAIPANlkkikevkrlrkeiglvfqfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 614 LNATLRDNILFGK----EFDEERYNSVLNSCclrpDLAILPNsdltEIGERGA-NLSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK13645 104 FQETIEKDIAFGPvnlgENKQEAYKKVPELL----KLVQLPE----DYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 689 DPLSALDAHvGNHIFNSAIQKHLKS--KTVLFITHQL-QYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK13645 176 EPTGGLDPK-GEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
559-750 |
2.02e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.98 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGqmsLLE---GSIAVNGT-FAYVAQQAW---------------------- 612
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLR---LEEptsGEILFDGQdITGLSGRELrplrrrmqmvfqdpyaslnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 613 ----ILNATLRDNILFGKEFDEERYNSVLNSCCLRPDLAilpnsdlteigERGAN-LSGGQRQRISLARALYSDRDIYIL 687
Cdd:COG4608 113 tvgdIIAEPLRIHGLASKAERRERVAELLELVGLRPEHA-----------DRYPHeFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 688 DDPLSALDAHVGNHIFN--SAIQKHLKSkTVLFITHQL---QYLadCDEVIFMKEGCITERGTHEELM 750
Cdd:COG4608 182 DEPVSALDVSIQAQVLNllEDLQDELGL-TYLFISHDLsvvRHI--SDRVAVMYLGKIVEIAPRDELY 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1188-1386 |
2.05e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKLSIIPQEP---VLFSG 1261
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 TVRSNLD-PFNQYT----EDQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEAT 1336
Cdd:PRK10419 107 TVREIIRePLRHLLsldkAERLARASEMLRAVDLDDSVLDKRPPQL-------SGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1337 AAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:PRK10419 180 SNL----DLVLQagvirllKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
559-749 |
2.24e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.18 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKtsliSSILGQMSLL----EGSIAVNGTFAYVAQQAW----------------ILNATL 618
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGK----STIAKHMNALlipsEGKVYVDGLDTSDEENLWdirnkagmvfqnpdnqIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNILFGKEfdeerynsvlnscclrpDLAILPNsdltEIGERGAN-----------------LSGGQRQRISLARALYSD 681
Cdd:PRK13633 104 EEDVAFGPE-----------------NLGIPPE----EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 682 RDIYILDDPLSALDAHVGNHIFNSAiqKHLKSK---TVLFITHQLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTI--KELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1188-1386 |
2.44e-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: 62.16 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI--IPQEPVLFSG-TVR 1264
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-PHERARAGIayVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLdpfnqytedQI-WDALERTHMK--ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1341
Cdd:TIGR03410 94 ENL---------LTgLAALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1814750642 1342 ETDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:TIGR03410 165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVA 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1195-1378 |
2.59e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1195 TIKPKEKIGIVGRTGSGKSSLGMALfrlvelsGGCIKIDGvrisdiGLADLRSKLSIIPQE-PVLFSGTVRSNLDpfnqy 1273
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDE------GEVDPELKISYKPQYiKPDYDGTVEDLLR----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1274 tedQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 1352
Cdd:PRK13409 423 ---SITDDLGSSYYKSEIIK-PLQLE-RLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170 180 190
....*....|....*....|....*....|
gi 1814750642 1353 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 1378
Cdd:PRK13409 498 R-IAeerEATALVVDHDIYMIdYISDRLMV 526
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
557-736 |
2.67e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT----------FAYVAQQA---WILNATLRDNIL 623
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FG-----------KEFDEERYNSVLNscclRPDLAILPNSdltEIGErganLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:PRK15056 103 MGryghmgwlrraKKRDRQIVTAALA----RVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1814750642 693 ALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMK 736
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1192-1410 |
2.72e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.09 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIglADLRSKLSIIPQEPVLFSG-TVRSNLD-- 1268
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQNIAfg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1269 ------PFNQYTeDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTE 1342
Cdd:PRK11607 116 lkqdklPKAEIA-SRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1343 ----TDLLIQETIREAFADCTMLTiaH---RLHTVLGsdRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1410
Cdd:PRK11607 184 lrdrMQLEVVDILERVGVTCVMVT--HdqeEAMTMAG--RIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
559-750 |
2.76e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVN------GTFAYVAQQ------------------AWIL 614
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRirmifqdpstslnprqriSQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 615 NATLRDNILFGKEFDEERYNSVLNSCCLRPDLA-ILPNSdlteigerganLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:PRK15112 111 DFPLRLNTDLEPEQREKQIIETLRQVGLLPDHAsYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 694 LDAHVGNHIFNSAIQkhLKSK---TVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELM 750
Cdd:PRK15112 180 LDMSMRSQLINLMLE--LQEKqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1189-1397 |
2.76e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEP--VLFSGTVRSN 1266
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 L--DPFNQ-----YTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAM 1339
Cdd:PRK13647 101 VafGPVNMgldkdEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1340 DTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:PRK13647 170 DPRG----QETLMEILDRLhnqgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1195-1378 |
3.03e-10 |
|
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: 64.81 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1195 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGvrisdiGLADLRSKLSIIPQEPV-LFSGTVRSNLdpfnqy 1273
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTF-------AKILAGVLKPDE------GEVDEDLKISYKPQYISpDYDGTVEEFL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1274 tEDQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 1352
Cdd:COG1245 423 -RSANTDDFGSSYYKTEIIK-PLGLE-KLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|
gi 1814750642 1353 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 1378
Cdd:COG1245 500 R-FAenrGKTAMVVDHDIYLIdYISDRLMV 528
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1188-1396 |
3.10e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.79 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI--SDIGLADLRSKLSIIPQEP--VLFSGTV 1263
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSNL--DPFN-----QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEAT 1336
Cdd:PRK13639 97 EEDVafGPLNlglskEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1337 AAMD----TETDLLIQETIREAfadctmLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:PRK13639 166 SGLDpmgaSQIMKLLYDLNKEG------ITIIISTHDVdlvpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1172-1365 |
3.39e-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: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcikidgvrisdigladlrskLSI 1251
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSGTVrsnldpfnqytedqiwdaleRTHMKECIAQLPlklesevmengdNFSVGERQLLCIARALLRHCKILI 1331
Cdd:cd03221 46 IAGELEPDEGIV--------------------TWGSTVKIGYFE------------QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 1814750642 1332 LDEATAAMDTETDLLIQETIREaFaDCTMLTIAH 1365
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-Y-PGTVILVSH 125
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
554-750 |
4.21e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQAWILNA-TLR 619
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGK-----------EFDEERYNSVLNscclRPDLAILPNSDLTEigerganLSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK11231 95 ELVAYGRspwlslwgrlsAEDNARVNQAME----QTRINHLADRRLTD-------LSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 689 DPLSALDAhvgNH---IFNSAIQKHLKSKTVLFITHQL-QYLADCDEVIFMKEGCITERGTHEELM 750
Cdd:PRK11231 164 EPTTYLDI---NHqveLMRLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
559-750 |
4.24e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.52 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG----TFAYVAQQAWIL---------NATLRDNIL-F 624
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVvpqfdnldpDFTVRENLLvF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 GKEFD------EERYNSVLnscclrpDLAILPNSDLTEIGErganLSGGQRQRISLARALYSDRDIYILDDPLSALDAHv 698
Cdd:PRK13537 105 GRYFGlsaaaaRALVPPLL-------EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 699 GNHIfnsaIQKHLKS-----KTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELM 750
Cdd:PRK13537 173 ARHL----MWERLRSllargKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1172-1385 |
5.53e-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: 60.76 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiglADLRSKLSI 1251
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSG-TVRSNLDPFNQ-------YTEDQIWDALERTHMKEciaqlplKLESEVMEngdnFSVGERQLLCIARAL 1323
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYLAQlkglkkeEARRRIDEWLERLELSE-------YANKRVEE----LSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1324 LRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
884-1004 |
5.71e-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: 62.18 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 884 MKDNPLMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV 963
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSD 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1814750642 964 RLPFQAEMFIQNVILVFFCVGMIAGVfPWFL-----VAVGPLIILF 1004
Cdd:cd18572 109 PLSTNLNVFLRNLVQLVGGLAFMFSL-SWRLtllafITVPVIALIT 153
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1188-1391 |
7.14e-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: 63.28 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE----LSGGCI--------------------------------K 1231
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDqyepTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1232 IDGVRISDIGLADLRSKLSIIPQEPVLFSG--TVRSN-LDPFNQ--YT-EDQIWDALERTHMkeciaqlpLKLESEVMEN 1305
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvLEALEEigYEgKEAVGRAVDLIEM--------VQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1306 GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVLG-SDRIMVLAQG 1382
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
....*....
gi 1814750642 1383 QVVEFDTPS 1391
Cdd:TIGR03269 246 EIKEEGTPD 254
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1188-1385 |
9.72e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.87 E-value: 9.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADL-RSKL-SIIPQEPVL---FSGT 1262
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYkRAKYiGRVFQDPMMgtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1263 VRSNLdpfnqytedqiwdAL-----------------ERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLR 1325
Cdd:COG1101 99 IEENL-------------ALayrrgkrrglrrgltkkRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1326 HCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVL--GsDRIMVLAQGQVV 1385
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEEnnLTTLMVTHNMEQALdyG-NRLIMMHEGRII 228
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
563-720 |
1.24e-09 |
|
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: 62.84 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 563 EIEEGKLVGICGSVGSGKTSLISsILGQMSLLEG---SIAVNGTFAYVAQQAWILNATLRDNILFGKEFDEERYNSVLNS 639
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 640 cclrpDL-AILPNSDLTEIGERGAN----------LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNsaiq 708
Cdd:TIGR00954 553 -----DLeQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR---- 623
|
170
....*....|..
gi 1814750642 709 kHLKSKTVLFIT 720
Cdd:TIGR00954 624 -LCREFGITLFS 634
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1180-1368 |
1.24e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1180 RYQEN--LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV---RISDIGLADLRS-KLSIIP 1253
Cdd:PRK11629 14 RYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1254 QepvlfsgtvrsnldpFNQYTEDqiWDALERTHMKECIAQLPLK--------------LESEVMENGDNFSVGERQLLCI 1319
Cdd:PRK11629 94 Q---------------FHHLLPD--FTALENVAMPLLIGKKKPAeinsralemlaavgLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1320 ARALLRHCKILILDEATAAMDTET-----DLLIQETIRE--AFADCTM-LTIAHRLH 1368
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNadsifQLLGELNRLQgtAFLVVTHdLQLAKRMS 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
557-745 |
1.24e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTfaYVAQQAWILNATLRDNIL-FGKEFDEeryns 635
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQKLgFIYQFHH----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 636 vlnsccLRPDLAILPN--------------------SDLTEIG------ERGANLSGGQRQRISLARALYSDRDIYILDD 689
Cdd:PRK11629 98 ------LLPDFTALENvamplligkkkpaeinsralEMLAAVGlehranHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 690 PLSALDAHVGNHIFNSAIQKHLKSKTV-LFITHQLQYLADCDEVIFMKEGCITERGT 745
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTAfLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1172-1398 |
1.34e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.95 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS----DIGLAD 1244
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1245 LRSKLSIIPQ--EPVLFSGTVRSNLD--P--FNQYTEDqiwdalerthMKECIAQLPLKL--ESEVMENGD-NFSVGERQ 1315
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIfgPknFKMNLDE----------VKNYAHRLLMDLgfSRDVMSQSPfQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1316 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSV 1392
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
....*.
gi 1814750642 1393 LLSNDS 1398
Cdd:PRK13646 233 LFKDKK 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
557-749 |
1.61e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWILNA-------------------- 616
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 TLRDNILF---GKEFDEERYNSVLNSCCLRPdlAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:PRK14246 106 SIYDNIAYplkSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 694 LDAhVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
559-751 |
1.69e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.04 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYVAQQAWIL-NATLRDNIL 623
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFrKLTVEDNIL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 -------FGKEFDEERYNSVLNscclrpDLailpnsDLTEIGE-RGANLSGGQRQRISLARALYSDRDIYILD------D 689
Cdd:COG1137 101 avlelrkLSKKEREERLEELLE------EF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDepfagvD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 690 PLSALDahvgnhifnsaIQK---HLKSK--TVLfIT-HQLQ-YLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:COG1137 169 PIAVAD-----------IQKiirHLKERgiGVL-ITdHNVReTLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1189-1385 |
1.81e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQE-PVLFSGTVRSN 1266
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LdPFNQYTEDQIW--DALERTHMKECIAQLPLK--LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM-DT 1341
Cdd:PRK09700 101 L-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1814750642 1342 ETD---LLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:PRK09700 180 EVDylfLIMNQLRKEGTA---IVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1188-1390 |
2.04e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS---DIGLA---DL--RsklsiipqEPVLF 1259
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSallELGAGfhpELtgR--------ENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1260 SGTVrsnldpfNQYTEDQIwdaleRTHMKECIA--------QLPLKlesevmengdNFSVGERQLLCIARALLRHCKILI 1331
Cdd:COG1134 112 NGRL-------LGLSRKEI-----DEKFDEIVEfaelgdfiDQPVK----------TYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1332 LDEATAAMDTE-----TDlLIQETIREAfadCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1390
Cdd:COG1134 170 VDEVLAVGDAAfqkkcLA-RIRELRESG---RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1175-1386 |
2.25e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.86 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1175 ENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGVRI--SDIGLADLRS 1247
Cdd:PRK14267 8 VNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1248 KLSIIPQEPVLFSG-TVRSN----------LDPFNQYTEDQIWdALERthmkeciAQLPLKLESEVMENGDNFSVGERQL 1316
Cdd:PRK14267 86 EVGMVFQYPNPFPHlTIYDNvaigvklnglVKSKKELDERVEW-ALKK-------AALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1317 LCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHR-LHTVLGSDRIMVLAQGQVVE 1386
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
555-742 |
2.26e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLY-NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI--AVNGTFAYVAQQAWIL--NATLRDNILFGKEFD 629
Cdd:COG0488 328 KTLLdDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklGETVKIGYFDQHQEELdpDKTVLDELRDGAPGG 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 630 EERY-NSVLNSCCLRPDLAilpnsdLTEIGergaNLSGGQRQRISLARALYSDRDIYILDDPlsaldahvGNH------- 701
Cdd:COG0488 408 TEQEvRGYLGRFLFSGDDA------FKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP--------TNHldietle 469
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1814750642 702 IFNSAIQKHlkSKTVLFITHQlQYLAD--CDEVIFMKEGCITE 742
Cdd:COG0488 470 ALEEALDDF--PGTVLLVSHD-RYFLDrvATRILEFEDGGVRE 509
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1189-1385 |
2.40e-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: 61.38 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVELSG---GCIKIDGVRISDIGLADLRSK-LSIIPQEPVLFSG-TV 1263
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSNLDPFNQYTE--DQIWDALERTHMKECIAQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKILILDEATAAM-D 1340
Cdd:TIGR02633 96 AENIFLGNEITLpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSSLtE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1814750642 1341 TETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:TIGR02633 175 KETEILL-DIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
554-751 |
2.85e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYVAQQAWILNA-TL 618
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNIL--------FGKEFDEERYNSVL---NSCCLRPDLailpnsdlteigerGANLSGGQRQRISLARALYSDRDIYIL 687
Cdd:PRK10895 96 YDNLMavlqirddLSAEQREDRANELMeefHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 688 DDPLSALDAHVGNHIfnSAIQKHLKSK--TVLFITHQL-QYLADCDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK10895 162 DEPFAGVDPISVIDI--KRIIEHLRDSglGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
555-751 |
3.05e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWILN---------------ATLR 619
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFG-------KEFDEERYNSVLNSCclrpdlailpnsDLTEIGERGA-NLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:PRK13647 99 DDVAFGpvnmgldKDEVERRVEEALKAV------------RMWDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 692 SALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
894-1075 |
3.11e-09 |
|
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: 60.11 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 894 ASIYALSMAVMLILkairGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqAEMFI 973
Cdd:cd18547 52 LGLYLLSALFSYLQ----NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNI-------SQALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 974 QNVILVFFCVGMIAGVF-------PWF-LVAVGPLIILFSILHIV---SRVLIREL-KRLDNITqspflSHITSSIQGLA 1041
Cdd:cd18547 121 QSLTQLISSILTIVGTLimmlyisPLLtLIVLVTVPLSLLVTKFIakrSQKYFRKQqKALGELN-----GYIEEMISGQK 195
|
170 180 190
....*....|....*....|....*....|....
gi 1814750642 1042 TIHAYKKGQEFLHRYQELldnNQRpffLFTCAMR 1075
Cdd:cd18547 196 VVKAFNREEEAIEEFDEI---NEE---LYKASFK 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
664-749 |
3.20e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 61.24 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 664 LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVgnhifnsaiQ-------KHLKSKT---VLFITHQLQYLAD-CDEV 732
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV---------QaqildllKDLQRELgmaLLLITHDLGVVRRfADRV 227
|
90
....*....|....*..
gi 1814750642 733 IFMKEGCITERGTHEEL 749
Cdd:COG4172 228 AVMRQGEIVEQGPTAEL 244
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
559-793 |
3.21e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAV----------NGTFAYVAQQAWILNA------------ 616
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFkelrrrvsmvfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 ---------TLRDNILFG-------KEFDEERYNSVLNSCCLRPDLAilpnsdlteigERGA-NLSGGQRQRISLARALY 679
Cdd:PRK13631 124 fpeyqlfkdTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYL-----------ERSPfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 680 SDRDIYILDDPLSALDAHvGNHIFNSAIQKHLKS-KTVLFITHQL-QYLADCDEVIFMKEGCITERGTheelmnlngDYA 757
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANnKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT---------PYE 262
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1814750642 758 TIFNNLLLGET----PPV--EINSKKETSGSQKKTQDKCPKT 793
Cdd:PRK13631 263 IFTDQHIINSTsiqvPRViqVINDLIKKDPKYKKLYQKQPRT 304
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1189-1397 |
3.36e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----------VELSGGCIKIDGVRISDIGLA-----------DLRS 1247
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARDIRKSrantgyifqqfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1248 KLSIIpqEPVLFS--GTV---RSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARA 1322
Cdd:PRK09984 100 RLSVL--ENVLIGalGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTL-----------SGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1323 LLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVeFDTPSVLLSND 1397
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQFDNE 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
559-750 |
3.49e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYVAQQ----AWILNATLRD 620
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITESrrdnGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGKEFDEERYNSVLN----------SCCLRPDLAILPNSDLTEIGErganLSGGQRQRISLARALYSDRDIYILDDP 690
Cdd:PRK09700 361 NMAISRSLKDGGYKGAMGlfhevdeqrtAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 691 LSALDAHVGNHIFNSAIQKHLKSKTVLFITHQL-QYLADCDEVIFMKEGCITE------RGTHEELM 750
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQiltnrdDMSEEEIM 503
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1188-1385 |
4.27e-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: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSIIpqepvlfsgtvrsnl 1267
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLRRIGVV--------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1268 dpFNQYTEdQIWD--ALERTHMKECIAQLP-------LKLESEVMENGD-------NFSVGERQLLCIARALLRHCKILI 1331
Cdd:cd03267 100 --FGQKTQ-LWWDlpVIDSFYLLAAIYDLPparfkkrLDELSELLDLEElldtpvrQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1332 LDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
886-1099 |
6.72e-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: 59.00 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 886 DNPLMQYYASIYALSM----AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTP--TGRILNRFSKDMD 959
Cdd:cd18578 43 DDDELRSEANFWALMFlvlaIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDAS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 960 EV----DVRLPfqaeMFIQNVILVFFCVGmIAGVFPWFL----VAVGPLIILFSILHIvsRVLIR-ELKRLDNITQSpfl 1030
Cdd:cd18578 123 DVrglvGDRLG----LILQAIVTLVAGLI-IAFVYGWKLalvgLATVPLLLLAGYLRM--RLLSGfEEKNKKAYEES--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1031 SHITS-SIQGLATIHAYKKGQEFLHRYQELLDNNQR-------------------PFFLFTCAMRWLAVrldLISIALIT 1090
Cdd:cd18578 193 SKIASeAVSNIRTVASLTLEDYFLEKYEEALEEPLKkglrralisglgfglsqslTFFAYALAFWYGGR---LVANGEYT 269
|
....*....
gi 1814750642 1091 TTGLMIVLM 1099
Cdd:cd18578 270 FEQFFIVFM 278
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
555-738 |
7.24e-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: 59.84 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILG--QMSLLEGSIAVNGT--------------FAYVAQQ-AWILNAT 617
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFGKEFDEE----RYNSVLNSC-CLRPDLAILPNSDLTEIGERGanlsGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:TIGR02633 95 VAENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1814750642 693 ALDAHVGNHIFNsaIQKHLKSKTV--LFITHQLQYL-ADCDEVIFMKEG 738
Cdd:TIGR02633 171 SLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVkAVCDTICVIRDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
555-738 |
8.78e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYVAQQAWILNA-TLR 619
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGKE----------FDEERYNSVLNSCCLRPDLAILPNsdlteigERGANLSGGQRQRISLARALYSDRDIYILDD 689
Cdd:PRK09700 99 ENLYIGRHltkkvcgvniIDWREMRVRAAMMLLRVGLKVDLD-------EKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 690 PLSALDAHVGNHIFnsAIQKHLKS--KTVLFITHQL-QYLADCDEVIFMKEG 738
Cdd:PRK09700 172 PTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
550-728 |
9.00e-09 |
|
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: 57.80 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 NLRLQRTLYNIDLEIEEGKL-----VGICGSVGSGKTSLISSILGQMSLLEGSIAV-NGTFAYVAQQAWILNATLRDNIL 623
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIeLDTVSYKPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKEfdeeryNSVLNSCCLRPDlaILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRDIYILDDPLSALDahVGNHI 702
Cdd:cd03237 83 SSIT------KDFYTHPYFKTE--IAKPLQIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRL 152
|
170 180 190
....*....|....*....|....*....|..
gi 1814750642 703 FNSAIQKHL---KSKTVLFITHQL---QYLAD 728
Cdd:cd03237 153 MASKVIRRFaenNEKTAFVVEHDIimiDYLAD 184
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
534-728 |
9.33e-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: 59.80 E-value: 9.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 534 ERPSPEEEEGKHTHLGNLRLQRTLYNIDLEIEEGKL-----VGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVA 608
Cdd:COG1245 328 EVHAPRREKEEETLVEYPDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKP 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 609 QqaWILN-------ATLRDNIlfGKEFDEERYNSVLnsccLRPdLAI--LPNSDLTEigerganLSGGQRQRISLARALY 679
Cdd:COG1245 408 Q--YISPdydgtveEFLRSAN--TDDFGSSYYKTEI----IKP-LGLekLLDKNVKD-------LSGGELQRVAIAACLS 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 680 SDRDIYILDDPLSALDA----HVGnhifnSAIQKHLKS--KTVLFITHQLQ---YLAD 728
Cdd:COG1245 472 RDADLYLLDEPSAHLDVeqrlAVA-----KAIRRFAENrgKTAMVVDHDIYlidYISD 524
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
557-740 |
1.04e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.79 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---TFAYVAQQA-WIL------------NATLRD 620
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRAkYIGrvfqdpmmgtapSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILF----GKEF---------DEERYnsvlnscclRPDLAILpnsDL-------TEIGergaNLSGGQRQRISLARALYS 680
Cdd:COG1101 102 NLALayrrGKRRglrrgltkkRRELF---------RELLATL---GLglenrldTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 681 DRDIYILDDPLSALD---AHVGNHIFNSAIQ-KHLkskTVLFITHQLQYLADC-DEVIFMKEGCI 740
Cdd:COG1101 166 KPKLLLLDEHTAALDpktAALVLELTEKIVEeNNL---TTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
902-1007 |
1.23e-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: 58.21 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 902 AVMLILKAIRGVV-FVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ 974
Cdd:cd18542 43 LLILGVALLRGVFrYLQGYLaekasqKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVR 122
|
90 100 110
....*....|....*....|....*....|....*.
gi 1814750642 975 NVILVFFCVGMIAGVFP---WFLVAVGPLIILFSIL 1007
Cdd:cd18542 123 AVLLFIGALIIMFSINWkltLISLAIIPFIALFSYV 158
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
559-752 |
1.32e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLissilgqMSLL-------EGSIAVNG---TFA--YVAQQAWI--------L--NA 616
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTL-------MKILyglyqpdSGEILIDGkpvRIRspRDAIALGIgmvhqhfmLvpNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 TLRDNILFGKEfdeerynsvlNSCCLRPDLAILpNSDLTEIGER-G---------ANLSGGQRQRISLARALYSDRDIYI 686
Cdd:COG3845 96 TVAENIVLGLE----------PTKGGRLDRKAA-RARIRELSERyGldvdpdakvEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 687 LDDPLSALDAHVGNHIFnsAIQKHLKS--KTVLFITHQLQ-YLADCDEVIFMKEG-----CITERGTHEELMNL 752
Cdd:COG3845 165 LDEPTAVLTPQEADELF--EILRRLAAegKSIIFITHKLReVMAIADRVTVLRRGkvvgtVDTAETSEEELAEL 236
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
898-1142 |
1.32e-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: 57.90 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 898 ALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVI 977
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 978 LVFFCVGMIAGVFPWFLVAV---GPLIILFSILH--IVSRVLIRELKRLDNITqspflSHITSSIQGLATIHAYkkGQE- 1051
Cdd:cd18563 130 MIIGIGVVLFSLNWKLALLVlipVPLVVWGSYFFwkKIRRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAF--GQEk 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1052 -----FLHRYQELLDNNQRpfflftCAMRWLAVrldLISIALITTTGLMIV-------LMHGQIPP----AYaglaISYA 1115
Cdd:cd18563 203 reikrFDEANQELLDANIR------AEKLWATF---FPLLTFLTSLGTLIVwyfggrqVLSGTMTLgtlvAF----LSYL 269
|
250 260
....*....|....*....|....*..
gi 1814750642 1116 VQLTGLFQFTVRLASETEARFTSVERI 1142
Cdd:cd18563 270 GMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1172-1391 |
1.38e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.82 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG----LAD 1244
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1245 LRSKLSIIPQEP--VLFSGTVRSNL----DPFNQYTEDQIWDALERTHM----KECIAQLPLKLesevmengdnfSVGER 1314
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMvglaDEFWEKSPFEL-----------SGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1315 QLLCIARALLRHCKILILDEATAAMDTETDLLIQ---ETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1390
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
.
gi 1814750642 1391 S 1391
Cdd:PRK13643 229 S 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1188-1402 |
1.50e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.96 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFR----LVELSGGCIKIDGVRISDIGLaDLRSKLSI--IPQEPVLFSG 1261
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 -TVRSNLDPFNQYTEdqiwdaLERTHMKECIAQLplkLE----SEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:COG1137 93 lTVEDNILAVLELRK------LSKKEREERLEEL---LEefgiTHLRKSkAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1336 TAAMD--TETDllIQETIREafadctmLT---IA-----HRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR-FY 1402
Cdd:COG1137 164 FAGVDpiAVAD--IQKIIRH-------LKergIGvlitdHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPLVRkVY 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1172-1388 |
1.61e-08 |
|
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: 56.49 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLSI 1251
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1252 IPQEPVLFSG-TVRSNLD---PFNQYTEDQIwdaLERTHMkecIAQLpLKLESEVMENGDNFSVGERQLLCIARALLRHC 1327
Cdd:cd03301 77 VFQNYALYPHmTVYDNIAfglKLRKVPKDEI---DERVRE---VAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1328 KILILDEATAAMDTEtdlliqetIREAfadctMLTIAHRLHTVLG----------------SDRIMVLAQGQVVEFD 1388
Cdd:cd03301 150 KVFLMDEPLSNLDAK--------LRVQ-----MRAELKRLQQRLGtttiyvthdqveamtmADRIAVMNDGQIQQIG 213
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1191-1395 |
1.66e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.89 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1191 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRlVELSGGCIKIDGVRISDIGLADL----RSKL-----SIIPQEPvlfsg 1261
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLspreRRKLvghnvSMIFQEP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 tvRSNLDPfNQYTEDQIWDAL----------ERTHMK-----ECIAQLPLKLESEVMENGD-NFSVGERQLLCIARALLR 1325
Cdd:PRK15093 99 --QSCLDP-SERVGRQLMQNIpgwtykgrwwQRFGWRkrraiELLHRVGIKDHKDAMRSFPyELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1326 HCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1395
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
545-736 |
1.68e-08 |
|
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: 55.44 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 545 HTHLGNLRLQRtlYNIDLEIEEGKLVGICGSVGSGKTSLISSIlgqmsllegsiavngtfayvaqqawILNATLRDNILF 624
Cdd:cd03227 1 KIVLGRFPSYF--VPNDVTFGEGSLTIITGPNGSGKSTILDAI-------------------------GLALGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 625 GKEFDEERYNSVLNSCCLRpdlailpnsdLTEIGerganLSGGQRQRISLARAL----YSDRDIYILDDPLSALDAHVGN 700
Cdd:cd03227 54 RRSGVKAGCIVAAVSAELI----------FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 1814750642 701 HIFNsAIQKHLKSK-TVLFITHQLQYLADCDEVIFMK 736
Cdd:cd03227 119 ALAE-AILEHLVKGaQVIVITHLPELAELADKLIHIK 154
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
559-750 |
1.68e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.05 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNgtfayvAQQAWIlNATLRDNILFGKEfdeERYNSVLN 638
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR------VGDEWV-DMTKPGPDGRGRA---KRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 639 S-CCLRPDLAILPNsdLT---------EIGERGA-----------------------NLSGGQRQRISLARALYSDRDIY 685
Cdd:TIGR03269 372 QeYDLYPHRTVLDN--LTeaiglelpdELARMKAvitlkmvgfdeekaeeildkypdELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 686 ILDDPLSALD----AHVGNHIFNSAIQkhlKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELM 750
Cdd:TIGR03269 450 ILDEPTGTMDpitkVDVTHSILKAREE---MEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1190-1384 |
1.83e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1190 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIP---QEPVLF------ 1259
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1260 --SGTVRSNLDPFNQYT--EDQIwdaLERTHmkeciAQLPLKLeSEVMENGDNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:PRK15439 360 wnVCALTHNRRGFWIKParENAV---LERYR-----RALNIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1336 TAAMDTETDLLIQETIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQV 1384
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1168-1399 |
2.10e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.90 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1168 QEGEVTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG-----VRISD--I 1240
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDgqL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1241 GLAD------LRSKLSIIPQEPVLFSG-TVRSNLdpfnQYTEDQIWdALERTHMKECIAQLPLKL---ESEVMENGDNFS 1310
Cdd:PRK10619 80 KVADknqlrlLRTRLTMVFQHFNLWSHmTVLENV----MEAPIQVL-GLSKQEARERAVKYLAKVgidERAQGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1311 VGERQLLCIARALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIE 231
|
250
....*....|....
gi 1814750642 1386 EFDTPSVLLSNDSS 1399
Cdd:PRK10619 232 EEGAPEQLFGNPQS 245
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
546-722 |
2.10e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.43 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 546 THLGNLRlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWILNA--------- 616
Cdd:PRK11614 13 AHYGKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 ------TLRDNILFGKEF-DEERYNSVLNSCC-LRPDLailpnsdLTEIGERGANLSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK11614 90 rvfsrmTVEENLAMGGFFaERDQFQERIKWVYeLFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 1814750642 689 DPLSALDAHVGNHIFNSaIQKHLKSKTVLFITHQ 722
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDT-IEQLREQGMTIFLVEQ 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
555-751 |
2.30e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYN-IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-------------FAYVAQQawiLNA---- 616
Cdd:PRK10575 24 RTLLHpLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQ---LPAaegm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 617 TLRDNIL------------FGKEfDEERYNSVLNSCCLRPDLAILPNSdlteigerganLSGGQRQRISLARALYSDRDI 684
Cdd:PRK10575 101 TVRELVAigrypwhgalgrFGAA-DREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 685 YILDDPLSALD-AHVGNHIfnSAIQK--HLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK10575 169 LLLDEPTSALDiAHQVDVL--ALVHRlsQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
557-751 |
2.74e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.70 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQAWILNA-TLRDNI 622
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLSFPfTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 623 LFGKE---FDEERYNSVLNSCCLRPDLAILPNSDLTEigerganLSGGQRQRISLARAL------YSDRDIYILDDPLSA 693
Cdd:PRK13548 98 AMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 694 LD-AHvGNHIFNSAiqKHLKSK---TVLFITHQL----QYladCDEVIFMKEGCITERGTHEELMN 751
Cdd:PRK13548 171 LDlAH-QHHVLRLA--RQLAHErglAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVLT 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
559-752 |
2.92e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQM--SLLEGSIAVNGT--------------FAYVA----QQAWILNATL 618
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKevdvstvsdaidagLAYVTedrkGYGLNLIDDI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNI----LFG----------KEFDE-ERYnsvlnscclRPDLAILPNSDLTEIGergaNLSGGQRQRISLARALYSDRD 683
Cdd:NF040905 358 KRNItlanLGKvsrrgvidenEEIKVaEEY---------RKKMNIKTPSVFQKVG----NLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 684 IYILDDPLSALDahVGN--HIFnSAIQKHLKS-KTVLFITHQL-QYLADCDEVIFMKEGCIT-----ERGTHEELMNL 752
Cdd:NF040905 425 VLILDEPTRGID--VGAkyEIY-TIINELAAEgKGVIVISSELpELLGMCDRIYVMNEGRITgelprEEASQERIMRL 499
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
559-749 |
2.97e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---TFAYV--AQQAWI------LN----ATLRDNIL 623
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvRFRSPrdAQAAGIaiihqeLNlvpnLSVAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKE------FD----EERYNSVLNscclRPDLAILPNsdlTEIGErganLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:COG1129 102 LGREprrgglIDwramRRRARELLA----RLGLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 694 LDAHVGNHIFnsAIQKHLKSK--TVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:COG1129 171 LTEREVERLF--RIIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
557-733 |
3.12e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.47 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQ--MSLLEGSIAVNGTFAYVAQQAWI----------LNATLRDN--- 621
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPalARRLHLKKEQPGNHDRIEGLEHIdkvividqspIGRTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ---------ILF-----GKEFDEE----RYN-----SVLNSCC------------LRPDLAILPNSDLTEI--GERGANL 664
Cdd:cd03271 91 ytgvfdeirELFcevckGKRYNREtlevRYKgksiaDVLDMTVeealeffenipkIARKLQTLCDVGLGYIklGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 665 SGGQRQRISLARALySDRD----IYILDDPLSALDAHVGNHIFNsAIQKHL-KSKTVLFITHQLQYLADCDEVI 733
Cdd:cd03271 171 SGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLE-VLQRLVdKGNTVVVIEHNLDVIKCADWII 242
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1182-1390 |
3.48e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1182 QENLPLVLKKVSFTIKpKEKI-GIVGRTGSGKSSLgmalfrlVELSGGCIKidgVRISDIGLADLRSKLSIIPQEPVLFS 1260
Cdd:PRK13631 35 QENELVALNNISYTFE-KNKIyFIIGNSGSGKSTL-------VTHFNGLIK---SKYGTIQVGDIYIGDKKNNHELITNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1261 GT--------VRSNLDPFNQYTEDQIW-DALERTHMKECIAQLPLKLES--------EVMENGDNF--------SVGERQ 1315
Cdd:PRK13631 104 YSkkiknfkeLRRRVSMVFQFPEYQLFkDTIEKDIMFGPVALGVKKSEAkklakfylNKMGLDDSYlerspfglSGGQKR 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1316 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1390
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1187-1385 |
4.49e-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: 55.35 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1187 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGVRISDiglADLRSKLSIIPQEPVLFSG-T 1262
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1263 VRSNLdpfnQYTedqiwdALERTHmkECIAQLPLKLESEVMENGD------------NFSVGERQLLCIARALLRHCKIL 1330
Cdd:cd03234 98 VRETL----TYT------AILRLP--RKSSDAIRKKRVEDVLLRDlaltriggnlvkGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1331 ILDEATAAMDTETDLLIQETIREafadctmltIAHRLHTVLGS------------DRIMVLAQGQVV 1385
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQ---------LARRNRIVILTihqprsdlfrlfDRILLLSSGEIV 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1188-1396 |
4.66e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.91 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLADLRSKLSIIPQEpvlfSGTVRSN 1266
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQH----VGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LDPFNQYTedqiwdALE---------RTHMKECIAQLPLKLESEVMENGDN------FSVGERQLLCIARALLRHCKILI 1331
Cdd:PRK11264 94 FNLFPHRT------VLEniiegpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1332 LDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1396
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
560-749 |
4.77e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.78 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 560 IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-----------FAYVAQQ-AWILNATLRDNILFG-- 625
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSVRENMAYGlk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 626 -----KEFDEERynsvlnscclrpdlaILPNSDLTEIGE----RGANLSGGQRQRISLARALYSDRDIYILDDPLSALDA 696
Cdd:PRK11650 103 irgmpKAEIEER---------------VAEAARILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 697 HVGNH----IfnSAIQKHLKSkTVLFITH-QLQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:PRK11650 168 KLRVQmrleI--QRLHRRLKT-TSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
534-728 |
5.34e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 534 ERPSPEEEEGKHTHLGNLRLQRTLYNIDLEIEEGKL-----VGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVA 608
Cdd:PRK13409 327 EERPPRDESERETLVEYPDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 609 Q----------QAWILNATlrdnilfgKEFDEERYNSVLnsccLRP-DLAILPNSDLTEigerganLSGGQRQRISLARA 677
Cdd:PRK13409 407 QyikpdydgtvEDLLRSIT--------DDLGSSYYKSEI----IKPlQLERLLDKNVKD-------LSGGELQRVAIAAC 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 678 LYSDRDIYILDDPLSALDahVGNHIFNSAIQKHL---KSKTVLFITHQLQ---YLAD 728
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLD--VEQRLAVAKAIRRIaeeREATALVVDHDIYmidYISD 522
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
885-1101 |
6.22e-08 |
|
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: 55.94 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 885 KDNPLMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvr 964
Cdd:cd18545 34 GDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 965 lpfqAEMFIQNVIlvffcvgmiaGVFPWFLVAVGPLIILFS--------------ILHIVSRVL---IRELKRLDNITQS 1027
Cdd:cd18545 111 ----SDLLSNGLI----------NLIPDLLTLVGIVIIMFSlnvrlalvtlavlpLLVLVVFLLrrrARKAWQRVRKKIS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1028 PFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDNNQRPFflftcaMRwlAVRL-DLI--SIALITTTGLMIVLMHG 1101
Cdd:cd18545 177 NLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKAN------MR--AVRLnALFwpLVELISALGTALVYWYG 245
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
898-1061 |
6.47e-08 |
|
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: 55.64 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 898 ALSMAVMLILKAIrgVVFVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 971
Cdd:cd18557 39 ALILLAIYLLQSV--FTFVRYYLfniageRIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 972 FIQNVILVFFCVGMIAgVFPWFLVAVgpLIILFSILHIVSRVLIRELKRLDNITQSPFL---SHITSSIQGLATIHAYKK 1048
Cdd:cd18557 117 LLRNILQVIGGLIILF-ILSWKLTLV--LLLVIPLLLIASKIYGRYIRKLSKEVQDALAkagQVAEESLSNIRTVRSFSA 193
|
170
....*....|...
gi 1814750642 1049 GQEFLHRYQELLD 1061
Cdd:cd18557 194 EEKEIRRYSEALD 206
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
890-1065 |
6.72e-08 |
|
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: 55.94 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 890 MQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfQ- 968
Cdd:cd18577 46 VNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLI------Qd 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 969 --AE---MFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLIILFSIlhIVSRVLIR-ELKRLDNITQSpfLSHITSS 1036
Cdd:cd18577 120 giGEklgLLIQSLSTFIagFIIAFIYS---WkltlVLLATLPLIAIVGG--IMGKLLSKyTKKEQEAYAKA--GSIAEEA 192
|
170 180
....*....|....*....|....*....
gi 1814750642 1037 IQGLATIHAYKKGQEFLHRYQELLDNNQR 1065
Cdd:cd18577 193 LSSIRTVKAFGGEEKEIKRYSKALEKARK 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1189-1389 |
6.75e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG------GCIKIDG--VRISDIGLAdLRSKLSIIPQE----P 1256
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL------LKILSGnyqpdaGSILIDGqeMRFASTTAA-LAAGVAIIYQElhlvP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1257 VLfsgTVRSNLdpfnqytedqiwdalerthmkeCIAQLPLK--------LESEVMEN----GDNF---------SVGERQ 1315
Cdd:PRK11288 93 EM---TVAENL----------------------YLGQLPHKggivnrrlLNYEAREQlehlGVDIdpdtplkylSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1316 LLCIARALLRHCKILILDEATAAMDT-ETDLLIQeTIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQVVE-FDT 1389
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAEGRvILYVSHRMEEIFAlCDAITVFKDGRYVAtFDD 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
557-749 |
7.05e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------------TFAYVAQQAWILNAT 617
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFG-KEF----DEERYNSV--LNSCCLRPDLailpnsdlteIGERGANLSGGQRQRISLARALYSDRDIYILDDP 690
Cdd:PRK13641 103 VLKDVEFGpKNFgfseDEAKEKALkwLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 691 LSALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
906-1060 |
7.27e-08 |
|
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: 55.68 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 906 ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVRLPFQAEMFIQNVILVFFCVGM 985
Cdd:cd18782 57 VLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVIYIAV 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 986 IAgVFPWFL----VAVGPLIILFSILhiVSRVLIRELKRLdNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELL 1060
Cdd:cd18782 136 LF-SYSPLLtlvvLATVPLQLLLTFL--FGPILRRQIRRR-AEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRY 210
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
896-1065 |
8.42e-08 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 55.53 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 896 IYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmdevDVrlpfqaeM 971
Cdd:cd18570 43 IISIGLILLYLFQSllsyIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN------DA-------N 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 972 FIQNVI-----------LVFFCVGMIAGVFPW--FLVAVGPLIILFSILHIVSRVLIRELKRLdNITQSPFLSHITSSIQ 1038
Cdd:cd18570 110 KIREAIssttislfldlLMVIISGIILFFYNWklFLITLLIIPLYILIILLFNKPFKKKNREV-MESNAELNSYLIESLK 188
|
170 180
....*....|....*....|....*..
gi 1814750642 1039 GLATIHAYKKGQEFLHRYQELLDNNQR 1065
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLLK 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1188-1391 |
8.49e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSK-LSIIPQEPVLFSG-T 1262
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRREhFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1263 VRSNLD-PfnqytedQIWDALERTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1339
Cdd:PRK10535 103 AAQNVEvP-------AVYAGLERKQRLLRAQELlqRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1340 DT---ETDLLIQETIREafADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEfDTPS 1391
Cdd:PRK10535 176 DShsgEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPA 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
557-742 |
9.08e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGqmsLLEGSiavNGTFAYVAQQAWILN----ATLR-DNILFgkefdee 631
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGS---SGEVSLVGQPLHQMDeearAKLRaKHVGF------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 632 rynsVLNSCCLRPDLAILPNSDLTEI----------------------GER----GANLSGGQRQRISLARALYSDRDIY 685
Cdd:PRK10584 93 ----VFQSFMLIPTLNALENVELPALlrgessrqsrngakalleqlglGKRldhlPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 686 ILDDPLSALDAHVGNHIFN---SAIQKHlkSKTVLFITHQLQYLADCDEVIFMKEGCITE 742
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADllfSLNREH--GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
557-763 |
9.44e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.44 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWiLNATLR--DNI--------LFGK 626
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSG-LNGQLTgiENIelkglmmgLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 627 EFDEerynsvlnscclrpdlaILPNS-DLTEIG----ERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:PRK13545 119 KIKE-----------------IIPEIiEFADIGkfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 702 IFNSAIQKHLKSKTVLFITHQL-QYLADCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNL 763
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHSLsQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQM 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
554-735 |
1.01e-07 |
|
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: 53.48 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILgqmsllegsiavngtfayvaqqawilnatlrdnilfgKEFDEERY 633
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------------------------------YASGKARL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 634 NSVLNSCCLRPDLAILPNSDLTEIG------ERGAN-LSGGQRQRISLARALYSD--RDIYILDDPLSALDAHVGNHIFN 704
Cdd:cd03238 51 ISFLPKFSRNKLIFIDQLQFLIDVGlgyltlGQKLStLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLE 130
|
170 180 190
....*....|....*....|....*....|.
gi 1814750642 705 SAIQKHLKSKTVLFITHQLQYLADCDEVIFM 735
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1171-1405 |
1.88e-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: 53.88 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1171 EVTFENAEMRYqENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLS 1250
Cdd:cd03296 2 SIEVRNVSKRF-GDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1251 IIPQEPVLFSG-TVRSNL-----------DPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 1318
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1319 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1395
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|
gi 1814750642 1396 NDSSRFYAMF 1405
Cdd:cd03296 227 HPASPFVYSF 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
560-749 |
1.90e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.71 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 560 IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-FAYVAQQAWI----------------LNA--TLRD 620
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWRavrsdiqmifqdplasLNPrmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NIL---------FGKEFDEERYNSVLNSCCLRPDLailpnsdlteIGERGANLSGGQRQRISLARALYSDRDIYILDDPL 691
Cdd:PRK15079 120 IIAeplrtyhpkLSRQEVKDRVKAMMLKVGLLPNL----------INRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 692 SALDAHVGNHIFN--SAIQKHLkSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:PRK15079 190 SALDVSIQAQVVNllQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1170-1411 |
2.47e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1170 GEVTFENAEMRYQENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSL------------GMALFRLVELSGGCIKIDG 1234
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMiqltngliisetGQTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1235 VRisdiglaDLRSKLSIIPQEP--VLFSGTVRSNL--DPFNQYTEDQiwDALERTHMKECIAQLPlklESEVMENGDNFS 1310
Cdd:PRK13645 85 VK-------RLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKKVPELLKLVQLP---EDYVKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1311 VGERQLLCIARALLRHCKILILDEATAAMDT--ETDL--LIQETIREAFADCTMLTiaHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgEEDFinLFERLNKEYKKRIIMVT--HNMDQVLRiADEVIVMHEGKVI 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1814750642 1386 EFDTPSVLLSN---------DSSRFYAMFAAAENK 1411
Cdd:PRK13645 231 SIGSPFEIFSNqelltkieiDPPKLYQLMYKLKNK 265
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
555-738 |
2.55e-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: 52.63 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISsILGQ---MSLLEGSIAVNG-----TFA----YVAQQ-AWILNATLRDN 621
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLD-VLAGrktAGVITGEILINGrpldkNFQrstgYVEQQdVHSPNLTVREA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFgkefdeerynsvlnSCCLRpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:cd03232 100 LRF--------------SALLR-------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1814750642 702 IFNsAIQKHLKS-KTVLFITHQ--LQYLADCDEVIFMKEG 738
Cdd:cd03232 147 IVR-FLKKLADSgQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1179-1386 |
2.58e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.55 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1179 MRYQENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----VELSGGCIKIDGVRISdigLADLRSKL-SIIP 1253
Cdd:PRK10418 10 IALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVA---PCALRGRKiATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1254 QEPvlfsgtvRSNLDPFNQYtedqiwdaleRTHMKECI---------AQLPLKLESEVMENGD--------NFSVGERQL 1316
Cdd:PRK10418 86 QNP-------RSAFNPLHTM----------HTHARETClalgkpaddATLTAALEAVGLENAArvlklypfEMSGGMLQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1317 LCIARALLRHCKILILDEATaamdTETDLLIQETIREAFADCT------MLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPT----TDLDVVAQARILDLLESIVqkralgMLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
555-738 |
2.64e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLissilgqMSLL---------EGSIAVNG---TFAYV--AQQAWIL------ 614
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTL-------MKVLsgvyphgtyEGEIIFEGeelQASNIrdTERAGIAiihqel 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 615 ----NATLRDNILFGKE---FDEERYNSVLNSC--CLRP-DLAILPNsdlTEIGergaNLSGGQRQRISLARALYSDRDI 684
Cdd:PRK13549 92 alvkELSVLENIFLGNEitpGGIMDYDAMYLRAqkLLAQlKLDINPA---TPVG----NLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 685 YILDDPLSALDAHVGNHIFNsaIQKHLKSKTV--LFITHQLQYLAD-CDEVIFMKEG 738
Cdd:PRK13549 165 LILDEPTASLTESETAVLLD--IIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
557-747 |
2.64e-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: 52.53 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMS--LLEGSIAVNGTFayvaqqawILNATLRDNILFG--KEFDE-E 631
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGED--------ITDLPPEERARLGifLAFQYpP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 632 RYNSVLNSCCLRpdlailpnsdltEIGErgaNLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQKHL 711
Cdd:cd03217 88 EIPGVKNADFLR------------YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLRE 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1814750642 712 KSKTVLFITHQlQYLADC---DEVIFMKEGCITERGTHE 747
Cdd:cd03217 153 EGKSVLIITHY-QRLLDYikpDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
555-745 |
3.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.59 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT---------------------FAYVAQQawI 613
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvglvFQFPESQ--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 614 LNATLRDNILFG-------KEFDEERynsvlnsccLRPDLAILPNSDltEIGERGA-NLSGGQRQRISLARALYSDRDIY 685
Cdd:PRK13649 99 FEETVLKDVAFGpqnfgvsQEEAEAL---------AREKLALVGISE--SLFEKNPfELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 686 ILDDPLSALDAHVGNHIFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGT 745
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
664-749 |
3.41e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 664 LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFN--SAIQKHLkSKTVLFITHQLQYLAD-CDEVIFMKEGCI 740
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQKEM-SMGVIFITHDMGVVAEiADRVLVMYQGEA 247
|
....*....
gi 1814750642 741 TERGTHEEL 749
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
892-1101 |
3.53e-07 |
|
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: 53.58 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 892 YYASIYALSMAVMLILKAIRgvvfvkgtlrassrlhDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 971
Cdd:cd18552 56 SYLQTYLMAYVGQRVVRDLR----------------NDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 972 FIQNVILVFFCVG-MIagVFPWFL----VAVGPLIILfsILHIVSRVL----IRELKRLDNITqspflSHITSSIQGLAT 1042
Cdd:cd18552 120 LVRDPLTVIGLLGvLF--YLDWKLtliaLVVLPLAAL--PIRRIGKRLrkisRRSQESMGDLT-----SVLQETLSGIRV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1043 IHAYKKGQEFLHRYQELLDNNQRpfflftcAMRWLAVRLDLIS--IALITTTGLMIVLMHG 1101
Cdd:cd18552 191 VKAFGAEDYEIKRFRKANERLRR-------LSMKIARARALSSplMELLGAIAIALVLWYG 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1188-1397 |
3.95e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQE-PVLFSGTVRSn 1266
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVRE- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LDPFNQYTedqiWD-------ALERTHMKECIAQLPLK-LESEVMengDNFSVGERQLLCIARALLRHCKILILDEATAA 1338
Cdd:PRK10575 105 LVAIGRYP----WHgalgrfgAADREKVEEAISLVGLKpLAHRLV---DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 1339 MD----TETDLLIQETIREafadcTMLTIAHRLHTVLGS----DRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:PRK10575 178 LDiahqVDVLALVHRLSQE-----RGLTVIAVLHDINMAarycDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
897-1101 |
4.18e-07 |
|
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: 53.26 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 897 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 972
Cdd:cd18576 38 IALLLLGLFLLQAVfsffRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 973 IQNVILVFFCVGMIAGVFP---WFLVAVGPLIILFSIlhIVSRVlIREL--KRLDNITQSpfLSHITSSIQGLATIHAYK 1047
Cdd:cd18576 118 LRQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAV--LFGRR-IRKLskKVQDELAEA--NTIVEETLQGIRVVKAFT 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1048 KGQEFLHRYQELLDNnqrpffLFTCAMRWLAVRLDLIS-IALITTTGLMIVLMHG 1101
Cdd:cd18576 193 REDYEIERYRKALER------VVKLALKRARIRALFSSfIIFLLFGAIVAVLWYG 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1192-1385 |
4.89e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIP----QEPVLFSGTVRSN 1266
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LD--------PFNQYTeDQIWdalERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:PRK11288 352 INisarrhhlRAGCLI-NNRW---EAENADRFIRSLNIKtpsREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1336 TAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1187-1396 |
4.90e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1187 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLadlrsklsiiPQEPVLFSGTVRS- 1265
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GL----------PGHQIARMGVVRTf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 -NLDPFNQYTedqiwdALE------RTHMKECIAQLPLKL------ESEVMENG-----------------DNFSVGERQ 1315
Cdd:PRK11300 87 qHVRLFREMT------VIEnllvaqHQQLKTGLFSGLLKTpafrraESEALDRAatwlervgllehanrqaGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1316 LLCIARALLRHCKILILDEATAAMD-TETDLLiQETI---REAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1390
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNpKETKEL-DELIaelRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTP 238
|
....*.
gi 1814750642 1391 SVLLSN 1396
Cdd:PRK11300 239 EEIRNN 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
554-695 |
5.16e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.69 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-FAYVAQ---------QAWIL--NATLRDN 621
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPPyqrpinmmfQSYALfpHMTVEQN 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 622 ILFGKEFDEERYNSVLNSCClrpdlAILPNSDLTEIGERGAN-LSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
554-722 |
5.29e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT------------FAYVAQQAWI-LNATLRD 620
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqLCFVGHRSGInPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILFGKEFDEEryNSVLNSCCLRPDLAILpnsdlteIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGN 700
Cdd:PRK13540 94 NCLYDIHFSPG--AVGITELCRLFSLEHL-------IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|...
gi 1814750642 701 HIFnSAIQKH-LKSKTVLFITHQ 722
Cdd:PRK13540 165 TII-TKIQEHrAKGGAVLLTSHQ 186
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1189-1404 |
5.40e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADL---RSKLSiiPQEPVLFsgtvrs 1265
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGS-IQFAGQPLEAWSAAELarhRAYLS--QQQTPPF------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NLDPFnQY---------TEDQIWDALERthmkecIAQLpLKLESEVMENGDNFSVGERQ-------LLCIARALLRHCKI 1329
Cdd:PRK03695 83 AMPVF-QYltlhqpdktRTEAVASALNE------VAEA-LGLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAGQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1330 LILDEATAAMD----TETDLLIQETIREAFAdctMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTP-SVLLSNDSSRFYA 1403
Cdd:PRK03695 155 LLLDEPMNSLDvaqqAALDRLLSELCQQGIA---VVMSSHDLnHTLRHADRVWLLKQGKLLASGRRdEVLTPENLAQVFG 231
|
.
gi 1814750642 1404 M 1404
Cdd:PRK03695 232 V 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
665-749 |
5.75e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.19 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 665 SGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHI----------FNSAIqkhlksktvLFITHQLQYLAD-CDEVI 733
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQImtllnelkreFNTAI---------IMITHDLGVVAGiCDKVL 233
|
90
....*....|....*.
gi 1814750642 734 FMKEGCITERGTHEEL 749
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
836-1101 |
7.43e-07 |
|
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: 52.49 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 836 LAFLVILSLFMLNVGSTafsnwwLSYWIKQGSGnttvtQENRTSVSssmkdnplmQYYASIYALSmAVMLILKAIRgVVF 915
Cdd:cd18575 2 LIALLIAAAATLALGQG------LRLLIDQGFA-----AGNTALLN---------RAFLLLLAVA-LVLALASALR-FYL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 916 VkGTL--RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVFPWF 993
Cdd:cd18575 60 V-SWLgeRVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLF-ITSPK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 994 L----VAVGPLIILFSIlhivsrVLIRELKRLDNITQSPFL---SHITSSIQGLATIHAYKKGQEFLHRYQELLDNNqrp 1066
Cdd:cd18575 138 LtllvLLVIPLVVLPII------LFGRRVRRLSRASQDRLAdlsAFAEETLSAIKTVQAFTREDAERQRFATAVEAA--- 208
|
250 260 270
....*....|....*....|....*....|....*.
gi 1814750642 1067 fflFTCAMRWLAVRLDLISIA-LITTTGLMIVLMHG 1101
Cdd:cd18575 209 ---FAAALRRIRARALLTALViFLVFGAIVFVLWLG 241
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
895-1099 |
9.13e-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: 52.13 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 895 SIYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmDEVDVRlpfqaE 970
Cdd:cd18555 42 NVLGIGILILFLLYGlfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAN---SNVYIR-----Q 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 971 MFIQNVI--------LVFFCVGMIagVFPWFL----VAVGPLIILFSILhivSRVLIRELKRLDNITQSPFLSHITSSIQ 1038
Cdd:cd18555 114 ILSNQVIsliidlllLVIYLIYML--YYSPLLtlivLLLGLLIVLLLLL---TRKKIKKLNQEEIVAQTKVQSYLTETLY 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1039 GLATI-------HAYKKgqeFLHRYQELLDNNQRpfflftcAMRWLAVrLDLISIALITTTGLMIVLM 1099
Cdd:cd18555 189 GIETIkslgsekNIYKK---WENLFKKQLKAFKK-------KERLSNI-LNSISSSIQFIAPLLILWI 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
664-751 |
9.31e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 664 LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFnsAIQKHLKSK---TVLFITHQL---QYLAdcDEVIFMKE 737
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL--QLLRELQQElnmGLLFITHNLsivRKLA--DRVAVMQN 232
|
90
....*....|....
gi 1814750642 738 GCITERGTHEELMN 751
Cdd:PRK15134 233 GRCVEQNRAATLFS 246
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1117-1366 |
9.40e-07 |
|
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: 53.60 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1117 QLTGlfqFTVRLASetearFTSV-ERIN--HYIKTLSLEAPARIKNKSPSSDWPQEGEVTFENAEMRYqENLPLV----- 1188
Cdd:TIGR00954 395 RLAG---FTARVDT-----LLQVlDDVKsgNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKF-ENIPLVtpngd 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 --LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVelsGGCIKIDGVRISdiglADLRSKLSIIPQEPVLFSGTVRsn 1266
Cdd:TIGR00954 466 vlIESLSFEVPSGNNLLICGPNGCGKSSL----FRIL---GELWPVYGGRLT----KPAKGKLFYVPQRPYMTLGTLR-- 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 ldpfnqyteDQIW--DALERTHMK-------ECIAQLpLKLESEVMENG---------DNFSVGERQLLCIARALLRHCK 1328
Cdd:TIGR00954 533 ---------DQIIypDSSEDMKRRglsdkdlEQILDN-VQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQ 602
|
250 260 270
....*....|....*....|....*....|....*...
gi 1814750642 1329 ILILDEATAAMDTETDLLIQETIREafADCTMLTIAHR 1366
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
663-728 |
1.39e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.39e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 663 NLSGGQRQRISLARALYSDRDIYILDDPLSALDahVGNHIfNSA--IQKHLKSKTVLFITHQ---LQYLAD 728
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRL-NVArlIRELAEGKYVLVVEHDlavLDYLAD 279
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1189-1386 |
1.49e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDG--VRISDIGLADlRSKLSIIPQE--- 1255
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKV-----LSGvyphgsyeGEILFDGevCRFKDIRDSE-ALGIVIIHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1256 -PVLfsgTVRSNLDPFNQYTEDQI--WDALERtHMKECIAQLPLKlesevmENGD----NFSVGERQLLCIARALLRHCK 1328
Cdd:NF040905 90 iPYL---SIAENIFLGNERAKRGVidWNETNR-RARELLAKVGLD------ESPDtlvtDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1329 ILILDEATAAMDtETD---LLiqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1386
Cdd:NF040905 160 LLILDEPTAALN-EEDsaaLL--DLLLELKAqGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
555-749 |
1.66e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT--------------FAYVAQQAWIL-NATLR 619
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFG---KEFDEERYNSVLN--SCCLRPDLAilpnsdlteigerGANLSGGQRQRISLARALYSDRDIYILDDPLSAL 694
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 695 DAHVGNHIFnSAIQKhLKSKTV--LFITHQLQYL-ADCDEVIFMKEGCITERGTHEEL 749
Cdd:PRK15439 172 TPAETERLF-SRIRE-LLAQGVgiVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1188-1343 |
1.69e-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: 52.63 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKI-DGVRISDIGLADLRS--KLSIIPQEPVL-FSGTV 1263
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTL--------------LRImAGVDKDFNGEARPQPgiKVGYLPQEPQLdPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1264 RSN-----------LDPFNQ----YTE-DQIWDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFSVG 1312
Cdd:TIGR03719 86 RENveegvaeikdaLDRFNEisakYAEpDADFDKLaaEQAELQEIIDAADAwDLDSQLeiaMDalrcpPWDadvtKLSGG 165
|
170 180 190
....*....|....*....|....*....|.
gi 1814750642 1313 ERQLLCIARALLRHCKILILDEATAAMDTET 1343
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
879-1062 |
1.83e-06 |
|
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: 51.36 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 879 SVSSSMKDNPLMQYYASIYALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRF 954
Cdd:cd18573 25 VASKESGDIEIFGLSLKTFALALLGVFVVGAAanfgRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 955 SKDMDEVdvrlpfqAEMFIQNV-------ILVFFCVGMIAGVFP---WFLVAVGPLIILFSIlhivsrVLIRELKRLDNI 1024
Cdd:cd18573 105 SSDTSVV-------GKSLTQNLsdglrslVSGVGGIGMMLYISPkltLVMLLVVPPIAVGAV------FYGRYVRKLSKQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1814750642 1025 TQSPfLSHITSS----IQGLATIHAYKKGQEFLHRYQELLDN 1062
Cdd:cd18573 172 VQDA-LADATKVaeerLSNIRTVRAFAAERKEVERYAKKVDE 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
557-695 |
2.04e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI-----------------AVNGT-FAYVAQ----QAWIL 614
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarlqqdpprNVEGTvYDFVAEgieeQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 615 NATLRDNILFGKEFDEE----------------------RYNSVLNSCCLRPDlailpnSDLTEigerganLSGGQRQRI 672
Cdd:PRK11147 99 KRYHDISHLVETDPSEKnlnelaklqeqldhhnlwqlenRINEVLAQLGLDPD------AALSS-------LSGGWLRKA 165
|
170 180
....*....|....*....|...
gi 1814750642 673 SLARALYSDRDIYILDDPLSALD 695
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
560-749 |
2.13e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 50.61 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 560 IDLEIEEGKLVGICGSVGSGKTSLISSI-----LGQMSLLEGSIAVNGTFAY--------VAQQAWIL--------NATL 618
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpieVRREVGMVfqypnpfpHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNILFG----------KEFDEeRYNSVLNSCCLRPDLAilpnsdlTEIGERGANLSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK14267 103 YDNVAIGvklnglvkskKELDE-RVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 689 DPLSALDAhVGNHIFNSAIQKHLKSKTVLFITHQ-LQYLADCDEVIFMKEGCITERGTHEEL 749
Cdd:PRK14267 175 EPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1189-1383 |
2.25e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS--------DIGLADLRSKLSIIPQEPV--- 1257
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQLTIaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1258 LFSGtvRSNLDPFNQYTEDQIW---DALerthmkecIAQLPLKLESEVMEnGDnFSVGERQLLCIARALLRHCKILILDE 1334
Cdd:PRK10762 100 IFLG--REFVNRFGRIDWKKMYaeaDKL--------LARLNLRFSSDKLV-GE-LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1335 ATAAM-DTETDLLIQeTIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 1383
Cdd:PRK10762 168 PTDALtDTETESLFR-VIRELKSqGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1188-1397 |
2.26e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.96 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEP--VLFSGTVRS 1265
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1266 NL--DPFN-----QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 1338
Cdd:PRK13652 99 DIafGPINlgldeETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 1339 MDTETdllIQETIR--EAFADCTMLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSND 1397
Cdd:PRK13652 168 LDPQG---VKELIDflNDLPETYGMTVIFSTHQLdlvpEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
560-742 |
2.54e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 560 IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGtfAYVAQQAW-----ILNATLRDNILF-------GKE 627
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPedyrkLFSAVFTDFHLFdqllgpeGKP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 628 FDEERYNSVLNSCCLrpdlailpNSDLTEIGERGAN--LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVgNHIFNS 705
Cdd:PRK10522 420 ANPALVEKWLERLKM--------AHKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 1814750642 706 AIQKHLKS--KTVLFITHQLQYLADCDEVIFMKEGCITE 742
Cdd:PRK10522 491 VLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
559-724 |
2.62e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 559 NIDLEIEEGKLVGICGSVGSGKTSLISSiLGQMSLL------EGSIAVNGTFAY---------------VAQQAWILNAT 617
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRC-FNRLNDLipgfrvEGKVTFHGKNLYapdvdpvevrrrigmVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 618 LRDNILFGK-------EFDE--ERynsvlnscCLRPdlAILPNSDLTEIGERGANLSGGQRQRISLARALYSDRDIYILD 688
Cdd:PRK14243 107 IYDNIAYGAringykgDMDElvER--------SLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1814750642 689 DPLSALDAhvgnhIFNSAIQ---KHLKSK-TVLFITHQLQ 724
Cdd:PRK14243 177 EPCSALDP-----ISTLRIEelmHELKEQyTIIIVTHNMQ 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1192-1386 |
2.92e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.31 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL---------RSKLSIIPQEP------ 1256
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdglrm 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1257 -VLFSGTVRSNLDPF--NQYTE--DQIWDALERTHMKEC-IAQLPlklesevmengDNFSVGERQLLCIARALLRHCKIL 1330
Cdd:PRK11701 105 qVSAGGNIGERLMAVgaRHYGDirATAGDWLERVEIDAArIDDLP-----------TTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1331 ILDEATAAMDTET-----DLLiQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVE 1386
Cdd:PRK11701 174 FMDEPTGGLDVSVqarllDLL-RGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
547-697 |
2.93e-06 |
|
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: 50.13 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 547 HLGNLRLQrTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVN---------------------GTFA 605
Cdd:COG4778 18 LQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 606 YVAQqawILNATLRDNIL-----------FGKEFDEERYNSVLNSCCLRPDLAILPNsdlteigergANLSGGQRQRISL 674
Cdd:COG4778 97 YVSQ---FLRVIPRVSALdvvaepllergVDREEARARARELLARLNLPERLWDLPP----------ATFSGGEQQRVNI 163
|
170 180
....*....|....*....|...
gi 1814750642 675 ARALYSDRDIYILDDPLSALDAH 697
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
554-733 |
3.15e-06 |
|
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: 49.95 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSL-------------ISSI-------LGQMS-----LLEG---SIAVN---- 601
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLsayarqfLGQMDkpdvdSIEGlspAIAIDqktt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 602 -----GTFAYVAQqawiLNATLRdnILFGKEFDEERYNSvlnscclrpdlailpnsdLTEIG------ERGAN-LSGGQR 669
Cdd:cd03270 88 srnprSTVGTVTE----IYDYLR--LLFARVGIRERLGF------------------LVDVGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 670 QRISLARALYSDRD--IYILDDPLSALDAHvGNHIFNSAIqKHLKSK--TVLFITHQLQYLADCDEVI 733
Cdd:cd03270 144 QRIRLATQIGSGLTgvLYVLDEPSIGLHPR-DNDRLIETL-KRLRDLgnTVLVVEHDEDTIRAADHVI 209
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
550-749 |
3.19e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 550 NLRLQ----RTLYNIDLEIEEGKLVGICGSVGSGKTSLISsILGQMSLLEGSIAVNGTFAYVAQQAW------------- 612
Cdd:PRK14247 8 DLKVSfgqvEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFkmdvielrrrvqm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 613 -------ILNATLRDNILFGKEFD---------EERYNSVLNSCCLRPDLAilpnsdlTEIGERGANLSGGQRQRISLAR 676
Cdd:PRK14247 87 vfqipnpIPNLSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 677 ALYSDRDIYILDDPLSALDAHvgnhifNSAIQKHL-----KSKTVLFITHQLQYLADC-DEVIFMKEGCITERGTHEEL 749
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPE------NTAKIESLflelkKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREV 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1188-1353 |
3.20e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.01 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVEL-SGGCIKIDG------VRISDIGLADLRSKLSIIPQE----P 1256
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEMpRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1257 VLfsgTVRSNL--DPFN------QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCK 1328
Cdd:PRK11124 96 HL---TVQQNLieAPCRvlglskDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQRVAIARALMMEPQ 161
|
170 180
....*....|....*....|....*
gi 1814750642 1329 ILILDEATAAMDTETDLLIQETIRE 1353
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1188-1386 |
3.40e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK--------LSIIP--- 1253
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1254 -QEPVLFSGTVRSNLDpfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1332
Cdd:PRK10584 105 aLENVELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1333 DEATAAMDTET-----DLLIQETIREAfadCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1386
Cdd:PRK10584 171 DEPTGNLDRQTgdkiaDLLFSLNREHG---TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
555-738 |
4.08e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI--------------AVNGTFAYVAQQA-WILNATLR 619
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlfqgkeidfksskeALENGISMVHQELnLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGkefdeeRYNS----VLNSCCLRPDLAILPNSDL-TEIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSAL 694
Cdd:PRK10982 92 DNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIdIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1814750642 695 DAHVGNHIFNsaIQKHLKSK--TVLFITHQL-QYLADCDEVIFMKEG 738
Cdd:PRK10982 166 TEKEVNHLFT--IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
892-1103 |
4.33e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 50.10 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 892 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 971
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 972 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLIILFsilhIVSRVLIRELKRLDNITQSPFlSHITSSIQ----GLATIHAY 1046
Cdd:cd18541 121 LVDALFLGVLVLVMMFTISPKLtLIALLPLPLLA----LLVYRLGKKIHKRFRKVQEAF-SDLSDRVQesfsGIRVIKAF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1047 KKGQEFLHRYQELLDNNQRpfflftcamRWLA-VRLD---LISIALITTTGLMIVL-------MHGQI 1103
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVE---------KNLRlARVDalfFPLIGLLIGLSFLIVLwyggrlvIRGTI 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1189-1384 |
4.48e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI--------GLA---DLRSKLSIIPQEPV 1257
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaneainhGFAlvtEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1258 LFSGTVrSNLDPFNQYtedqiWDALERTHMKE----CIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILD 1333
Cdd:PRK10982 344 GFNSLI-SNIRNYKNK-----VGLLDNSRMKSdtqwVIDSMRVKTPGHRTQIG-SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1334 EATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 1384
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
867-1065 |
4.52e-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: 50.35 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 867 SGNTTVTQENRTSVSSSMKDNPL---MQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFD 943
Cdd:cd18558 32 GGMTNITGNSSGLNSSAGPFEKLeeeMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 944 TTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLIILFSIL--HIVSRVLI 1015
Cdd:cd18558 112 VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGtgFIIGFIRG---WkltlVILAISPVLGLSAVVwaKILSGFTD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1016 RELKRLDNITQSPflshiTSSIQGLATIHAYKKGQEFLHRYQELLDNNQR 1065
Cdd:cd18558 189 KEKKAYAKAGAVA-----EEVLEAFRTVIAFGGQQKEETRYAQNLEIAKR 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
560-721 |
5.12e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 560 IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAwilnatlrdnilfgkefdeeRYNSVLNS 639
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--------------------RFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 640 C-CLRPDLAIL-----------------PNSDLTEIGERG------ANLSGGQRQRISLARALYSDRDIYILDDPLSALD 695
Cdd:PRK13543 90 LpGLKADLSTLenlhflcglhgrrakqmPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*..
gi 1814750642 696 AHvGNHIFNSAIQKHLKSK-TVLFITH 721
Cdd:PRK13543 170 LE-GITLVNRMISAHLRGGgAALVTTH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
555-755 |
6.89e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 555 RTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGTFAYVAQQAWILNA---------------TLR 619
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgvaiiyqelhlvpemTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 620 DNILFGK------EFDEERYNSVLNSCCLRPDLAILPNSDLteigergANLSGGQRQRISLARALYSDRDIYILDDPLSA 693
Cdd:PRK11288 98 ENLYLGQlphkggIVNRRLLNYEAREQLEHLGVDIDPDTPL-------KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1814750642 694 LDAHVGNHIFnsAIQKHLKS--KTVLFITHQL-QYLADCDEVIFMKEGCITErgTHEELMNLNGD 755
Cdd:PRK11288 171 LSAREIEQLF--RVIRELRAegRVILYVSHRMeEIFALCDAITVFKDGRYVA--TFDDMAQVDRD 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1204-1388 |
7.10e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1204 IVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIsdigLADLRSKLSIIP---------QEPVLFSG-TVRSNL----DP 1269
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNG-RV----LFDAEKGICLPPekrrigyvfQDARLFPHyKVRGNLrygmAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1270 FNQYTEDQIWDALERTHMkecIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDT--ETDLL- 1346
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprKRELLp 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1814750642 1347 -IQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1388
Cdd:PRK11144 170 yLERLARE--INIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
557-749 |
7.41e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.31 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-TFAYVAQQawILNATLRDNILFGKEFDEERYNS 635
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYDKKS--LLEVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 636 VLNSCCLRPDLAILPNSD--------LTEIGERG------ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNH 701
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEvekrvkeaLKAVGMEGfenkppHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1814750642 702 IFNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITERGTHEEL 749
Cdd:PRK13639 176 IMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1191-1402 |
7.79e-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: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1191 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPF 1270
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1271 NQYTEDQIWD--ALERTHMKECIAqlplkLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQ 1348
Cdd:TIGR01257 1027 YAQLKGRSWEeaQLEMEAMLEDTG-----LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 1349 ETIREAFADCTMLTIAHRLHT--VLGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFY 1402
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEadLLG-DRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1187-1392 |
1.05e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1187 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR-SKLSIIPQEP-----VLfS 1260
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRlgrglVP-D 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1261 GTVRSNLDpFNQYTEDQI-------WDALeRTHMKECIAQLPLK---LESEVmengDNFSVGERQLLCIARALLRHCKIL 1330
Cdd:COG3845 351 MSVAENLI-LGRYRRPPFsrggfldRKAI-RAFAEELIEEFDVRtpgPDTPA----RSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 1331 I-------LDEATAAMdtetdllIQETIREAfAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFDTPSV 1392
Cdd:COG3845 425 IaaqptrgLDVGAIEF-------IHQRLLEL-RDagAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEA 489
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
910-1021 |
1.10e-05 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 48.85 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 910 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF-FCVGMIag 988
Cdd:cd18784 55 IRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIgVIVFMF-- 132
|
90 100 110
....*....|....*....|....*....|...
gi 1814750642 989 VFPWFLVAVgpLIILFSILHIVSRVLIRELKRL 1021
Cdd:cd18784 133 KLSWQLSLV--TLIGLPLIAIVSKVYGDYYKKL 163
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1189-1385 |
1.10e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 48.73 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiglADLRSKLSIIPQE-------PVLFSG 1261
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 TVRSN-------LDPFNQYTEDQIWDALERTHMkeciaqlplkLESEVMENGDnFSVGERQLLCIARALLRHCKILILDE 1334
Cdd:PRK15056 100 VVMMGryghmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 1335 ATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVV 1385
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
557-749 |
1.13e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 48.69 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 557 LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT-FAYVAQQawILNatLRDNI-LFGKEFDEERYN 634
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKG--LMK--LRESVgMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 635 -SVLNSCCLRPDLAILPNSDLTEIGERGAN--------------LSGGQRQRISLARALYSDRDIYILDDPLSALDAhVG 699
Cdd:PRK13636 98 aSVYQDVSFGAVNLKLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP-MG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1814750642 700 nhifNSAIQKHLKSK------TVLFITHQLQYLA-DCDEVIFMKEGCITERGTHEEL 749
Cdd:PRK13636 177 ----VSEIMKLLVEMqkelglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
554-722 |
1.14e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.88 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYN-IDLEIEEGKLVGICGSVGSGKTSLISSILG--QMSLLEGSIAVNG---------TFAYVAQQAWIL-NATLRD 620
Cdd:PLN03211 80 ERTILNgVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNrkptkqilkRTGFVTQDDILYpHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NILF------GKEFDEERYNSVLNSCCLRPDLAILPNSDLTEIGERGanLSGGQRQRISLARALYSDRDIYILDDPLSAL 694
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180
....*....|....*....|....*...
gi 1814750642 695 DAHVGNHIFNSAIQKHLKSKTVLFITHQ 722
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
545-749 |
1.33e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.65 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 545 HTHLGNLRlqrTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-------------TFAYVAQQA 611
Cdd:PRK13652 11 YSYSGSKE---ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 612 --WILNATLRDNILFGK---EFDEE----RYNSVLNSCCLRPDLAILPNsdlteigergaNLSGGQRQRISLARALYSDR 682
Cdd:PRK13652 88 ddQIFSPTVEQDIAFGPinlGLDEEtvahRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 683 DIYILDDPLSALDAHVGNHIF---NSAIQKHlkSKTVLFITHQLQYLADCDEVIF-MKEGCITERGTHEEL 749
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIdflNDLPETY--GMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEI 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
552-754 |
1.36e-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: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 552 RLQRTLYnidleieEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-----TFAYVAQ------QAWIL--NATL 618
Cdd:TIGR01257 948 RLNITFY-------ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietNLDAVRQslgmcpQHNILfhHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 619 RDNILF-----GKEFDEERYNSVlnscclrpdlAILPNSDLT-EIGERGANLSGGQRQRISLARALYSDRDIYILDDPLS 692
Cdd:TIGR01257 1021 AEHILFyaqlkGRSWEEAQLEME----------AMLEDTGLHhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 693 ALDAHVGNHIFNsAIQKHLKSKTVLFITHQLQYlADC--DEVIFMKEGCITERGTHEELMNLNG 754
Cdd:TIGR01257 1091 GVDPYSRRSIWD-LLLKYRSGRTIIMSTHHMDE-ADLlgDRIAIISQGRLYCSGTPLFLKNCFG 1152
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
563-728 |
1.59e-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: 46.80 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 563 EIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG-TFAYVAQQAwilnatlrdnilfgkefdeerynsvlnscc 641
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQYI------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 642 lrpdlailpnsdlteigergaNLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIfnSAIQKHL---KSKTVLF 718
Cdd:cd03222 71 ---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA--ARAIRRLseeGKKTALV 127
|
170
....*....|...
gi 1814750642 719 ITHQL---QYLAD 728
Cdd:cd03222 128 VEHDLavlDYLSD 140
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
547-756 |
1.83e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 547 HLGNLRlQRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSI--------------AVNGTFAYVAQQAw 612
Cdd:PRK10982 255 NLTSLR-QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTItlhgkkinnhnaneAINHGFALVTEER- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 613 ilnatlRDNILFGKeFDEErYNSVL-NSCCLRPDLAILPNSDL-------------------TEIGergaNLSGGQRQRI 672
Cdd:PRK10982 333 ------RSTGIYAY-LDIG-FNSLIsNIRNYKNKVGLLDNSRMksdtqwvidsmrvktpghrTQIG----SLSGGNQQKV 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 673 SLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQKHLKSKTVLFITHQL-QYLADCDEVIFMKEGCI-----TERGTH 746
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVagivdTKTTTQ 480
|
250
....*....|
gi 1814750642 747 EELMNLNGDY 756
Cdd:PRK10982 481 NEILRLASLH 490
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
902-1142 |
2.22e-05 |
|
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: 47.86 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 902 AVMLILKAIRGVVFV-------KGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdVRLPFQAEMFIQ 974
Cdd:cd18543 43 LLLLALGVAEAVLSFlrrylagRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 975 NVILVFFCVGMIAGVFPWF-LVAVGPLIILFsilhIVSRVLIRELKRLDNITQS---PFLSHITSSIQGLATIHAYKKGQ 1050
Cdd:cd18543 122 NLLTLVVGLVVMLVLSPPLaLVALASLPPLV----LVARRFRRRYFPASRRAQDqagDLATVVEESVTGIRVVKAFGRER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1051 EFLHRYQELLDNnqrpffLFTCAMRwlAVRLDLISIALITT---TGLMIVL-------MHGQIPpayAG--LA-ISYAVQ 1117
Cdd:cd18543 198 RELDRFEAAARR------LRATRLR--AARLRARFWPLLEAlpeLGLAAVLalggwlvANGSLT---LGtlVAfSAYLTM 266
|
250 260
....*....|....*....|....*
gi 1814750642 1118 LTGLFQFTVRLASETEARFTSVERI 1142
Cdd:cd18543 267 LVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1152-1384 |
2.54e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 47.36 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1152 EAPARIKNKSPssdwpqegeVTFENAEMRYQENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcik 1231
Cdd:PRK11247 2 MNTARLNQGTP---------LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1232 idGVRISDIGLADLRSKLSIIPQEPVLF-------------SGTVRsnldpfnqyteDQIWDALERTHMKECIAQLPLKL 1298
Cdd:PRK11247 68 --ELLAGTAPLAEAREDTRLMFQDARLLpwkkvidnvglglKGQWR-----------DAALQALAAVGLADRANEWPAAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1299 esevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI-----REAFadcTMLTIAHRL-HTVLG 1372
Cdd:PRK11247 135 -----------SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDVsEAVAM 200
|
250
....*....|..
gi 1814750642 1373 SDRIMVLAQGQV 1384
Cdd:PRK11247 201 ADRVLLIEEGKI 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1192-1388 |
3.19e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1192 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDigladlRSklsiiPQEPvLFSGTVrsnldpfn 1271
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT------RS-----PQDG-LANGIV-------- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1272 qY-TEDQIWDAL-----ERTHMKEC-IAQLP-----LKLESEVMENGD-----------------NFSVGERQLLCIARA 1322
Cdd:PRK10762 331 -YiSEDRKRDGLvlgmsVKENMSLTaLRYFSraggsLKHADEQQAVSDfirlfniktpsmeqaigLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1814750642 1323 LLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 1388
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGmSDRILVMHEGRISgEFT 478
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
653-728 |
3.45e-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: 48.24 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 653 DLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLSALDahVGNHIfNSA--IQKHLKS-KTVLFITHQ---LQY 725
Cdd:COG1245 201 GLENILDRDiSELSGGELQRVAIAAALLRDADFYFFDEPSSYLD--IYQRL-NVArlIRELAEEgKYVLVVEHDlaiLDY 277
|
...
gi 1814750642 726 LAD 728
Cdd:COG1245 278 LAD 280
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
664-751 |
3.84e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 664 LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIfNSAIQKHLKSKTVLFITHQLQYLAD-CDEVIFMKEGCITE 742
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVE 242
|
....*....
gi 1814750642 743 RGTHEELMN 751
Cdd:PRK14271 243 EGPTEQLFS 251
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
548-749 |
4.47e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.62 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 548 LGNLRLQRT---LYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQM----SLLEGSIAVNGTFAYVAQQAWILNATLRD 620
Cdd:PRK10418 7 LRNIALQAAqplVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRGRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 621 NilfgkefDEERYNSVLN-------SCCLR---PDLAILPNSdLTEIG----ERGANL-----SGGQRQRISLARALYSD 681
Cdd:PRK10418 87 N-------PRSAFNPLHTmhthareTCLALgkpADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1814750642 682 RDIYILDDPLSALDAHVGNHIFN---SAIQKHlkSKTVLFITHQLQYLADC-DEVIFMKEGCITERGTHEEL 749
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDlleSIVQKR--ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1188-1343 |
4.52e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLG--MAlfrlvelsgGCIK-IDG-VRISDiGLadlrsKLSIIPQEPVL-FSGT 1262
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLriMA---------GVDKeFEGeARPAP-GI-----KVGYLPQEPQLdPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1263 VRSN-----------LDPFNQ----YTE-DQIWDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFSV 1311
Cdd:PRK11819 87 VRENveegvaevkaaLDRFNEiyaaYAEpDADFDALaaEQGELQEIIDAADAwDLDSQLeiaMDalrcpPWDakvtKLSG 166
|
170 180 190
....*....|....*....|....*....|..
gi 1814750642 1312 GERQLLCIARALLRHCKILILDEATAAMDTET 1343
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
560-748 |
5.05e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 560 IDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNG---TFAYVA---------------QQAWILNATLRDN 621
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpiDIRSPRdairagimlcpedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 622 ILFGKefdeeRYNSVLNSCCLRP------------DLAILPNSDLTEIGergaNLSGGQRQRISLARALYSDRDIYILDD 689
Cdd:PRK11288 352 INISA-----RRHHLRAGCLINNrweaenadrfirSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 690 PLSALDAHVGNHIFNSAIQKHLKSKTVLFITHQL-QYLADCDEVIFMKEGCITERGTHEE 748
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1307-1405 |
5.42e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.02 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1307 DNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE---AFaDCTMLTIAHRLHTVLG-SDRIMVLAQG 1382
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqQF-NITSLYVTHDQSEAFAvSDTVIVMNKG 213
|
90 100
....*....|....*....|...
gi 1814750642 1383 QVVEFDTPSVLLSNDSSRFYAMF 1405
Cdd:PRK11432 214 KIMQIGSPQELYRQPASRFMASF 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1193-1342 |
6.99e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1193 SFTIKPKEKIGIVGRTGSGKSSlgmaLFRLveLSG------GCIKIDGVRISDIGlADLRSKLsiipqepvLFSG----- 1261
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTS----LLRI--LAGlarpdaGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 ----TVRSNLDpFNQ-----YTEDQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILIL 1332
Cdd:PRK13538 86 ktelTALENLR-FYQrlhgpGDDEALWEALAQVGLAG-FEDVPVR----------QLSAGQQRRVALARLWLTRAPLWIL 153
|
170
....*....|
gi 1814750642 1333 DEATAAMDTE 1342
Cdd:PRK13538 154 DEPFTAIDKQ 163
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1172-1340 |
7.37e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 46.28 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1172 VTFENAEMRYQENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS------DIgl 1242
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1243 ADLRSKLSIIPQ--EPVLFSGTVRSNL----DPFNQYTEDQIWDALERTHM----KECIAQLPLKLesevmengdnfSVG 1312
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALvgisESLFEKNPFEL-----------SGG 149
|
170 180
....*....|....*....|....*...
gi 1814750642 1313 ERQLLCIARALLRHCKILILDEATAAMD 1340
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
662-721 |
8.60e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.85 E-value: 8.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 662 ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAH-VgnhifnSAIQKHLK--SKTVLFITH 721
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsV------AWLERHLQeyPGTVVAVTH 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1188-1340 |
1.01e-04 |
|
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: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLveLSGGCIKIDG-VRISDIGLADLRSKLsiipQEPVLFSG----- 1261
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTL----LRI--LAGLSPPLAGrVLLNGGPLDFQRDSI----ARGLLYLGhapgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1262 ----TVRSNLDPFNQY-TEDQIWDALERTHMK----ECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILIL 1332
Cdd:cd03231 85 kttlSVLENLRFWHADhSDEQVEEALARVGLNgfedRPVAQL---------------SAGQQRRVALARLLLSGRPLWIL 149
|
....*...
gi 1814750642 1333 DEATAAMD 1340
Cdd:cd03231 150 DEPTTALD 157
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1188-1343 |
1.08e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDgVRISDIGladlrSKLSIIPQEPVlfsgtvrsnL 1267
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFG-----REASLIDAIGR---------K 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1814750642 1268 DPFNQYTEdqiwdALERTHMKEciAQLPLKLESEvmengdnFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1343
Cdd:COG2401 110 GDFKDAVE-----LLNAVGLSD--AVLWLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
898-1099 |
1.13e-04 |
|
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: 45.65 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 898 ALSMAVML--ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFsKDMDEVDVRLPFQAEMFIQN 975
Cdd:cd18566 47 GVVIAILLesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 976 VILVFFCVGMIAgVFPWFLVAV----GPLIILFSIL-HIVSRVLIRELKRLDNITQspflSHITSSIQGLATIHAYKKGQ 1050
Cdd:cd18566 126 LPFVLIFLGLIW-YLGGKLVLVplvlLGLFVLVAILlGPILRRALKERSRADERRQ----NFLIETLTGIHTIKAMAMEP 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1814750642 1051 EFLHRYQELLDNnqrpfflftCAMRWLAVRlDLISIALITTTGLMIVLM 1099
Cdd:cd18566 201 QMLRRYERLQAN---------AAYAGFKVA-KINAVAQTLGQLFSQVSM 239
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1198-1390 |
1.67e-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: 43.52 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1198 PKEKIGIVGRTGSGKSSLGMALFR-LVELSGGCIKIDGVRISDIGLADLRSKLsiipqepvlfsgtvrsnldpfnqyted 1276
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1277 qiwdalerthmkeciaqlplkleseVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR---- 1352
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1814750642 1353 ---EAFADCTMLTIAHRLHTVLgsDRIMVLAQGQVVEFDTP 1390
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1188-1404 |
1.81e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.98 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 1267
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1268 DPFNQYTEDQI---W-----DALERTHMKECIAQLPLklesevmENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1339
Cdd:PRK10253 102 VARGRYPHQPLftrWrkedeEAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1814750642 1340 DT--ETDL--LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND-SSRFYAM 1404
Cdd:PRK10253 175 DIshQIDLleLLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAElIERIYGL 243
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1189-1388 |
2.00e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.08 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKIdgvrISDIgladlrsklsIIPQepvlfSGTVRSN-L 1267
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTT--------------IKM----LTGI----------LVPT-----SGEVRVLgY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1268 DPFNQYTE--DQI-----------WD--ALERTHMKECIAQLP-------LKLESEVMENGD-------NFSVGERQLLC 1318
Cdd:COG4586 85 VPFKRRKEfaRRIgvvfgqrsqlwWDlpAIDSFRLLKAIYRIPdaeykkrLDELVELLDLGElldtpvrQLSLGQRMRCE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 1319 IARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHRLHTV--LgSDRIMVLAQGQVVeFD 1388
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGL----DVVSKEAIREFLKEynrergTTILLTSHDMDDIeaL-CDRVIVIDHGRII-YD 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1188-1412 |
2.46e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.07 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLSIIPQEPVLFSG-TVRSN 1266
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1267 LD-----------PFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEA 1335
Cdd:PRK10851 95 IAfgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1336 TAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENKI 1412
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRL 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1189-1385 |
2.49e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.10 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1189 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD---LRSKLSIIPQEP-VLFSGTVR 1264
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLD-PF---NQYTED---QIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 1337
Cdd:PRK10908 98 DNVAiPLiiaGASGDDirrRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1338 AMDTEtdllIQETIREAFAD-----CTMLTIAHRLHTVLGSD-RIMVLAQGQVV 1385
Cdd:PRK10908 167 NLDDA----LSEGILRLFEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
665-744 |
2.64e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.62 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 665 SGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSA--IQKHLkSKTVLFITHQLQYLADCD-EVIFMKEGCIT 741
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLldLQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIV 543
|
...
gi 1814750642 742 ERG 744
Cdd:PRK10261 544 EIG 546
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1181-1397 |
2.89e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.69 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1181 YQENLPLVLK---KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI--------------KIDGVRISDI--- 1240
Cdd:PRK13651 12 FNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEKVLEKLViqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1241 -------GLADLRSKLSIIPQ--EPVLFSGTVRSNL--DPFNQYTEDQiwDALERThmKECIAQLPLKlESEVMENGDNF 1309
Cdd:PRK13651 92 trfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAKKRA--AKYIELVGLD-ESYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1310 SVGERQLLCIARALLRHCKILILDEATAAMD---TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1385
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGK--TIILVTHDLDNVLEwTKRTIFFKDGKII 244
|
250
....*....|...
gi 1814750642 1386 -EFDTPSVLLSND 1397
Cdd:PRK13651 245 kDGDTYDILSDNK 257
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
911-1061 |
3.75e-04 |
|
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: 44.25 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 911 RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILvffCVGMIAgvf 990
Cdd:cd18590 56 RGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK---TLGMLG--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 991 pwFLVAVGPLIILFSILHIVSRVLI--------RELKR--LDNITQSPFLshITSSIQGLATIHAYKKGQEFLHRYQELL 1060
Cdd:cd18590 130 --FMLSLSWQLTLLTLIEMPLTAIAqkvyntyhQKLSQavQDSIAKAGEL--AREAVSSIRTVRSFKAEEEEACRYSEAL 205
|
.
gi 1814750642 1061 D 1061
Cdd:cd18590 206 E 206
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
249-445 |
4.48e-04 |
|
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: 44.08 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 249 EKSVGELINLCSNDGQRMFEAAAVGSLLAGGPVIAILGMIYNVIILGPTGFLGS-AVFILFYPAMMFVSRITAYFRRKCV 327
Cdd:cd07346 92 RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVAlLLLPLYVLILRYFRRRIRKASREVR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 328 TITDDRVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRMLEKAGYFQSITVGVAPIVMVIASVVTFSV--HMTLGF 405
Cdd:cd07346 172 ESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYggYLVLQG 251
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1814750642 406 DLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 445
Cdd:cd07346 252 SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
879-961 |
4.72e-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: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 879 SVSSSMKDNPLMQYYASIYALSMAVMLILKAIRGVVFVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILN 952
Cdd:cd18574 24 NVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLlsvvgeRVAARLRNDLFSSLLRQDIAFFDTHRTGELVN 103
|
....*....
gi 1814750642 953 RFSKDMDEV 961
Cdd:cd18574 104 RLTADVQEF 112
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
653-728 |
5.35e-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: 43.51 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 653 DLTEIGERG-ANLSGGQRQRISLARALYSDRDIYILDDPLSALDahVGNHIFNSAIQKHLKS--KTVLFITHQ---LQYL 726
Cdd:cd03236 128 ELRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQRLNAARLIRELAEddNYVLVVEHDlavLDYL 205
|
..
gi 1814750642 727 AD 728
Cdd:cd03236 206 SD 207
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
664-749 |
5.66e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 664 LSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIFNSAIQKHLKSKTVL-FITHQLQYLAD-CDEVIFMKEGCIT 741
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALvLITHDLALVAEaAHKIIVMYAGQVV 233
|
....*...
gi 1814750642 742 ERGTHEEL 749
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1188-1387 |
7.88e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1188 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG--GCIKIDGVRISDiglaDLRSKLSIIPQEPVLFSG-TVR 1264
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1265 SNLDPFNQYTEDQIWDALERTHMKE-CIAQLPL-KLESEVMENG--DNFSVGERQLLCIARALLRHCKILILDEATAAMD 1340
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAEsVISELGLtKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1341 TETDL-LIQetireafadcTMLTIAHRLHTVLGS------------DRIMVLAQGQVVEF 1387
Cdd:PLN03211 239 ATAAYrLVL----------TLGSLAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFF 288
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
662-721 |
7.91e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 7.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 662 ANLSGGQRQRISLARALYSDRDIYILDDPLSALDAH-VgnhifnSAIQKHLK--SKTVLFITH 721
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsV------AWLEQFLHdyPGTVVAVTH 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
630-697 |
8.79e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 8.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1814750642 630 EERYNSVLNSCCLRPDLAIlpnsdlteigERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAH 697
Cdd:PLN03073 321 EARAASILAGLSFTPEMQV----------KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
657-749 |
9.46e-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: 43.85 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 657 IGERGANLSGGQRQRISLARALySDRD----IYILDDPLSALDAHVGNHIFNsAIQKhLKSK--TVLFITHQLQYLADCD 730
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKEL-SKRStgrtLYILDEPTTGLHFDDIKKLLE-VLQR-LVDKgnTVVVIEHNLDVIKTAD 899
|
90 100
....*....|....*....|....*
gi 1814750642 731 EVIFM------KEGCITERGTHEEL 749
Cdd:TIGR00630 900 YIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
664-753 |
1.15e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 664 LSGGQRQRISLARALYS---DRDIYILDDPLSAL---DAHVGNHIFNSAI-QKHlkskTVLFITHQLQYLADCDEVIFM- 735
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLThQGH----TVVIIEHNMHVVKVADYVLELg 885
|
90 100
....*....|....*....|...
gi 1814750642 736 -----KEGCITERGTHEELMNLN 753
Cdd:PRK00635 886 peggnLGGYLLASCSPEELIHLH 908
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
909-1026 |
1.29e-03 |
|
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: 42.62 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 909 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDM----DEVDVRLpfqaEMFIQNVILVFFCVG 984
Cdd:cd18780 60 FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTqvlqNAVTVNL----SMLLRYLVQIIGGLV 135
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1814750642 985 MIaGVFPWFLVAVgpLIILFSILHIVSRVLIRELKRLDNITQ 1026
Cdd:cd18780 136 FM-FTTSWKLTLV--MLSVVPPLSIGAVIYGKYVRKLSKKFQ 174
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
905-1063 |
1.43e-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: 42.16 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 905 LILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDmDEVDVRLPFQAEMFIQNVILVFFCVG 984
Cdd:cd18568 56 ILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 985 MIAgVFPWFL--VAVGpLIILFSILHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYKKGQEFLHRYQELLDN 1062
Cdd:cd18568 135 LMF-YYNLQLtlIVLA-FIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAK 212
|
.
gi 1814750642 1063 N 1063
Cdd:cd18568 213 A 213
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
540-749 |
1.79e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 540 EEEGKHTHLGNLRlqrTLYNIDLEIEEGKLVGICGSVGSG--KTSLISSILG---------------QMSLLEGSIAVNG 602
Cdd:NF000106 15 EVRGLVKHFGEVK---AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*Gpdagrrpwrf*twcaNRRALRRTIG*HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 603 TFAYVAQQAWilnaTLRDNI-LFGKEFDEERYNSVLnscclRPDlAILPNSDLTEI-GERGANLSGGQRQRISLARALYS 680
Cdd:NF000106 92 PVR*GRRESF----SGRENLyMIGR*LDLSRKDARA-----RAD-ELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1814750642 681 DRDIYILDDPLSALDAHVGNHIFNSAIQKHLKSKTVLFIThqlQYLADCD----EVIFMKEGCITERGTHEEL 749
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT---QYMEEAEqlahELTVIDRGRVIADGKVDEL 231
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
898-1058 |
2.15e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 41.73 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 898 ALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpFQAEMFI 973
Cdd:cd18564 57 AAALVGIALLRGLasyaGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD---LLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 974 QNVILVFFCVGMIAGVF--PWFL----VAVGPLiILFSILHIVSRvlIRELKRldniTQSPFLSHITS----SIQGLATI 1043
Cdd:cd18564 134 PLLTNLLTLVGMLGVMFwlDWQLaliaLAVAPL-LLLAARRFSRR--IKEASR----EQRRREGALASvaqeSLSAIRVV 206
|
170
....*....|....*
gi 1814750642 1044 HAYKKGQEFLHRYQE 1058
Cdd:cd18564 207 QAFGREEHEERRFAR 221
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
897-1046 |
3.84e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 40.86 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 897 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR-LP-- 966
Cdd:cd18584 39 LLLLLLAALLLRALlawaQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDgyfARyLPql 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 967 FQAeMFIQNVILVF-FCVGMIAGVfpwFLVAVGPLIILFSIL-----HIVSRVLIRELKRLDNitqspflsHITSSIQGL 1040
Cdd:cd18584 119 VLA-AIVPLLILVAvFPLDWVSAL---ILLVTAPLIPLFMILigkaaQAASRRQWAALSRLSG--------HFLDRLRGL 186
|
....*.
gi 1814750642 1041 ATIHAY 1046
Cdd:cd18584 187 PTLKLF 192
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
926-1124 |
4.31e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 40.98 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 926 LHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNViLVFFCVGMIAGVFPWFLVAVG----PLI 1001
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNV-LTLVGVAIILFSINPKLALLTlipiPFL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 1002 ILFSILH-IVSRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYkkGQE------FLHRYQELLDNNQRpfflf 1070
Cdd:cd18778 154 ALGAWLYsKKVRPRYRKVRE--------ALGELNAllqdNLSGIREIQAF--GREeeeakrFEALSRRYRKAQLR----- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1814750642 1071 tcAMRWLAVRLDLISiaLITTTGLMIVLMHGqippayAGLAISYAVQLTGLFQF 1124
Cdd:cd18778 219 --AMKLWAIFHPLME--FLTSLGTVLVLGFG------GRLVLAGELTIGDLVAF 262
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
554-722 |
5.24e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 554 QRTLYNIDLEIEEGKLVGICGSVGSGKTSLISSILGQMSLLEGSIAVNGT---------FAYVAQQAWI-LNATLRDNIL 623
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCninniakpyCTYIGHNLGLkLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 624 FGKEFdeerYNSVLNsccLRPDLAILPNSDLteIGERGANLSGGQRQRISLARALYSDRDIYILDDPLSALDAHVGNHIF 703
Cdd:PRK13541 93 FWSEI----YNSAET---LYAAIHYFKLHDL--LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170
....*....|....*....
gi 1814750642 704 NSAIQKHLKSKTVLFITHQ 722
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSHL 182
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
659-756 |
7.04e-03 |
|
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: 40.77 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1814750642 659 ERGAN-LSGGQRQRISLARALYSDRD--IYILDDP---LSALDahvgNHIFNSAIqKHLKSK--TVLFITHQLQYLADCD 730
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIGSGLTgvLYVLDEPsigLHQRD----NRRLINTL-KRLRDLgnTLIVVEHDEDTIRAAD 557
|
90 100 110
....*....|....*....|....*....|....*.
gi 1814750642 731 EVIFMKE------GCITERGTHEELMN----LNGDY 756
Cdd:TIGR00630 558 YVIDIGPgagehgGEVVASGTPEEILAnpdsLTGQY 593
|
|
| |
